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 1-136 were originally filed September 30, 2022.
The amendment received June 5, 2023 amended claims 2, 9, 11-14, 25, 26, 30, 34, 43-46, 53, and 54 and canceled claims 3-8, 15-24, 28, 29, 31-33, 35-42, 47-52, and 55-136.
Claims 1, 2, 9-14, 25-27, 30, 34, 43-46, 53, and 54 are currently pending.
Claims 1, 2, 13, 14, 53, and 54 are currently under consideration.
Please note: several claims are drawn to more than one “invention”. See claims 13, 14, 25, 26, 27, 30, 34, and 43.
Please note: the scope of several claims is not restricted to the elected product of independent claim 1. Therefore, rejoinder may not be possible.
Please note: applicants should make sure that trademarks are not present in claim 54.
Please note: “preferably” in claim 26 is indefinite.
Please note: printed instructions are not provided patentable weight (see claim 53).
Please note: it is unclear if claim 53 is an improper use claim or not.
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1, 2, 12, 13 (in part), 14 (in part), 53 (in part), and 54 (in part)) in the reply filed on October 14, 2025 is acknowledged.
Claims 9-11, 25-27, 30, 34, and 43-46 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected products and methods, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on October 14, 2025.
Applicant’s election of SEQ ID NO: 16, SEQ ID NO: 16, and a pharmaceutically acceptable carrier, excipient, or diluent in the reply filed on October 14, 2025 is acknowledged. 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: a pharmaceutically acceptable carrier, excipient, or diluent is not a single, specific species.
Please note: SEQ ID NO: 16 is the D-form of SEQ ID NO: 15.
Please note: the elected species of SEQ ID NO: 16 was not found in the prior art. Therefore, the search was extended to additional species.
Claims 12, 53, and 54 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected species, there being no allowable generic or linking claim.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 October 14, 2025.
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/US2021/025280 filed March 31, 2021 which claims the benefit of 63/002,522 filed March 31, 2020.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on June 15, 2023; May 22, 2024; and October 14, 2025 are being considered by the examiner.
Please note: if only the abstract was provided, then only the abstract was considered.
Nucleotide and/or Amino Acid Sequence Disclosures
Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures
37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted:
1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying:
a. the name of the XML file
b. the date of creation; and
c. the size of the XML file in bytes; or
2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying:
a. the name of the XML file;
b. the date of creation; and
c. the size of the XML file in bytes.
SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS:
Specific deficiency - Sequences appearing in the specification are not identified by sequence identifiers (i.e., “SEQ ID NO:X” or the like) in accordance with 37 CFR 1.831(c).
See the abstract and Table 3.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers, consisting of:
• A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
• A copy of the amended specification without markings (clean version); and
• A statement that the substitute specification contains no new matter.
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 page 17, lines 4, 8, and 9; page 18, lines 6 and 11; and page 43, line 35.
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.
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.
Claim Objections
Claim 2 is objected to because of the following informalities: “D-ALA” should read “D-Ala” (the same is true for the other D amino acids in the claim). Appropriate correction is required.
Claim 13 is objected to because of the following informalities: the claim contains nonelected “inventions” (see “a polynucleotide encoding the polypeptide” and “a vector comprising the polynucleotide”). Appropriate correction is required.
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 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.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 2 recites the broad recitation “at least 80%”, and the claim also recites “at least” “85%, 90%, 95%, or 100%” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
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 polypeptide. For example, it is unclear how a polypeptide can have “at least” “100%” identity (e.g. encompassing more than 100% identity).
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 polypeptide. For example, it is unclear what structure is required for a polypeptide with at least 75% identity to any one of SEQ ID NOs: 1-28 to be an “antiviral peptide” or a “polypeptide disrupts the infectivity of a viral pathogen”.
Claim 14 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 polypeptide. For example, it is unclear what structure is required for a polypeptide with at least 75% identity to any one of SEQ ID NOs: 1-28 to be a composition with “low cytotoxicity” and/or if something else is required in the composition to have “low cytotoxicity”.
