DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Claims
Claims 1-30 were originally filed May 16, 2023.
The amendment received November 17, 2023 amended claims 2, 5, 9, 14, 16, 19, 24, and 27 and cancelled claims 3, 4, 6, 7, 11, 15, 23, and 28-30.
The amendment received January 20, 2026 changed the status identifiers only.
The amendment received June 25, 2026 amended claims 1, 2, 5, 8-10, 12-14, and 16-21; canceled claims 24-27; and added new claims 31-34.
Please note: the large gap between claims 28 and 29 should be removed.
Claims 1, 2, 5, 8-10, 12-14, 16-22, and 31-34 are currently pending.
Claims 1, 2, 5, 8, 10, 12, and 13 are currently under consideration.
Please note: it is unclear how the attorney of record is of the opinion that the drastic narrowing of the independent claim and some dependent claims in the June 25, 2026 amendment are “not narrowing” or how amendments specifically made to overcome rejections of record were not made “for reasons substantially related to the statutory requirements for patentability”. See page 19, last full paragraph.
Election/Restrictions
Applicants elected, without traverse, Group I (claims 1, 2, 5, 8-10, 12, and 13) in the reply filed on January 20, 2026.
Claims 14, 16-22, and 24-27 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected products and methods, there being no allowable generic or linking claim.
Applicants elected, without traverse, aminopeptidase N, salt solution, feed formulation, treatment, and PirA as the species in the reply filed on January 20, 2026. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Please note: based on the species election, claims 10, 12, and 13 should be withdrawn. However, due to various issues with the claims, the claims are being examined. This does not preclude withdrawal of the claims upon amendment or a requirement for an additional species election.
Claims 9, 14, 16, 17, and 31-34 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on January 20, 2026.
Potential Rejoinder
Applicant elected claims directed to a product. If a product claim is subsequently found allowable, withdrawn process claims that depend from or otherwise include all the limitations of the allowable product claim will be rejoined in accordance with the provisions of MPEP § 821.04. Process claims that depend from or otherwise include all the limitations of the patentable product will be entered as a matter of right if the amendment is presented prior to final rejection or allowance, whichever is earlier. Amendments submitted after final rejection are governed by 37 CFR 1.116; amendments submitted after allowance are governed by 37 CFR 1.312.
In the event of rejoinder, the requirement for restriction between the product claims and the rejoined process claims will be withdrawn, and the rejoined process claims will be fully examined for patentability in accordance with 37 CFR 1.104. Thus, to be allowable, the rejoined claims must meet all the criteria for patentability including the requirements of 35 U.S.C. 101, 102, 103, and 112. Until an elected product claim is found allowable, an otherwise proper restriction requirement between product claims and process claims may be maintained. Withdrawn process claims that are not commensurate in scope with an allowed product claim will not be rejoined. See “Guidance on Treatment of Product and Process Claims in light of In re Ochiai, In re Brouwer and 35 U.S.C. § 103(b),” 1184 O.G. 86 (March 26, 1996). Additionally, in order to retain the right to rejoinder in accordance with the above policy, applicant is advised that the process claims should be amended during prosecution either to maintain dependency on the product claims or to otherwise include the limitations of the product claims. Failure to do so may result in a loss of the right to a rejoinder. Further, note that the prohibition against double patenting rejections of 35 U.S.C. 121 does not apply where the restriction requirement is withdrawn by the examiner before the patent issues. See MPEP § 804.01.
Priority
The present application is a 371 (National Stage) of PCT/US2021/059561 filed November 16, 2021 which claims the benefit of 63/114,383 filed November 16, 2020.
Withdrawn Objections
The objection to claims 1, 2, 5, 8, and 12 regarding “Vibrio spp.” Should read “Vibrio species” to delete the embedded periods in the claims is withdrawn in view of the amendment received June 25, 2026.
The objection to claim 1 regarding “Vibiro spp. toxin” in line 2 should read “Vibrio species toxin” is withdrawn in view of the amendment received June 25, 2026.
The objection to claim 5 regarding a space is missing between “toxins;” and “(c)” is withdrawn in view of the amendment received June 25, 2026.
The objection to claim 13 regarding utilization of the full name along with the first recitation of the acronym is required is withdrawn in view of the amendment received June 25, 2026.
Maintained Objection
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. See paragraphs 40-42, 45-55, 143, 312-314, 317-322, and 329-333.
Arguments and Response
Applicants’ arguments directed to the objection regarding embedded hyperlinks and/or other form of browser-executable code were considered but are not persuasive for the following reasons.
Applicants contend that the amendments received June 25, 2026 negate the objections.
Applicants’ arguments are not convincing since embedded hyperlinks and/or other form of browser-executable code are still present.
The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant’s cooperation is requested in correcting any errors of which applicant may become aware in the specification.
New Objections Necessitated by Amendment
Specification
The amendment filed June 25, 2026 is objected to under 35 U.S.C. 132(a) because it introduces new matter into the disclosure. 35 U.S.C. 132(a) states that no amendment shall introduce new matter into the disclosure of the invention. The added material which is not supported by the original disclosure is as follows: withdrawn claims 17 (dispersed or mixed within the feed carrier; also should be crustacean feed carrier/lack of antecedent basis), 31 (combinations thereof), 33 (complete feed), and 34 (coated; also should be crustacean feed carrier/lack of antecedent basis).
Applicant is required to cancel the new matter in the reply to this Office Action.
Claim Objections
Claim 1 is objected to because of the following informalities: “comprising” should be “comprises”. Appropriate correction is required.
Claim 1 is objected to because of the following informalities: APN should be combined with the full name. Appropriate correction is required.
Claim 1 is objected to because of the following informalities: “APN of binding a Vibiro species PirA toxin or PirB toxin” does not make sense. Appropriate correction is required.
Claim 1 is objected to because of the following informalities: “Vibrio” should read “Vibrio” (see line 4). Appropriate correction is required.
Claim 5 is objected to because of the following informalities: “The Vibrio crustacean feed formulation” should read “The crustacean feed formulation” to correlate with the rest of the claims. Appropriate correction is required.
Claim 8 is objected to because of the following informalities: “SEQ ID NO:” should read “SEQ ID NOs:”. Appropriate correction is required.
Sequence Interpretation
The Office interprets claims comprising SEQ ID NOs: in the following manner: “comprising a sequence of SEQ ID NO: 1” requires only a 2mer of SEQ ID NO: 1, “comprising the sequence of SEQ ID NO: 1” requires the full-length sequence with 100% identity to SEQ ID NO: 1 with any N-/C-terminal additions or any 5’/3’ additions, “consisting of SEQ ID NO: 1” requires the full-length sequence with 100% identity to SEQ ID NO: 1 and the same length as SEQ ID NO: 1, and “selected from the group consisting of SEQ ID NOs: 1, 2, and 3” requires the full-length sequence with 100% identity to SEQ ID NOs: 1, 2, or 3 and the same length as SEQ ID NOs: 1, 2, or 3. Any claim requiring a specific percent identity, necessarily requires at least the recited percent identity.
Withdrawn Rejections
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in view of the amendment received June 25, 2026.
The rejection to claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 2 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 2 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 2 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 5 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 5 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 5 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claim 5 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 8-10, 12, and 13 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 8-10, 12, and 13 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 9 and 10 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 9 and 10 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of the amendment to claim 9 which caused the withdrawal of the claim as being drawn to a nonelected species and the amendment to claim 10 which changed the dependency from claim 9 to claim 1 in the amendment received June 25, 2026.
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 102(a)(1) as being anticipated by Prather et al. WO 2019/210175 published October 31, 2019 is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 102(a)(1) as being anticipated by Alexander-Miller WO 2017/091707 published June 1, 2017 is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 102(a)(1) as being anticipated by Haaning et al. WO 2016/062857 published April 28, 2016 is withdrawn in view of the amendment received June 25, 2026.
The rejection of claims 1, 2, 5, 8-10, 12, and 13 under 35 U.S.C. 102(a)(1) as being anticipated by Kapeller-Libermann et al. WO 01/00811 published January 4, 2001 is withdrawn in view of the amendment received June 25, 2026.
Maintained and/or Modified* Rejections
*wherein the modification is due to amendment
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 5 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claims. For example, it is unclear if the claim is open, closed, etc. (see “is” in line 2).
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(b) as being indefinite for claim 5 were considered but are not persuasive for the following reasons.
Applicants contend that the amendment received June 25, 2026 negates the rejection.
Applicants’ arguments are not convincing since the amendment received June 25, 2026 did not alter “is” at line 2.
Claim 5 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claims. For example, it is unclear how “recombinant” alters the protein.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(b) as being indefinite for claim 5 were considered but are not persuasive for the following reasons.
Applicants contend that the amendment received June 25, 2026 negates the rejection.
Applicants’ arguments are not convincing since the amendment received June 25, 2026 did not alter recombinant or explain how recombinant differentiates the Cry binding region domain of a shrimp APN.
Claims 12 and 13 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claims. For example, it is unclear what is required for the formulation to be effective to treat or prevent an infection, disease, or symptom.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(b) as being indefinite for claim 5 were considered but are not persuasive for the following reasons.
Applicants contend that the amendment received June 25, 2026 negates the rejection.
Applicants’ arguments are not convincing since the amendment received June 25, 2026 did not alter treat or prevent an infection, disease, or a symptom in a shrimp including AHPND.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 5 (a) is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 5 is dependent on independent claim 1. Claim 1 requires a “Vibrio species toxin binding protein”. Claim 5 requires that the protein is “recombinant”. The method of making the protein does not alter the protein structure. Therefore, claim 5 fails to further limit the protein of independent claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(d) as failing to further limit for claim 5 were considered but are not persuasive for the following reasons.
Applicants contend that the amendment added SEQ ID NOs: 2, 4, 6, 8, or 10, a CBR domain, GAMEN motif of SEQ ID NO: 11, and a zinc binding region to claim 5.
Applicants’ arguments are not convincing since the amendment received June 25, 2026 did not alter recombinant in claim 5. Claim 1 was amended to recite a CBR domain of shrimp APN. Claim 2 was amended to recite a GAMEN motif of SEQ ID NO: 11 and a zinc binding region. Claim 8 was amended to recited any one of SEQ ID NOs: 2, 4, 6, 8, or 10. Claim 5 is dependent on claim 1 only, therefore, it is unclear how claims 2 and 8 alter the structure of claim 5.
Claim 10 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 10 is dependent on independent claim 1. Independent claim 1 refers to a crustacean feed formulation comprising a CBR domain of shrimp APN. Dependent claim 10 requires that the feed formulation is for a shrimp. Therefore, dependent claim 10 does not alter the formulation but simply refers to the intended use of the feed formulation. Thus, dependent claim 10 fails to further limit the components of the feed formulation. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(d) as failing to further limit for claim 10 were considered but are not persuasive for the following reasons.
Applicants contend that the shrimp limits the crustacean feed formulation.
Applicants’ arguments are not convincing since the amendment to claim 10 received June 25, 2026 did not alter the crustacean feed formulation.
Claim 12 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 12 is dependent on independent claim 1. Claim 1 requires a “Vibrio species toxin binding protein” comprising a CBR domain of a shrimp APN. Claim 12 simply refers to the intended use of the “Vibrio species toxin binding protein” and crustacean feed carrier. Thus, dependent claim 12 does not alter the structure of the “Vibrio species toxin binding protein” or crustacean feed carrier and fails to further limit independent claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(d) as failing to further limit for claim 12 were considered but are not persuasive for the following reasons.
Applicants contend that the claim refers to specific therapeutic applications.
Applicants’ arguments are not convincing since the therapeutic applications are an intended use for the presently claimed crustacean feed formulation (i.e. not a method).
Claim 13 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 13 is dependent on claim 12 is dependent on independent claim 1. Claim 1 requires a “Vibrio species toxin binding protein” comprising a CBR domain of a shrimp APN. Claim 12 simply refers to the intended use of the “Vibrio species toxin binding protein” and crustacean feed carrier (i.e. treat or prevent an infection, disease, or a symptom) and claim 13 refers to a disease (i.e. AHPND). Thus, dependent claim 13 does not alter the structure of the “Vibrio species toxin binding protein” or crustacean feed carrier and fails to further limit independent claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Arguments and Response
Applicants’ arguments directed to the rejection under 35 USC 112(d) as failing to further limit for claim 13 were considered but are not persuasive for the following reasons.
Applicants contend that the claim refers to specific therapeutic applications.
Applicants’ arguments are not convincing since the therapeutic applications are an intended use for the presently claimed crustacean feed formulation (i.e. not a method).
New Rejections Necessitated by Amendment
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a new matter rejection.
A subgenus of “shrimp” APN was not found in the originally filed specification (see independent claim 1). Only Penaeus vannamei APN of SEQ ID NOs: 1-10 has support in the originally filed specification.
A subgenus of “crustacean feed carrier” was not found in the originally filed specification (see independent claim 1). Only the genus of carrier has support in the originally filed specification.
Zn2+ binding region was not found in the originally filed specification (see dependent claim 2).
In addition, it is applicants responsibility to specifically point out support in the originally filed specification for each and every amendment. Generic statements of “no new matter has been entered”, etc. are not sufficient.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claim. For example, it is unclear if the claims are drawn to a cry binding region (CBR) domain only or to the entire shrimp APN.
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claim. For example, it is unclear what “comprising a Cry binding region (CBR) domain of shrimp APN binding a Vibiro species PirA toxin or PirB toxin” means (i.e. the limitation does not make sense).
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claim. For example, it is unclear what a “crustacean feed carrier” is. This is especially important because the term is not defined in the specification and specific examples are not provided in the specification. Application/Control Number: 18/037,098 Page 20 Art Unit: 1658
Claim 2 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claim. For example, it is unclear what “having” and “according to” require (i.e. open, closed, etc.).
Claim 10 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. One of skill in the art would not be able to determine the scope of the present claim. For example, it is unclear how utilizing the crustacean feed formulation for a shrimp alters the formulation.
Maintained and/or Modified* Rejection
*wherein the modification is due to amendment
Claim Rejections – 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 101 because the claimed invention is directed to “Vibrio species toxin binding protein…comprising a Cry binding region (CBR) domain of shrimp APN” (i.e. aminopeptidase N; fragment of shrimp APN or the full-length APN) without significantly more. The claims recite the polypeptide (CBR domain) in
combination with a carrier. This judicial exception is not integrated into a practical application because the present claims are drawn to a product. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because it is unclear how or if the carrier alters the final structure of the polypeptide (CBR domain) (e.g. how is the carrier associated with the polypeptide, etc.). In addition, carriers are well-understood, routine, and conventional in the art.
See the present specification at paragraph 304 and Figures 16A-16E (i.e. shows SEQ ID NOs: 2, 4, 6, 8, 10, and 11 are naturally occurring). Also refer to the prior art for the specifically disclosed sequences of present dependent claim 8 (i.e. SEQ ID NO: 11 GAMEN of dependent claim 2 is part of the sequences of dependent claim 8).
Present SEQ ID NO: 2
RESULT 1
A0A423ST31_PENVA
ID A0A423ST31_PENVA Unreviewed; 978 AA.
AC A0A423ST31;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=C7M84_014558 {ECO:0000313|EMBL:ROT67356.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67356.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67356.1};
RA Sun Y., Gao Y., Yu Y.;
RT “The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.”;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67356.1}.
CC ---------------------------------------------------------------------------
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DR EMBL; QCYY01002818; ROT67356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423ST31; -.
DR SMR; A0A423ST31; -.
DR STRING; 6689.A0A423ST31; -.
DR OrthoDB; 510539at2759; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 1.25.50.20:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases (‘zincins’), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 34..57
FT /note=”Helical”
FT /evidence=”ECO:0000256|RuleBase:RU364040”
FT DOMAIN 105..297
FT /note=”Aminopeptidase N-like N-terminal”
FT /evidence=”ECO:0000259|Pfam:PF17900”
FT DOMAIN 332..557
FT /note=”Peptidase M1 membrane alanine aminopeptidase”
FT /evidence=”ECO:0000259|Pfam:PF01433”
FT DOMAIN 641..949
FT /note=”ERAP1-like C-terminal”
FT /evidence=”ECO:0000259|Pfam:PF11838”
FT ACT_SITE 405
FT /note=”Proton acceptor”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-1”
FT BINDING 404
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT BINDING 408
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT BINDING 427
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT SITE 490
FT /note=”Transition state stabilizer”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-4”
SQ SEQUENCE 978 AA; 111105 MW; A9D006EDA7794FD8 CRC64;
Query Match 99.8%; Score 5058.5; Length 978;
Best Local Similarity 99.9%;
Matches 959; Conservative 0; Mismatches 0; Indels 1; Gaps 1;
Qy 1 MTGSSRETLAMEMNQSAASVSFGKRNGCYVNRSVAVILGLLFVSATVATGLLVYYYAPQV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MTGSSRETLAMEMNQSAASVSFGKRNGCYVNRSVAVILGLLFVSATVATGLLVYYYAPQV 60
Qy 61 REAGDPLNLARTSLATERPMVPTTPMTPASEVKPKIDVRLPRSVKPLHYKVKLQPLINGN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 REAGDPLNLARTSLATERPMVPTTPMTPASEVKPKIDVRLPRSVKPLHYKVKLQPLINGN 120
Qy 121 FSILGYVEVEVEVLEATSNVTLHIADIVTKNETIKLAPSDQVQGPGIGINKHSYDNERQF 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 FSILGYVEVEVEVLEATSNVTLHIADIVTKNETIKLAPSDQVQGPGIGINKHSYDNERQF 180
Qy 181 YVAELGEELEVGKKYVLSMDFEGYLNDQLHGFYSRLTRRGRSDRLIASTQFQPTDARRAF 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YVAELGEELEVGKKYVLSMDFEGYLNDQLHGFYSRLTRRGRSDRLIASTQFQPTDARRAF 240
Qy 241 PCFDEPGMKATFEVYLGREEGMSSISNMPKFESIPIEGQPGWVWDHFNTSVPMSTYLVAF 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 PCFDEPGMKATFEVYLGREEGMSSISNMPKFESIPIEGQPGWVWDHFNTSVPMSTYLVAF 300
Qy 301 VISDFSHMNSTANDHVLFRVWARKAAIEQANYALTTGPDILTFFEGYFNVPFPLPKQDMI 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 VISDFSHMNSTANDHVLFRVWARKAAIEQANYALTTGPDILTFFEGYFNVPFPLPKQDMI 360
Qy 361 AIPDFSAGAMENWGLITYRETAMLYDPAVSAASNKQRVVVVVAHELAHQWFGNLVTPEWW 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 AIPDFSAGAMENWGLITYRETAMLYDPAVSAASNKQRVVVVVAHELAHQWFGNLVTPEWW 420
Qy 421 TDLWLNEGFASFMEYLGVDHSEPSWKMMEQFVPDDLHDVFAIDCLESSHPISIPVGHPDE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 TDLWLNEGFASFMEYLGVDHSEPSWKMMEQFVPDDLHDVFAIDCLESSHPISIPVGHPDE 480
Qy 481 INEIFDRISYAKGASIIRMMNHFLTEATFRKGLSNYLTDLKYQNAEQDDLWQYLTTAAYE 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 INEIFDRISYAKGASIIRMMNHFLTEATFRKGLSNYLTDLKYQNAEQDDLWQYLTTAAYE 540
Qy 541 DNTLPTDISVKKIMDTWTLQMGYPVIKVTRSSDGTSATVTQERFLLVKNPNSTDTHDYKW 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 DNTLPTDISVKKIMDTWTLQMGYPVIKVTRSSDGTSATVTQERFLLVKNPNSTDTHDYKW 600
Qy 601 WVPLSYTTETSPDFETTKPQRWMMDTEQQLTISSLPAKDKWVIFNVQETGYYRVNYDAEN 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 WVPLSYTTETSPDFETTKPQRWMMDTEQQLTISSLPAKDKWVIFNVQETGYYRVNYDAEN 660
Qy 661 WNLIIQQLKDQHESIHVINRAQII-DVLNLARAGQVSYDTALSVNAYLGKEVEYVPWDTA 719
|||||||||||||||||||||||| |||||||||||||||||||||||||||||||||||
Db 661 WNLIIQQLKDQHESIHVINRAQIIDDVLNLARAGQVSYDTALSVNAYLGKEVEYVPWDTA 720
Qy 720 LNNLGYLENMFTRSSGYGDLKSYLLDILIPLYNSVGFEDNLNDPHLDQYKRVKALSWACN 779
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 LNNLGYLENMFTRSSGYGDLKSYLLDILIPLYNSVGFEDNLNDPHLDQYKRVKALSWACN 780
Qy 780 LGYQDCVDNSQSLFNTWSTVYCTGVAEGGEEEWNFAWEQYINSNVATEKAKLLSAMGCTK 839
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 LGYQDCVDNSQSLFNTWSTVYCTGVAEGGEEEWNFAWEQYINSNVATEKAKLLSAMGCTK 840
Qy 840 EVWILSRYLDMAFTEGSGIRKQDASQVFAAVARNDVGRYLAWNYLRDQWQKIADYYGSGF 899
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 EVWILSRYLDMAFTEGSGIRKQDASQVFAAVARNDVGRYLAWNYLRDQWQKIADYYGSGF 900
Qy 900 FAIA RIIKAATRAFNTKLELAELELFKQQHEGQLGTATRAVDQAIERTENNIKWMDNNYD 959
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 FAIA RIIKAATRAFNTKLELAELELFKQQHEGQLGTATRAVDQAIERTENNIKWMDNNYD 960
For present SEQ ID NO: 4
RESULT 1
A0A3R7NUX0_PENVA
ID A0A3R7NUX0_PENVA Unreviewed; 435 AA.
AC A0A3R7NUX0;
DT 10-APR-2019, integrated into ntry version 17.
DE SubName: Full=Putative aminopeptidase N {ECO:0000313|EMBL:ROT67357.1};
GN ORFNames=C7M84_014559 {ECO:0000313|EMBL:ROT67357.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67357.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBLARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67357.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67357.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67357.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67357.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYY01002818; ROT67357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7NUX0; -.
DR SMR; A0A3R7NUX0; -.
DR OrthoDB; 510539at2759; -.
DR “ Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; ”EA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:TreeGrafter.
DR Gene3D; 1.25.50.20; -; 2.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ROT67357.1};
KW Hydrolase {ECO:0000313|EMBL:ROT67357.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ROT67357.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..359
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 145..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..190
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47363 MW; D09EBEF645DDB144 CRC64;
Query Match 100.0%; Score 2335; Length 435;
Best Local Similarity 100.0%;
Matches 435; Conservative 0; Mismatches 0; Indels ”; Gaps” 0;
Qy 1 MLSATAGYGALRFLYLPSSFLFISSLLLPPLLLLHLTPLFIPLPRSLPSLSRLSTSLSFS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MLSATAGYGALRFLYLPSSFLFISSLLLPPLLLLHLTPLFIPLPRSLPSLSRLSTSLSFS 60
Qy 61 YPSLPLSSSSLPLPYLALTQSSSSSTHHLHLPSALPHLTPPSQPPIPPLTLPPYILTSPL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 YPSLPLSSSSLPLPYLALTQSSSSSTHHLHLPSALPHLTPPSQPPIPPLTLPPYILTSPL 120
Qy 121 PPSISSSLSLLTHLPSHPPSISPRLSFPPLLLPSHPPSPSPHHPPSHPPLPPPHPPRSPP 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 PPSISSSLSLLTHLPSHPPSISPRLSFPPLLLPSHPPSPSPHHPPSHPPLPPPHPPRSPP 180
Qy 181 LILSQLHSTPHPSPHTLPPPSYPPTLTPPSSHSPLAHLPPHPRPPHFHLTPPPYFLPLPA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LILSQLHSTPHPSPHTLPPPSYPPTLTPPSSHSPLAHLPPHPRPPHFHLTPPPYFLPLPA 240
Qy 241 IPLPSPAHSLYNSVGFEDDLQGPHLDQYKRAMALRWTCGLGYVDCVDRSVLQFEEWINNG 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 IPLPSPAHSLYNSVGFEDDLQGPHLDQYKRAMALRWTCGLGYVDCVDRSVLQFEEWINNG 300
Qy 301 SDVSPNLKSTVYCSAIA AGGEEEWGAAWDMYLSANLASEKSVLLSALGCTEEVWLLASYD 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SDVSPNLKSTVYCSAIA AGGEEEWGAAWDMYLSANLASEKSVLLSALGCTEEVWLLASYD 360
Qy 361 TFASLGSLITSATAKFNTREERRQLESFIEENQDSLSSVARSVSQALENTNNNIAWMDSN 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 TFASLGSLITSATAKFNTREERRQLESFIEENQDSLSSVARSVSQALENTNNNIAWMDSN 420
Qy 421 YDVIVQWLNDHGYGQ 435
|||||||||||||||
Db 421 YDVIVQWLNDHGYGQ 435
For present SEQ ID NO: 6
RESULT 1
A0A3R7M511_PENVA
ID A0A3R7M511_PENVA Unreviewed; 690 AA.
AC A0A3R7M511;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-ame: Full=Putative aminopeptidase N-like {ECO:0000313|EMBL:ROT67358.1};
GN ORFNames=C7M84_014560 {ECO:0000313|EMBL:ROT67358.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; costraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67358.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT67358.1, ECO:0000A].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67358.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67358.1, ECO:0000313|Proteomes:U=Muscle {ECO:0000313|EMBL:ROT67358.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molpact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67358.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYY01002818; ROT67358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7M511; -.
DR OrthoDB; 510539at2759; “.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular s”ace; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000016; Glutamyl aminopeptidase; 1.
DR Gene3D; 1.10.3480.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ROT67358.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 294..519
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 572..624
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 224..253
FT ‘ /’ote="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..690
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 366
FT /ligand="Zn(2+)"
FT ” /lig”nd_id="ChEBI:CHEBI:29105"
FT ” /ligand_n”te="catalytic"
FT /evidence="ECO:000025”|PIRSR:PIRSR634016-3"
FT BINDI”G 370
FT ” /ligand="Zn(2+)"
FT ” /ligand_id="ChEBI:CHEBI:29105"
FT ” /ligand_note="catalytic"
FT ” /evidence="ECO:0000256|”IRSR:PIRSR634016-3"
FT ”BINDING 389
FT /ligand="Zn(2+)"
”T /”igand_id="ChEBI:CHEBI:29105"
FT ” /ligand”note="catalytic"
FT /evidence="ECO:00002”6|PIRSR:PI”SR634016-3"
FT SITE ”452
FT /n”te="Transition state stabilizer"
FT /evi”ence="ECO:”000256|PIRSR:PIRSR634016-4"
SQ ”SEQUENCE 690 AA; 76838 M”; 77230FCA1F577276 CRC64;
Query Match 100.”%; Score 36”9; Length 690;
Best Local Sim”larity 100.0%;
Matche” 690; Conservative 0; Mismatches 0; Indels 0;” Gaps 0;
Qy 1 MRWTVAIGGGILAMAVLIGGAVWGYLAKPPPDDLFRLPTDLKPVHYEVRLQPFLSGNFSV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MRWTVAIGGGILAMAVLIGGAVWGYLAKPPPDDLFRLPTDLKPVHYEVRLQPFLSGNFSV 60
Qy 61 LGHVDIELKALTEAYSITLHVADIDINTGTIRVAPPNSTTETGFEILETATDTNLDLFVV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LGHVDIELKALTEAYSITLHVADIDINTGTIRVAPPNSTTETGFEILETATDTNLDLFVV 120
Qy 121 HLKQRLLEGESYILSLDFEGHLNDELRGFYRSSYKDEAGDDRMLAATFFAPAHARRAFPC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 HLKQRLLEGESYILSLDFEGHLNDELRGFYRSSYKDEAGDDRMLAATFFAPAHARRAFPC 180
Qy 181 MDEPALKATFSISLAHEDRLHALSNMPLRDSEPVHPFPHEHLLPKCNLDVQHPPPSSNPR 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 MDEPALKATFSISLAHEDRLHALSNMPLRDSEPVHPFPHEHLLPKCNLDVQHPPPSSNPR 240
Qy 241 PPPSLQRGAGGVGVGPLRDVGAHVHVPRRLRHLGLQEQVGWTWAREAALEQVDYALETGP 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 PPPSLQRGAGGVGVGPLRDVGAHVHVPRRLRHLGLQEQVGWTWAREAALEQVDYALETGP 300
Qy 301 KALSFFEDYFGIPYPLPKEDMVALPDFAPGAMENWGLITYRETAMLYSPEESSASNKQRV 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 KALSFFEDYFGIPYPLPKEDMVALPDFAPGAMENWGLITYRETAMLYSPEESSASNKQRV 360
Qy 361 ATVVVHELAHQWFGNLVTPTWWTDVWLNEGFASFMEYVGTEHVEPSWQMKEQFVVSELQY 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 ATVVVHELAHQWFGNLVTPTWWTDVWLNEGFASFMEYVGTEHVEPSWQMKEQFVVSELQY 420
Qy 421 VFGIDSLESSHPISVPVVNQDQLGEIYDVIAYVKGASIIRMMNYYLGEETFRKGISNYLK 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VFGIDSLESSHPISVPVVNQDQLGEIYDVIAYVKGASIIRMMNYYLGEETFRKGISNYLK 480
Qy 481 AFEYAAADQDDLWQFLTQAAHEDDALAADVTVKDIMDTWTLQTGYPVVKVERDVTGTTAL 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 AFEYAAADQDDLWQFLTQAAHEDDALAADVTVKDIMDTWTLQTGYPVVKVERDVTGTTAL 540
Qy 541 DAPDFTRTRPSAWLTPGTSTLILDGLPSADAWVLLNLQQTGYFRVNYDAGNWELLTKQLA 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 DAPDFTRTRPSAWLTPGTSTLILDGLPSADAWVLLNLQQTGYFRVNYDAGNWELLTKQLA 600
Qy 601 DAHEVIHVTNRAQVMDDALNLARAVNPSSPTTNQLPEPQLTSPFFHKASSPDLAHKPLFL 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 DAHEVIHVTNRAQVMDDALNLARAVNPSSPTTNQLPEPQLTSPFFHKASSPDLAHKPLFL 660
Qy 661 PPPKPPHQPFSLPLSPSQQKLLSPPKASFP 690
||||||||||||||||||||||||||||||
Db 661 PPPKPPHQPFSLPLSPSQQKLLSPPKASFP 690
For present SEQ ID NO: 8
RESULT 1
A0A3R7MI14_PENVA
ID A0A3R7MI14_PENVA Unreviewed; 1107 AA.
AC A0A3R7MI14;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2A:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=C7M84_004249 {ECO:0000313|EMBL:ROT77087.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazmalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT77087.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT77087.1, ECO:C DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT77087.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT77087.1, ECO:0000313|ProteomSSUE=Muscle {ECO:0000313|EMBL:ROT77087.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on gen!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow alyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); XCO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT77087.1}.
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DR EMBL; QCYY01001567; ROT77087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7MI14; -.
DR SMR; A0A3R7MI14; -.
DR STRING; 6689.A0A3R7MI14; -.
DR OrthoDB; 510539at2759; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO“ GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277” F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 1.25.50.20:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ROT77087.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..431
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 468..674
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 758..1078
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..223
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 539
FT ‘ /note’"Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
SQ SEQUENCE 1107 AA; 125669 MW; 21353A65D7181CAC CRC64;
Query Match 99.7%; Score 5826.5; Length 1107;
Best Local Similarity 99.8%;
Matches 1105; Conservative 0; Mismatches 1; Indels 1; Gaps 1;
Qy 1 MHPEAVSLEPCRVGQGRKGRRSGAGRPPALPLPAPSPLSKQTPSRTGRARATGYSRLAQC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MHPEAVSLEPCRVGQGRKGRRSGAGRPPALPLPAPSPLSKQTPSRTGRARATGYSRLAQC 60
Qy 61 RTVSCRVRRCDRRIGREVYNLDGRSASRDQEQGGLAASAAMNNYNTQAATDVV-MDIHQP 119
||||||||||||||||||||||||||||||||||||||||||||||||||||| ||||||
Db 61 RTVSCRVRRCDRRIGREVYNLDGRSASRDQEQGGLAASAAMNNYNTQAATDVVAMDIHQP 120
Qy 120 DHMVSFGKKKGCYISRSVSLLLAVFFLSGMVATGLLVYYYAPHDVEAKAQQETIRYTQAN 179
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 DHMVSFGKKKGCYISRSVSLLLAVFFLSGMVATGLLVYYYAPHDVEAKAQQETIRYTQAN 180
Qy 180 DNTRNVIPEVTKPPKITTTTTTSTTTTTTTKPMPTTTPTTTTTTMAPKEKVNVRLPRSLK 239
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 DNTRNVIPEVTKPPKITTTTTTSTTTTTTTKPMPTTTPTTTTTTMAPKEKVNVRLPRSLK 240
Qy 240 PMHYLVKLQPLINGNFSILGYVEVEMEVLEPTSNITLHIADQITYNDTVKLKGMGNASAP 299
||||||||||||||||||||||||||||||||||||||||| ||||||||||||||||||
Db 241 PMHYLVKLQPLINGNFSILGYVEVEMEVLEPTSNITLHIADIITYNDTVKLKGMGNASAP 300
Qy 300 GIKMHEYDNYREFYIAHLDKELQQGEKYVLSMEFLGYLNDQLRGFYRSSYKDEDGKEKML 359
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 GIKMHEYDNYREFYIAHLDKELQQGEKYVLSMEFLGYLNDQLRGFYRSSYKDEDGKEKML 360
Qy 360 AVTQFQATSARRAFPCFDEPALKATFEVYLGRQENMSSISNMRIMETMPIEGQEGWLWDH 419
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 AVTQFQATSARRAFPCFDEPALKATFEVYLGRQENMSSISNMRIMETMPIEGQEGWLWDH 420
Qy 420 YEESVPMSTYLVAFVVSDFANMNSTVNDHVLFRVWSRQSAIKQAEYSREIGPAILTHFED 479
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 YEESVPMSTYLVAFVVSDFANMNSTVNDHVLFRVWSRQSAIKQAEYSREIGPAILTHFED 480
Qy 480 YFGEPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSGPSNKHRVALVVAHEL 539
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 YFGEPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSGPSNKHRVALVVAHEL 540
Qy 540 AHQWFGNLVTPTWWTDLWLNEGFASFVQYIGMDYVEPSWKVMEEFVISRLQRVFALDSLE 599
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AHQWFGNLVTPTWWTDLWLNEGFASFVQYIGMDYVEPSWKVMEEFVISRLQRVFALDSLE 600
Qy 600 SSHEISIPVGASIIRMMNHFLSENTFRKGVSNYLTAFKYEAAEQDDLWEHLTMAAHEDGT 659
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 SSHEISIPVGASIIRMMNHFLSENTFRKGVSNYLTAFKYEAAEQDDLWEHLTMAAHEDGT 660
Qy 660 LPQDVTVKKVMDTWTLQMGYPVIKVERSADGMSASVSQNRFLLVAKENSSDDHDYKWWVP 719
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 LPQDVTVKKVMDTWTLQMGYPVIKVERSADGMSASVSQNRFLLVAKENSSDDHDYKWWVP 720
Qy 720 LTYTTQSESNFSQTQAMVWMKDSEEQITLSSLPPKDEWVIFNLQETGYYRVNYDDHNWGL 779
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 LTYTTQSESNFSQTQAMVWMKDSEEQITLSSLPPKDEWVIFNLQETGYYRVNYDDHNWGL 780
Qy 780 LIQQLKDDHEVISTTNRAQIIDDAMDLARAGQLNYEIALGVYAYLGNETEYVPWAAAVNN 839
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 LIQQLKDDHEVISTTNRAQIIDDAMDLARAGQLNYEIALGVYAYLGNETEYVPWAAAVNN 840
Qy 840 IGYLEGMFKRKAGYGALKKYILDLVVPLYESVGFTNRHDDPFLEQSKRRTAVSWACMLGH 899
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 IGYLEGMFKRKAGYGALKKYILDLVVPLYESVGFTNRHDDPFLEQSKRRTAVSWACMLGH 900
Qy 900 QDCLDNVLSLYRQWMSNPENETLISPNLKSTVYCRAIA EGGEAEWDFAWDQYLKSNVGTE 959
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 QDCLDNVLSLYRQWMSNPENETLISPNLKSTVYCRAIA EGGEAEWDFAWDQYLKSNVGTE 960
Qy 960 KALLLSAMGCSKEIWILSRYLDMAFTPGSGIRKQDSDRVFASVAYNKVGGPLAWRFLRDQ 1019
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 961 KALLLSAMGCSKEIWILSRYLDMAFTPGSGIRKQDSDRVFASVAYNKVGGPLAWRFLRDQ 1020
Qy 1020 WKRIYDFHGKPKGGLIKSGTSGFNTDLQLKEIELFKQEHEEELGGVSRSVDQVLESTKNS 1079
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1021 WKRIYDFHGKPKGGLIKSGTSGFNTDLQLKEIELFKQEHEEELGGVSRSVDQVLESTKNS 1080
Qy 1080 IAWLDRNYETIVQWLDNNGYSTKLQNE 1106
|||||||||||||||||||||||||||
Db 1081 IAWLDRNYETIVQWLDNNGYSTKLQNE 1107
For present SEQ ID NO: 10
RESULT 1
A0A3R7M3S3_PENVA
ID A0A3R7M3S3_PENVA Unreviewed; 987 AA.
AC A0A3R7M3S3;
DT 10-APR-2019, integrated into Uniy version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=C7M84_009601 {ECO:0000313|EMBL:ROT72064.1};
OS Penaeus vannameioa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT72064.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72064.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ datab509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72064.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:00002500256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMary data.
CC {ECO:0000313|EMBL:ROT72064.1}.
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DR EMBL; QCYY01002214; ROT72064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7M3S3; -.
DR STRING; 6689.A0A3R7M3S3; -.
DR OrthoDB; 510539at2759; -.
C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloami GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 2.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene“A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW ”minopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 128..319
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 359..579
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 663..858
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 859..958
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 512
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 987 AA; 112556 MW; 2EDC7B86C3642F3C CRC64;
Query Match 100.0%; Score 5231; Length 987;
Best Local Similarity 100.0%;
‘ Matche’ 987; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSGSSREVLAMETSHPDHVISFGKKKGCYVSRCVAALLGVFFLSGMVATGLLVYYYAPHI 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSGSSREVLAMETSHPDHVISFGKKKGCYVSRCVAALLGVFFLSGMVATGLLVYYYAPHI 60
Qy 61 RDSQRESLILQKPVVPLHKSLPPPTRRPSATSTTTEALRPTVQPPTTSATAAPAAEALDV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RDSQRESLILQKPVVPLHKSLPPPTRRPSATSTTTEALRPTVQPPTTSATAAPAAEALDV 120
Qy 121 RLPTALRPLHYLIKLQPFINGNFSILGYMEVEMEVLEPTSNITLHIADIITHNDTVTVAA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 RLPTALRPLHYLIKLQPFINGNFSILGYMEVEMEVLEPTSNITLHIADIITHNDTVTVAA 180
Qy 181 SGDSGPSIRIKRHQYDHDRQFYIAQLDQQLEKNKKYVLSMEFLGYLNDQLRGFYRSTYKD 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SGDSGPSIRIKRHQYDHDRQFYIAQLDQQLEKNKKYVLSMEFLGYLNDQLRGFYRSTYKD 240
Qy 241 EDGSDKMLAVTQFQATDARRAFPCFDEPEMKATFEVSLAREENMSSISNMPIKETLPVQN 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 EDGSDKMLAVTQFQATDARRAFPCFDEPEMKATFEVSLAREENMSSISNMPIKETLPVQN 300
Qy 301 QEGWVWDHYHRSVPMSTYLVAFVVSDFANLKSRANENTFFRVWARESAIQQAEYAGQVGP 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 QEGWVWDHYHRSVPMSTYLVAFVVSDFANLKSRANENTFFRVWARESAIQQAEYAGQVGP 360
Qy 361 MILNHFEKYFSMPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSAASNKQYV 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 MILNHFEKYFSMPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSAASNKQYV 420
Qy 421 VAVVAHELAHQWFGNIVTPSWWTDLWLNEGFASYVEYIGINHVEPKWQVMEQFVLREVQE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VAVVAHELAHQWFGNIVTPSWWTDLWLNEGFASYVEYIGINHVEPKWQVMEQFVLREVQE 480
Qy 481 VFGLDCLESSHPISIPVGHPDEIGQIFDRISYGKGASIIRMMNHFLTEVTFRRGLRNYLD 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 VFGLDCLESSHPISIPVGHPDEIGQIFDRISYGKGASIIRMMNHFLTEVTFRRGLRNYLD 540
Qy 541 AFKYSTAEQDDLWEYLTAVAHQDGTLPRGLTVKMIMDTWTLQMGYPVVKVTRGPDGTSAV 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AFKYSTAEQDDLWEYLTAVAHQDGTLPRGLTVKMIMDTWTLQMGYPVVKVTRGPDGTSAV 600
Qy 601 VSQERFLLVRSENSSDTHDYKWWVPLTYTTQSEANFNQTQAMVWMKDSEAQISLSSLPPR 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 VSQERFLLVRSENSSDTHDYKWWVPLTYTTQSEANFNQTQAMVWMKDSEAQISLSSLPPR 660
Qy 661 DQWVIFNLQETGYYRVNYDDHNWGLLIQQLRNDHEVISTINRAQIIDDAMNLAKAGQITY 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 DQWVIFNLQETGYYRVNYDDHNWGLLIQQLRNDHEVISTINRAQIIDDAMNLAKAGQITY 720
Qy 721 ETALSVYTYLSKETEYVPLAAAINNLGYLRSMFVRAGGYGSLRSYLLDILVPLYESVGFE 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 ETALSVYTYLSKETEYVPLAAAINNLGYLRSMFVRAGGYGSLRSYLLDILVPLYESVGFE 780
Qy 781 DSPDDPLLDQYKRTKALSWACLLGHQHCLDSASALYRTWMANPTNDSIISPNLKSTVYCR 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 DSPDDPLLDQYKRTKALSWACLLGHQHCLDSASALYRTWMANPTNDSIISPNLKSTVYCR 840
Qy 841 AIA EGGEAEWNFAWHKYLKYLEMAFTPDSGIRKQDAYRVFGAVAKNVVGRPLAWNYLQNE 900
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 AIA EGGEAEWNFAWHKYLKYLEMAFTPDSGIRKQDAYRVFGAVAKNVVGRPLAWNYLQNE 900
Qy 901 WDKIYDFYGKAKPHFIKYATGGFNTEQHLKEVEHFRKEHEHHLGSASRTVEQVIERTKNN 960
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 WDKIYDFYGKAKPHFIKYATGGFNTEQHLKEVEHFRKEHEHHLGSASRTVEQVIERTKNN 960
Qy 961 IAWMKTNYDVIVKWLDANGYSTKLSTA 987
|||||||||||||||||||||||||||
Db 961 IAWMKTNYDVIVKWLDANGYSTKLSTA 987
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 2, 5, 8, 10, 12, and 13 are rejected under 35 U.S.C. 103 as being unpatentable over Haaning et al. WO 2016/062857 published April 28, 2016 and GenBank submissions for 2018 and 2019.
For present claims 1, 2, 5, 8, 10, 12, and 13, Haaning et al. teach aminopeptidase N and carriers in feed formulations for crustations including shrimp (please refer to the entire specification particularly the abstract; pages 1, 2, 12, 13, 14, 143-157, 159).
Present SEQ ID NO: 2
RESULT 1
A0A423ST31_PENVA
ID A0A423ST31_PENVA Unreviewed; 978 AA.
AC A0A423ST31;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=C7M84_014558 {ECO:0000313|EMBL:ROT67356.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67356.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67356.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67356.1};
RA Sun Y., Gao Y., Yu Y.;
RT “The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.”;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67356.1}.
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DR EMBL; QCYY01002818; ROT67356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423ST31; -.
DR SMR; A0A423ST31; -.
DR STRING; 6689.A0A423ST31; -.
DR OrthoDB; 510539at2759; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 1.25.50.20:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases (‘zincins’), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 34..57
FT /note=”Helical”
FT /evidence=”ECO:0000256|RuleBase:RU364040”
FT DOMAIN 105..297
FT /note=”Aminopeptidase N-like N-terminal”
FT /evidence=”ECO:0000259|Pfam:PF17900”
FT DOMAIN 332..557
FT /note=”Peptidase M1 membrane alanine aminopeptidase”
FT /evidence=”ECO:0000259|Pfam:PF01433”
FT DOMAIN 641..949
FT /note=”ERAP1-like C-terminal”
FT /evidence=”ECO:0000259|Pfam:PF11838”
FT ACT_SITE 405
FT /note=”Proton acceptor”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-1”
FT BINDING 404
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT BINDING 408
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT BINDING 427
FT /ligand=”Zn(2+)”
FT /ligand_id=”ChEBI:CHEBI:29105”
FT /ligand_note=”catalytic”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-3”
FT SITE 490
FT /note=”Transition state stabilizer”
FT /evidence=”ECO:0000256|PIRSR:PIRSR634016-4”
SQ SEQUENCE 978 AA; 111105 MW; A9D006EDA7794FD8 CRC64;
Query Match 99.8%; Score 5058.5; Length 978;
Best Local Similarity 99.9%;
Matches 959; Conservative 0; Mismatches 0; Indels 1; Gaps 1;
Qy 1 MTGSSRETLAMEMNQSAASVSFGKRNGCYVNRSVAVILGLLFVSATVATGLLVYYYAPQV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MTGSSRETLAMEMNQSAASVSFGKRNGCYVNRSVAVILGLLFVSATVATGLLVYYYAPQV 60
Qy 61 REAGDPLNLARTSLATERPMVPTTPMTPASEVKPKIDVRLPRSVKPLHYKVKLQPLINGN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 REAGDPLNLARTSLATERPMVPTTPMTPASEVKPKIDVRLPRSVKPLHYKVKLQPLINGN 120
Qy 121 FSILGYVEVEVEVLEATSNVTLHIADIVTKNETIKLAPSDQVQGPGIGINKHSYDNERQF 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 FSILGYVEVEVEVLEATSNVTLHIADIVTKNETIKLAPSDQVQGPGIGINKHSYDNERQF 180
Qy 181 YVAELGEELEVGKKYVLSMDFEGYLNDQLHGFYSRLTRRGRSDRLIASTQFQPTDARRAF 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YVAELGEELEVGKKYVLSMDFEGYLNDQLHGFYSRLTRRGRSDRLIASTQFQPTDARRAF 240
Qy 241 PCFDEPGMKATFEVYLGREEGMSSISNMPKFESIPIEGQPGWVWDHFNTSVPMSTYLVAF 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 PCFDEPGMKATFEVYLGREEGMSSISNMPKFESIPIEGQPGWVWDHFNTSVPMSTYLVAF 300
Qy 301 VISDFSHMNSTANDHVLFRVWARKAAIEQANYALTTGPDILTFFEGYFNVPFPLPKQDMI 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 VISDFSHMNSTANDHVLFRVWARKAAIEQANYALTTGPDILTFFEGYFNVPFPLPKQDMI 360
Qy* 361 AIPDFSAGAMENWGLITYRETAMLYDPAVSAASNKQRVVVVVAHELAHQWFGNLVTPEWW 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db* 361 AIPDFSAGAMENWGLITYRETAMLYDPAVSAASNKQRVVVVVAHELAHQWFGNLVTPEWW 420
Qy 421 TDLWLNEGFASFMEYLGVDHSEPSWKMMEQFVPDDLHDVFAIDCLESSHPISIPVGHPDE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 TDLWLNEGFASFMEYLGVDHSEPSWKMMEQFVPDDLHDVFAIDCLESSHPISIPVGHPDE 480
Qy 481 INEIFDRISYAKGASIIRMMNHFLTEATFRKGLSNYLTDLKYQNAEQDDLWQYLTTAAYE 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 INEIFDRISYAKGASIIRMMNHFLTEATFRKGLSNYLTDLKYQNAEQDDLWQYLTTAAYE 540
Qy 541 DNTLPTDISVKKIMDTWTLQMGYPVIKVTRSSDGTSATVTQERFLLVKNPNSTDTHDYKW 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 DNTLPTDISVKKIMDTWTLQMGYPVIKVTRSSDGTSATVTQERFLLVKNPNSTDTHDYKW 600
Qy 601 WVPLSYTTETSPDFETTKPQRWMMDTEQQLTISSLPAKDKWVIFNVQETGYYRVNYDAEN 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 WVPLSYTTETSPDFETTKPQRWMMDTEQQLTISSLPAKDKWVIFNVQETGYYRVNYDAEN 660
Qy 661 WNLIIQQLKDQHESIHVINRAQII-DVLNLARAGQVSYDTALSVNAYLGKEVEYVPWDTA 719
|||||||||||||||||||||||| |||||||||||||||||||||||||||||||||||
Db 661 WNLIIQQLKDQHESIHVINRAQIIDDVLNLARAGQVSYDTALSVNAYLGKEVEYVPWDTA 720
Qy 720 LNNLGYLENMFTRSSGYGDLKSYLLDILIPLYNSVGFEDNLNDPHLDQYKRVKALSWACN 779
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 LNNLGYLENMFTRSSGYGDLKSYLLDILIPLYNSVGFEDNLNDPHLDQYKRVKALSWACN 780
Qy 780 LGYQDCVDNSQSLFNTWSTVYCTGVAEGGEEEWNFAWEQYINSNVATEKAKLLSAMGCTK 839
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 LGYQDCVDNSQSLFNTWSTVYCTGVAEGGEEEWNFAWEQYINSNVATEKAKLLSAMGCTK 840
Qy 840 EVWILSRYLDMAFTEGSGIRKQDASQVFAAVARNDVGRYLAWNYLRDQWQKIADYYGSGF 899
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 EVWILSRYLDMAFTEGSGIRKQDASQVFAAVARNDVGRYLAWNYLRDQWQKIADYYGSGF 900
Qy 900 FAIA RIIKAATRAFNTKLELAELELFKQQHEGQLGTATRAVDQAIERTENNIKWMDNNYD 959
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 FAIA RIIKAATRAFNTKLELAELELFKQQHEGQLGTATRAVDQAIERTENNIKWMDNNYD 960
For present SEQ ID NO: 4
RESULT 1
A0A3R7NUX0_PENVA
ID A0A3R7NUX0_PENVA Unreviewed; 435 AA.
AC A0A3R7NUX0;
DT 10-APR-2019, integrated into ntry version 17.
DE SubName: Full=Putative aminopeptidase N {ECO:0000313|EMBL:ROT67357.1};
GN ORFNames=C7M84_014559 {ECO:0000313|EMBL:ROT67357.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67357.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBLARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67357.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67357.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67357.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67357.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYY01002818; ROT67357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7NUX0; -.
DR SMR; A0A3R7NUX0; -.
DR OrthoDB; 510539at2759; -.
DR “ Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; ”EA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:TreeGrafter.
DR Gene3D; 1.25.50.20; -; 2.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ROT67357.1};
KW Hydrolase {ECO:0000313|EMBL:ROT67357.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ROT67357.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..359
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 145..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..190
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47363 MW; D09EBEF645DDB144 CRC64;
Query Match 100.0%; Score 2335; Length 435;
Best Local Similarity 100.0%;
Matches 435; Conservative 0; Mismatches 0; Indels ”; Gaps” 0;
Qy 1 MLSATAGYGALRFLYLPSSFLFISSLLLPPLLLLHLTPLFIPLPRSLPSLSRLSTSLSFS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MLSATAGYGALRFLYLPSSFLFISSLLLPPLLLLHLTPLFIPLPRSLPSLSRLSTSLSFS 60
Qy 61 YPSLPLSSSSLPLPYLALTQSSSSSTHHLHLPSALPHLTPPSQPPIPPLTLPPYILTSPL 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 YPSLPLSSSSLPLPYLALTQSSSSSTHHLHLPSALPHLTPPSQPPIPPLTLPPYILTSPL 120
Qy 121 PPSISSSLSLLTHLPSHPPSISPRLSFPPLLLPSHPPSPSPHHPPSHPPLPPPHPPRSPP 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 PPSISSSLSLLTHLPSHPPSISPRLSFPPLLLPSHPPSPSPHHPPSHPPLPPPHPPRSPP 180
Qy 181 LILSQLHSTPHPSPHTLPPPSYPPTLTPPSSHSPLAHLPPHPRPPHFHLTPPPYFLPLPA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LILSQLHSTPHPSPHTLPPPSYPPTLTPPSSHSPLAHLPPHPRPPHFHLTPPPYFLPLPA 240
Qy 241 IPLPSPAHSLYNSVGFEDDLQGPHLDQYKRAMALRWTCGLGYVDCVDRSVLQFEEWINNG 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 IPLPSPAHSLYNSVGFEDDLQGPHLDQYKRAMALRWTCGLGYVDCVDRSVLQFEEWINNG 300
Qy 301 SDVSPNLKSTVYCSAIA AGGEEEWGAAWDMYLSANLASEKSVLLSALGCTEEVWLLASYD 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SDVSPNLKSTVYCSAIA AGGEEEWGAAWDMYLSANLASEKSVLLSALGCTEEVWLLASYD 360
Qy 361 TFASLGSLITSATAKFNTREERRQLESFIEENQDSLSSVARSVSQALENTNNNIAWMDSN 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 TFASLGSLITSATAKFNTREERRQLESFIEENQDSLSSVARSVSQALENTNNNIAWMDSN 420
Qy 421 YDVIVQWLNDHGYGQ 435
|||||||||||||||
Db 421 YDVIVQWLNDHGYGQ 435
For present SEQ ID NO: 6
RESULT 1
A0A3R7M511_PENVA
ID A0A3R7M511_PENVA Unreviewed; 690 AA.
AC A0A3R7M511;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-ame: Full=Putative aminopeptidase N-like {ECO:0000313|EMBL:ROT67358.1};
GN ORFNames=C7M84_014560 {ECO:0000313|EMBL:ROT67358.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; costraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT67358.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT67358.1, ECO:0000A].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT67358.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT67358.1, ECO:0000313|Proteomes:U=Muscle {ECO:0000313|EMBL:ROT67358.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molpact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT67358.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYY01002818; ROT67358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7M511; -.
DR OrthoDB; 510539at2759; “.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular s”ace; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000016; Glutamyl aminopeptidase; 1.
DR Gene3D; 1.10.3480.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ROT67358.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 294..519
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 572..624
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 224..253
FT ‘ /’ote="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..690
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 366
FT /ligand="Zn(2+)"
FT ” /lig”nd_id="ChEBI:CHEBI:29105"
FT ” /ligand_n”te="catalytic"
FT /evidence="ECO:000025”|PIRSR:PIRSR634016-3"
FT BINDI”G 370
FT ” /ligand="Zn(2+)"
FT ” /ligand_id="ChEBI:CHEBI:29105"
FT ” /ligand_note="catalytic"
FT ” /evidence="ECO:0000256|”IRSR:PIRSR634016-3"
FT ”BINDING 389
FT /ligand="Zn(2+)"
”T /”igand_id="ChEBI:CHEBI:29105"
FT ” /ligand”note="catalytic"
FT /evidence="ECO:00002”6|PIRSR:PI”SR634016-3"
FT SITE ”452
FT /n”te="Transition state stabilizer"
FT /evi”ence="ECO:”000256|PIRSR:PIRSR634016-4"
SQ ”SEQUENCE 690 AA; 76838 M”; 77230FCA1F577276 CRC64;
Query Match 100.”%; Score 36”9; Length 690;
Best Local Sim”larity 100.0%;
Matche” 690; Conservative 0; Mismatches 0; Indels 0;” Gaps 0;
Qy 1 MRWTVAIGGGILAMAVLIGGAVWGYLAKPPPDDLFRLPTDLKPVHYEVRLQPFLSGNFSV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MRWTVAIGGGILAMAVLIGGAVWGYLAKPPPDDLFRLPTDLKPVHYEVRLQPFLSGNFSV 60
Qy 61 LGHVDIELKALTEAYSITLHVADIDINTGTIRVAPPNSTTETGFEILETATDTNLDLFVV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LGHVDIELKALTEAYSITLHVADIDINTGTIRVAPPNSTTETGFEILETATDTNLDLFVV 120
Qy 121 HLKQRLLEGESYILSLDFEGHLNDELRGFYRSSYKDEAGDDRMLAATFFAPAHARRAFPC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 HLKQRLLEGESYILSLDFEGHLNDELRGFYRSSYKDEAGDDRMLAATFFAPAHARRAFPC 180
Qy 181 MDEPALKATFSISLAHEDRLHALSNMPLRDSEPVHPFPHEHLLPKCNLDVQHPPPSSNPR 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 MDEPALKATFSISLAHEDRLHALSNMPLRDSEPVHPFPHEHLLPKCNLDVQHPPPSSNPR 240
Qy 241 PPPSLQRGAGGVGVGPLRDVGAHVHVPRRLRHLGLQEQVGWTWAREAALEQVDYALETGP 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 PPPSLQRGAGGVGVGPLRDVGAHVHVPRRLRHLGLQEQVGWTWAREAALEQVDYALETGP 300
Qy 301 KALSFFEDYFGIPYPLPKEDMVALPDFAPGAMENWGLITYRETAMLYSPEESSASNKQRV 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 KALSFFEDYFGIPYPLPKEDMVALPDFAPGAMENWGLITYRETAMLYSPEESSASNKQRV 360
Qy 361 ATVVVHELAHQWFGNLVTPTWWTDVWLNEGFASFMEYVGTEHVEPSWQMKEQFVVSELQY 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 ATVVVHELAHQWFGNLVTPTWWTDVWLNEGFASFMEYVGTEHVEPSWQMKEQFVVSELQY 420
Qy 421 VFGIDSLESSHPISVPVVNQDQLGEIYDVIAYVKGASIIRMMNYYLGEETFRKGISNYLK 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VFGIDSLESSHPISVPVVNQDQLGEIYDVIAYVKGASIIRMMNYYLGEETFRKGISNYLK 480
Qy 481 AFEYAAADQDDLWQFLTQAAHEDDALAADVTVKDIMDTWTLQTGYPVVKVERDVTGTTAL 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 AFEYAAADQDDLWQFLTQAAHEDDALAADVTVKDIMDTWTLQTGYPVVKVERDVTGTTAL 540
Qy 541 DAPDFTRTRPSAWLTPGTSTLILDGLPSADAWVLLNLQQTGYFRVNYDAGNWELLTKQLA 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 DAPDFTRTRPSAWLTPGTSTLILDGLPSADAWVLLNLQQTGYFRVNYDAGNWELLTKQLA 600
Qy 601 DAHEVIHVTNRAQVMDDALNLARAVNPSSPTTNQLPEPQLTSPFFHKASSPDLAHKPLFL 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 DAHEVIHVTNRAQVMDDALNLARAVNPSSPTTNQLPEPQLTSPFFHKASSPDLAHKPLFL 660
Qy 661 PPPKPPHQPFSLPLSPSQQKLLSPPKASFP 690
||||||||||||||||||||||||||||||
Db 661 PPPKPPHQPFSLPLSPSQQKLLSPPKASFP 690
For present SEQ ID NO: 8
RESULT 1
A0A3R7MI14_PENVA
ID A0A3R7MI14_PENVA Unreviewed; 1107 AA.
AC A0A3R7MI14;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2A:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=C7M84_004249 {ECO:0000313|EMBL:ROT77087.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazmalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT77087.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT77087.1, ECO:C DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT77087.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT77087.1, ECO:0000313|ProteomSSUE=Muscle {ECO:0000313|EMBL:ROT77087.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on gen!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow alyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); XCO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT77087.1}.
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DR EMBL; QCYY01001567; ROT77087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7MI14; -.
DR SMR; A0A3R7MI14; -.
DR STRING; 6689.A0A3R7MI14; -.
DR OrthoDB; 510539at2759; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO“ GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR GO; GO:0042277” F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 1.25.50.20:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ROT77087.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..431
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 468..674
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 758..1078
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..223
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 539
FT ‘ /note’"Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
SQ SEQUENCE 1107 AA; 125669 MW; 21353A65D7181CAC CRC64;
Query Match 99.7%; Score 5826.5; Length 1107;
Best Local Similarity 99.8%;
Matches 1105; Conservative 0; Mismatches 1; Indels 1; Gaps 1;
Qy 1 MHPEAVSLEPCRVGQGRKGRRSGAGRPPALPLPAPSPLSKQTPSRTGRARATGYSRLAQC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MHPEAVSLEPCRVGQGRKGRRSGAGRPPALPLPAPSPLSKQTPSRTGRARATGYSRLAQC 60
Qy 61 RTVSCRVRRCDRRIGREVYNLDGRSASRDQEQGGLAASAAMNNYNTQAATDVV-MDIHQP 119
||||||||||||||||||||||||||||||||||||||||||||||||||||| ||||||
Db 61 RTVSCRVRRCDRRIGREVYNLDGRSASRDQEQGGLAASAAMNNYNTQAATDVVAMDIHQP 120
Qy 120 DHMVSFGKKKGCYISRSVSLLLAVFFLSGMVATGLLVYYYAPHDVEAKAQQETIRYTQAN 179
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 DHMVSFGKKKGCYISRSVSLLLAVFFLSGMVATGLLVYYYAPHDVEAKAQQETIRYTQAN 180
Qy 180 DNTRNVIPEVTKPPKITTTTTTSTTTTTTTKPMPTTTPTTTTTTMAPKEKVNVRLPRSLK 239
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 DNTRNVIPEVTKPPKITTTTTTSTTTTTTTKPMPTTTPTTTTTTMAPKEKVNVRLPRSLK 240
Qy 240 PMHYLVKLQPLINGNFSILGYVEVEMEVLEPTSNITLHIADQITYNDTVKLKGMGNASAP 299
||||||||||||||||||||||||||||||||||||||||| ||||||||||||||||||
Db 241 PMHYLVKLQPLINGNFSILGYVEVEMEVLEPTSNITLHIADIITYNDTVKLKGMGNASAP 300
Qy 300 GIKMHEYDNYREFYIAHLDKELQQGEKYVLSMEFLGYLNDQLRGFYRSSYKDEDGKEKML 359
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 GIKMHEYDNYREFYIAHLDKELQQGEKYVLSMEFLGYLNDQLRGFYRSSYKDEDGKEKML 360
Qy 360 AVTQFQATSARRAFPCFDEPALKATFEVYLGRQENMSSISNMRIMETMPIEGQEGWLWDH 419
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 AVTQFQATSARRAFPCFDEPALKATFEVYLGRQENMSSISNMRIMETMPIEGQEGWLWDH 420
Qy 420 YEESVPMSTYLVAFVVSDFANMNSTVNDHVLFRVWSRQSAIKQAEYSREIGPAILTHFED 479
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 YEESVPMSTYLVAFVVSDFANMNSTVNDHVLFRVWSRQSAIKQAEYSREIGPAILTHFED 480
Qy 480 YFGEPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSGPSNKHRVALVVAHEL 539
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 YFGEPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSGPSNKHRVALVVAHEL 540
Qy 540 AHQWFGNLVTPTWWTDLWLNEGFASFVQYIGMDYVEPSWKVMEEFVISRLQRVFALDSLE 599
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AHQWFGNLVTPTWWTDLWLNEGFASFVQYIGMDYVEPSWKVMEEFVISRLQRVFALDSLE 600
Qy 600 SSHEISIPVGASIIRMMNHFLSENTFRKGVSNYLTAFKYEAAEQDDLWEHLTMAAHEDGT 659
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 SSHEISIPVGASIIRMMNHFLSENTFRKGVSNYLTAFKYEAAEQDDLWEHLTMAAHEDGT 660
Qy 660 LPQDVTVKKVMDTWTLQMGYPVIKVERSADGMSASVSQNRFLLVAKENSSDDHDYKWWVP 719
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 LPQDVTVKKVMDTWTLQMGYPVIKVERSADGMSASVSQNRFLLVAKENSSDDHDYKWWVP 720
Qy 720 LTYTTQSESNFSQTQAMVWMKDSEEQITLSSLPPKDEWVIFNLQETGYYRVNYDDHNWGL 779
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 LTYTTQSESNFSQTQAMVWMKDSEEQITLSSLPPKDEWVIFNLQETGYYRVNYDDHNWGL 780
Qy 780 LIQQLKDDHEVISTTNRAQIIDDAMDLARAGQLNYEIALGVYAYLGNETEYVPWAAAVNN 839
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 LIQQLKDDHEVISTTNRAQIIDDAMDLARAGQLNYEIALGVYAYLGNETEYVPWAAAVNN 840
Qy 840 IGYLEGMFKRKAGYGALKKYILDLVVPLYESVGFTNRHDDPFLEQSKRRTAVSWACMLGH 899
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 IGYLEGMFKRKAGYGALKKYILDLVVPLYESVGFTNRHDDPFLEQSKRRTAVSWACMLGH 900
Qy 900 QDCLDNVLSLYRQWMSNPENETLISPNLKSTVYCRAIA EGGEAEWDFAWDQYLKSNVGTE 959
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 QDCLDNVLSLYRQWMSNPENETLISPNLKSTVYCRAIA EGGEAEWDFAWDQYLKSNVGTE 960
Qy 960 KALLLSAMGCSKEIWILSRYLDMAFTPGSGIRKQDSDRVFASVAYNKVGGPLAWRFLRDQ 1019
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 961 KALLLSAMGCSKEIWILSRYLDMAFTPGSGIRKQDSDRVFASVAYNKVGGPLAWRFLRDQ 1020
Qy 1020 WKRIYDFHGKPKGGLIKSGTSGFNTDLQLKEIELFKQEHEEELGGVSRSVDQVLESTKNS 1079
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1021 WKRIYDFHGKPKGGLIKSGTSGFNTDLQLKEIELFKQEHEEELGGVSRSVDQVLESTKNS 1080
Qy 1080 IAWLDRNYETIVQWLDNNGYSTKLQNE 1106
|||||||||||||||||||||||||||
Db 1081 IAWLDRNYETIVQWLDNNGYSTKLQNE 1107
For present SEQ ID NO: 10
RESULT 1
A0A3R7M3S3_PENVA
ID A0A3R7M3S3_PENVA Unreviewed; 987 AA.
AC A0A3R7M3S3;
DT 10-APR-2019, integrated into Uniy version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=C7M84_009601 {ECO:0000313|EMBL:ROT72064.1};
OS Penaeus vannameioa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT72064.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72064.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ datab509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72064.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:00002500256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMary data.
CC {ECO:0000313|EMBL:ROT72064.1}.
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CC Distri----------------------------------------------------------------------
DR EMBL; QCYY01002214; ROT72064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7M3S3; -.
DR STRING; 6689.A0A3R7M3S3; -.
DR OrthoDB; 510539at2759; -.
C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloami GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR FunFam; 1.10.390.10:FF:000001; Aminopeptidase; 1.
DR FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR FunFam; 2.60.40.1730:FF:000012; Aminopeptidase N; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF294; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 2.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene“A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW ”minopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 128..319
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 359..579
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 663..858
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 859..958
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 512
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 987 AA; 112556 MW; 2EDC7B86C3642F3C CRC64;
Query Match 100.0%; Score 5231; Length 987;
Best Local Similarity 100.0%;
‘ Matche’ 987; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSGSSREVLAMETSHPDHVISFGKKKGCYVSRCVAALLGVFFLSGMVATGLLVYYYAPHI 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSGSSREVLAMETSHPDHVISFGKKKGCYVSRCVAALLGVFFLSGMVATGLLVYYYAPHI 60
Qy 61 RDSQRESLILQKPVVPLHKSLPPPTRRPSATSTTTEALRPTVQPPTTSATAAPAAEALDV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RDSQRESLILQKPVVPLHKSLPPPTRRPSATSTTTEALRPTVQPPTTSATAAPAAEALDV 120
Qy 121 RLPTALRPLHYLIKLQPFINGNFSILGYMEVEMEVLEPTSNITLHIADIITHNDTVTVAA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 RLPTALRPLHYLIKLQPFINGNFSILGYMEVEMEVLEPTSNITLHIADIITHNDTVTVAA 180
Qy 181 SGDSGPSIRIKRHQYDHDRQFYIAQLDQQLEKNKKYVLSMEFLGYLNDQLRGFYRSTYKD 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SGDSGPSIRIKRHQYDHDRQFYIAQLDQQLEKNKKYVLSMEFLGYLNDQLRGFYRSTYKD 240
Qy 241 EDGSDKMLAVTQFQATDARRAFPCFDEPEMKATFEVSLAREENMSSISNMPIKETLPVQN 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 EDGSDKMLAVTQFQATDARRAFPCFDEPEMKATFEVSLAREENMSSISNMPIKETLPVQN 300
Qy 301 QEGWVWDHYHRSVPMSTYLVAFVVSDFANLKSRANENTFFRVWARESAIQQAEYAGQVGP 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 QEGWVWDHYHRSVPMSTYLVAFVVSDFANLKSRANENTFFRVWARESAIQQAEYAGQVGP 360
Qy 361 MILNHFEKYFSMPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSAASNKQYV 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 MILNHFEKYFSMPYPLPKQDMIAIPDFSAGAMENWGLITYRETAMLYDPVVSAASNKQYV 420
Qy 421 VAVVAHELAHQWFGNIVTPSWWTDLWLNEGFASYVEYIGINHVEPKWQVMEQFVLREVQE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VAVVAHELAHQWFGNIVTPSWWTDLWLNEGFASYVEYIGINHVEPKWQVMEQFVLREVQE 480
Qy 481 VFGLDCLESSHPISIPVGHPDEIGQIFDRISYGKGASIIRMMNHFLTEVTFRRGLRNYLD 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 VFGLDCLESSHPISIPVGHPDEIGQIFDRISYGKGASIIRMMNHFLTEVTFRRGLRNYLD 540
Qy 541 AFKYSTAEQDDLWEYLTAVAHQDGTLPRGLTVKMIMDTWTLQMGYPVVKVTRGPDGTSAV 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AFKYSTAEQDDLWEYLTAVAHQDGTLPRGLTVKMIMDTWTLQMGYPVVKVTRGPDGTSAV 600
Qy 601 VSQERFLLVRSENSSDTHDYKWWVPLTYTTQSEANFNQTQAMVWMKDSEAQISLSSLPPR 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 VSQERFLLVRSENSSDTHDYKWWVPLTYTTQSEANFNQTQAMVWMKDSEAQISLSSLPPR 660
Qy 661 DQWVIFNLQETGYYRVNYDDHNWGLLIQQLRNDHEVISTINRAQIIDDAMNLAKAGQITY 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 DQWVIFNLQETGYYRVNYDDHNWGLLIQQLRNDHEVISTINRAQIIDDAMNLAKAGQITY 720
Qy 721 ETALSVYTYLSKETEYVPLAAAINNLGYLRSMFVRAGGYGSLRSYLLDILVPLYESVGFE 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 ETALSVYTYLSKETEYVPLAAAINNLGYLRSMFVRAGGYGSLRSYLLDILVPLYESVGFE 780
Qy 781 DSPDDPLLDQYKRTKALSWACLLGHQHCLDSASALYRTWMANPTNDSIISPNLKSTVYCR 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 DSPDDPLLDQYKRTKALSWACLLGHQHCLDSASALYRTWMANPTNDSIISPNLKSTVYCR 840
Qy 841 AIA EGGEAEWNFAWHKYLKYLEMAFTPDSGIRKQDAYRVFGAVAKNVVGRPLAWNYLQNE 900
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 AIA EGGEAEWNFAWHKYLKYLEMAFTPDSGIRKQDAYRVFGAVAKNVVGRPLAWNYLQNE 900
Qy 901 WDKIYDFYGKAKPHFIKYATGGFNTEQHLKEVEHFRKEHEHHLGSASRTVEQVIERTKNN 960
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 WDKIYDFYGKAKPHFIKYATGGFNTEQHLKEVEHFRKEHEHHLGSASRTVEQVIERTKNN 960
Qy 961 IAWMKTNYDVIVKWLDANGYSTKLSTA 987
|||||||||||||||||||||||||||
Db 961 IAWMKTNYDVIVKWLDANGYSTKLSTA 987
All the claimed elements (APN; APN with a specific sequence) were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in the respective functions and the combination would have yielded predictable results (APN activity in a crustacean feed formulation) to one of ordinary skill in the art at the time of the invention. The claims would have been obvious because the substitution of one known element (APN) for another (APN) of a specific seqeucne would have yielded predictable results ()specific APN in a crustacean feed formulation to one of ordinary skill in the art at the time of the invention. The claims would have been obvious because a particular known technique (adding APN to a crustacean feed formulation) was recognized as part of the ordinary capabilities of one skilled in the art. The claims would have been obvious because a person of ordinary skill has good reason to pursue the known options within their technical grasp. If this leads to the anticipated success, it is likely the product no of innovation but of ordinary skill and common sense. See KSR International Co v. Teleflex Inc., 82 USPQ2d 1385 (U.S. 2007).
Conclusion
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Lin et al., 2019, Structural Insights to the Heterotetrameric Interaction between the Vibrioparahaemolyticus PirAvp and PirBvp Toxins and Activation of the Cry-Like Pore-Forming Domain, Toxins, 11: 233 (15 pages).
Cuzon et al., 1994, Composition, preparation and utilization of feeds for Crustacea, Aquaculture, 124: 253-267.
Jeffs et al., 2020, Feeding and Nutrition of Crustacean Larvae, Developmental Biology and Larval Ecology, Volume 7, Anger et al. (eds), Volume 7, pages 309-331.
Encarnacao, 2016, Functional feed additives in aquaculture feeds, Aquafeed Formulation, 217-237.
WO 2013/189972
WO 2013/110766
CN 101816380
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/AMBER D STEELE/Primary Examiner, Art Unit 1658
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