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 2 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 2 depends on independent claim 1. Independent claim 1 requires the structure of a polypeptide with at least 75% sequence identity to any one of SEQ ID NOs: 1-28. The Markush group for claim 2 includes “b) the polypeptide is an antiviral peptide” (i.e. simply reciting the function of SEQ ID NOs: 1-28); “c) the polypeptide disrupts the infectivity of a viral pathogen” (i.e. simply reciting the function of SEQ ID NOs: 1-28); “d) the polypeptide comprises one or more D-amino acids, one or more L-amino acids, or a mixture” (the sequence listing already designated which amino acids in SEQ ID NOs: 1-28 are L or D); and “e) the polypeptide is 5-34 amino acids long” (i.e. encompassing polypeptides with less than 75% identity to SEQ ID NOs: 1-28). Therefore, claim 2 b)-e) fail to further limit independent claim 1. The Markush members of b) and c) recite the function of SEQ ID NOs: 1-28 and, therefore, do not alter the structure of SEQ ID NOs: 1-28. The Markush member of d) is repetitive based on the designation of L- and D-amino acids in the sequence listing for SEQ ID NOs: 1-28. The Markush member of e) encompasses polypeptides with less than 75% sequence identity as required in independent claim 1 (e.g. 5mer of a 15mer has 33% identity). 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.
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 depends on independent claim 1. Independent claim 1 requires a polypeptide with at least 75% identity with any one of SEQ ID NOs: 1-28. Claim 13 simply changed the preamble to “composition” instead of “polypeptide”. Claim 13 does not add any additional structure and/or components to the composition. Therefore, claim 13 fails to further limit independent clam 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.
Claim 14 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 14 depends on claim 13 which depends on independent claim 1. Independent claim 1 requires a polypeptide with at least 75% identity to any one of SEQ ID NOs: 1-28. The Markush member of “c)” states that the polypeptide is incorporated in the composition. Therefore, the composition simply reiterates that the polypeptide is required. The Markush member of “d)” states that the composition has “low cytotoxicity”. Therefore, it appears that the composition does not alter the polypeptides recited in independent claim 1. The Markush members of “e)” and “f)” simply recites the functions of a polypeptide with at least 75% identity to any one of SEQ ID NOs: 1-28 (e.g. antiviral activity in the presence of serum or a serum component; antiviral activity with an EC50 of less than or equal to 10 mM). Therefore, the functional language does not alter the polypeptides 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.
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, 13, and 14 are rejected under 35 U.S.C. 101 because the claimed invention is directed to fragments of naturally occurring polypeptides without significantly more. The claims recite the polypeptides alone or in a composition wherein the composition further comprises pharmaceutically acceptable carrier, diluent, or excipient and/or a therapeutic agent. This judicial exception is not integrated into a practical application because the present claims are drawn to the product only. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because pharmaceutically acceptable carrier, diluent, or excipient and/or a therapeutic agent are well-understood, routine, and conventional. In addition, there is not a requirement that the pharmaceutically acceptable carrier, diluent, or excipient and/or a therapeutic agent are directly linked.
SEQ ID NO: 2
RESULT 1
A0A8D8D6X9_CULPI
ID A0A8D8D6X9_CULPI Unreviewed; 123 AA.
AC A0A8D8D6X9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 14-DEC-2022, entry version 4.
DE SubName: Full=(northern house mosquito) hypothetical protein {ECO:0000313|EMBL:CAG6506236.1};
OS Culex pipiens (House mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7175 {ECO:0000313|EMBL:CAG6506236.1};
RN [1] {ECO:0000313|EMBL:CAG6506236.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HBUE01152991; CAG6506236.1; -; Transcribed_RNA.
DR EMBL; HBUE01258001; CAG6557541.1; -; Transcribed_RNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 123 AA; 14322 MW; 91D7ECE341965CE8 CRC64;
Query Match 76.5%; Score 63.5; Length 123;
Best Local Similarity 63.6%;
Matches 14; Conservative 0; Mismatches 1; Indels 7; Gaps 1;
Qy 1 RRGWLLLRLLL-------WGRR 15
|||| |||||| ||||
Db 65 RRGWWLLRLLLFRPPRSHWGRR 86
SEQ ID NO: 4
RESULT 1
A0A9I9DK20_CUCME
ID A0A9I9DK20_CUCME Unreviewed; 819 AA.
AC A0A9I9DK20;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 05-FEB-2025, entry version 4.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:MELO3C019519.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|EnsemblPlants:MELO3C019519.2.1};
RN [1] {ECO:0000313|EnsemblPlants:MELO3C019519.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
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DR EnsemblPlants; MELO3C019519.2.1; MELO3C019519.2.1; MELO3C019519.2.
DR Gramene; MELO3C019519.2.1; MELO3C019519.2.1; MELO3C019519.2.
PE 4: Predicted;
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..809
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 91085 MW; 6C00A7E96F5EA637 CRC64;
Query Match 91.0%; Score 61; Length 819;
Best Local Similarity 90.9%;
Matches 10; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 RRGWLRLWGRR 11
|||||| ||||
Db 799 RRGWLRRWGRR 809
SEQ ID NO: 5
RESULT 1
A0A087XNU5_POEFO
ID A0A087XNU5_POEFO Unreviewed; 415 AA.
AC A0A087XNU5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 05-FEB-2025, entry version 37.
DE SubName: Full=Cytohesin 1a {ECO:0000313|Ensembl:ENSPFOP00000007448.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000007448.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000007448.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (OCT-2024) to UniProtKB.
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DR EMBL; AYCK01006524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XNU5; -.
DR Ensembl; ENSPFOT00000007460.1; ENSPFOP00000007448.1; ENSPFOG00000007359.2.
DR GeneTree; ENSGT00940000157519; -.
DR OMA; MEGETYV; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd01252; PH_GRP1-like; 1.
DR CDD; cd00171; Sec7; 1.
DR FunFam; 1.10.1000.11:FF:000002; Cytohesin 1; 1.
DR FunFam; 1.10.220.20:FF:000003; Cytohesin 1; 1.
DR FunFam; 2.30.29.30:FF:000009; Cytohesin 1; 1.
DR Gene3D; 1.10.220.20; -; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663:SF340; CYTOHESIN-1; 1.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 73..260
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 278..394
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT COILED 35..72
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 415 AA; 48354 MW; 009D68230513EA4F CRC64;
Query Match 78.7%; Score 59; Length 415;
Best Local Similarity 75.0%;
Matches 9; Conservative 2; Mismatches 1; Indels 0; Gaps 0;
Qy 1 RRGWLLRLLWGR 12
| ||||:|:|||
Db 281 REGWLLKLVWGR 292
SEQ ID NO: 6
RESULT 1
A0A1M3LYW8_9MICO
ID A0A1M3LYW8_9MICO Unreviewed; 419 AA.
AC A0A1M3LYW8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 05-FEB-2025, entry version 22.
DE SubName: Full=Chloride channel protein {ECO:0000313|EMBL:OJX78146.1};
GN ORFNames=BGO91_09790 {ECO:0000313|EMBL:OJX78146.1};
OS Leifsonia sp. 71-9.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=1895934 {ECO:0000313|EMBL:OJX78146.1, ECO:0000313|Proteomes:UP000184281};
RN [1] {ECO:0000313|EMBL:OJX78146.1, ECO:0000313|Proteomes:UP000184281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-9 {ECO:0000313|EMBL:OJX78146.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OJX78146.1}.
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DR EMBL; MKVJ01000010; OJX78146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3LYW8; -.
DR STRING; 1895934.BGO91_09790; -.
DR Proteomes; UP000184281; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd01033; ClC_like; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; ClC.
DR InterPro; IPR050368; ClC-type_chloride_channel.
DR PANTHER; PTHR43427; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR PANTHER; PTHR43427:SF6; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 4: Predicted;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023173}.
FT TRANSMEM 9..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 419 AA; 42779 MW; 58CD0603684B94D1 CRC64;
Query Match 78.7%; Score 59; Length 419;
Best Local Similarity 90.9%;
Matches 10; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 3 GWLLLRLWGRR 13
|| ||||||||
Db 76 GWWLLRLWGRR 86
SEQ ID NO: 22
RESULT 1
A0A1I8H5P1_9PLAT
ID A0A1I8H5P1_9PLAT Unreviewed; 3183 AA.
AC A0A1I8H5P1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 32.
DE SubName: Full=SAM domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR WBParaSite; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:TreeGrafter.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR Gene3D; 3.10.20.230; Doublecortin domain; 1.
DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR InterPro; IPR043188; DCDC1.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR022136; DUF3668.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR46302; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46302:SF3; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12416; DUF3668; 1.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF89837; Doublecortin (DC); 4.
DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 553..640
FT /note="Phospholipase A2"
FT /evidence="ECO:0000259|Pfam:PF05826"
FT DOMAIN 2274..2436
FT /note="DUF3668"
FT /evidence="ECO:0000259|Pfam:PF12416"
FT REGION 374..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2219..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1651
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2440..2449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3183 AA; 356116 MW; 51676C8634740BE6 CRC64;
Query Match 80.4%; Score 63.5; Length 3183;
Best Local Similarity 93.3%;
Matches 14; Conservative 0; Mismatches 0; Indels 1; Gaps 1;
Qy 1 RRWLLLLRLLLLWRR 15
||||||| |||||||
Db 159 RRWLLLL-LLLLWRR 172
SEQ ID NO: 23
RESULT 1
A0A1I8H5P1_9PLAT
ID A0A1I8H5P1_9PLAT Unreviewed; 3183 AA.
AC A0A1I8H5P1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 32.
DE SubName: Full=SAM domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR WBParaSite; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:TreeGrafter.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR Gene3D; 3.10.20.230; Doublecortin domain; 1.
DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR InterPro; IPR043188; DCDC1.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR022136; DUF3668.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR46302; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46302:SF3; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12416; DUF3668; 1.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF89837; Doublecortin (DC); 4.
DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 553..640
FT /note="Phospholipase A2"
FT /evidence="ECO:0000259|Pfam:PF05826"
FT DOMAIN 2274..2436
FT /note="DUF3668"
FT /evidence="ECO:0000259|Pfam:PF12416"
FT REGION 374..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2219..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1651
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2440..2449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3183 AA; 356116 MW; 51676C8634740BE6 CRC64;
Query Match 79.4%; Score 63.5; Length 3183;
Best Local Similarity 93.3%;
Matches 14; Conservative 0; Mismatches 0; Indels 1; Gaps 1;
Qy 1 RRWLLLLNLLLLWRR 15
||||||| |||||||
Db 159 RRWLLLL-LLLLWRR 172
SEQ ID NO: 27
RESULT 1
K3Y6N1_SETIT
ID K3Y6N1_SETIT Unreviewed; 511 AA.
AC K3Y6N1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 05-FEB-2025, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:KQK97178};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK97178, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQK97178}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK97178};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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DR EMBL; AGNK02004333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3Y6N1; -.
DR EnsemblPlants; KQK97178; KQK97178; SETIT_009872mg.
DR Gramene; KQK97178; KQK97178; SETIT_009872mg.
DR HOGENOM; CLU_533637_0_0_1; -.
DR InParanoid; K3Y6N1; -.
DR Proteomes; UP000004995; Unassembled WGS sequence.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000004995}.
FT REGION 308..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 54181 MW; DF1A38BF2985F39C CRC64;
Query Match 78.4%; Score 58; Length 511;
Best Local Similarity 85.7%;
Matches 12; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 RRWLLLLRLLLLFR 14
||||||| |||||
Db 403 RRWLLLLLFLLLFR 416
SEQ ID NO: 28
RESULT 1
A0A1I8H5P1_9PLAT
ID A0A1I8H5P1_9PLAT Unreviewed; 3183 AA.
AC A0A1I8H5P1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 32.
DE SubName: Full=SAM domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0004382-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR WBParaSite; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5-mRNA-1; maker-uti_cns_0004382-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:TreeGrafter.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR Gene3D; 3.10.20.230; Doublecortin domain; 1.
DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR InterPro; IPR043188; DCDC1.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR022136; DUF3668.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR46302; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46302:SF3; DOUBLECORTIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12416; DUF3668; 1.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF89837; Doublecortin (DC); 4.
DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 553..640
FT /note="Phospholipase A2"
FT /evidence="ECO:0000259|Pfam:PF05826"
FT DOMAIN 2274..2436
FT /note="DUF3668"
FT /evidence="ECO:0000259|Pfam:PF12416"
FT REGION 374..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2219..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2486
FT /note="Disordered"
FT /evidence="ECO: