DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1, 6, 8-11, 17-21, 23, 26, 27, and 31 are pending in the application.
Applicant’s preliminary amendment to the claims, filed January 13, 2026, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Restriction/Election
Applicant’s election without traverse of Group I, claims 1, 26, 27, and 31, in the reply filed on January 13, 2026 is acknowledged.
Claims 6, 8-11, 17-21, and 23 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international application PCT/US2021/063768, filed December 16, 2021, which claims foreign priority under 35 U.S.C. 119(a)-(d) to Chinese application PCT/CN2020/136710, filed December 16, 2020. A certified copy of the foreign priority document has been filed in this application on June 14, 2023.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on January 14, 2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS has been considered by the examiner.
Drawings
According to 37 CFR 1.84(u):
(u) Numbering of views.
(1) The different views must be numbered in consecutive Arabic numerals, starting with 1, independent of the numbering of the sheets and, if possible, in the order in which they appear on the drawing sheet(s). Partial views intended to form one complete view, on one or several sheets, must be identified by the same number followed by a capital letter. View numbers must be preceded by the abbreviation "FIG." Where only a single view is used in an application to illustrate the claimed invention, it must not be numbered and the abbreviation "FIG." must not appear.
(2) Numbers and letters identifying the views must be simple and clear and must not be used in association with brackets, circles, or inverted commas. The view numbers must be larger than the numbers used for reference characters.
The drawings filed June 14, 2023 are objected to because the view numbers are preceded by “Figure,” however, view numbers must be preceded by the abbreviation "FIG." Appropriate correction is required.
Figure 4 of the drawings filed June 14, 2023, which shows the amino acid sequence of SEQ ID NO: 1 of the sequence listing XML file, is objected to because sequences that are included in the "Sequence Listing XML" should not be duplicated in the drawings. See MPEP 2412.06.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Objections
Claim 1 is objected to in the recitation of “isolated polypeptide or active fragment thereof having lysozyme activity” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “isolated polypeptide having lysozyme activity or an enzymatically active fragment thereof.”
Claim Rejections - 35 USC § 112(b)
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.
Claims 27 and 31 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claim 27 (claim 31 dependent therefrom) is indefinite in the recitation of “(iii) optionally, at least one additional polypeptide…and (iv) a surfactant” because it is unclear as to whether the term “optionally” is intended to apply only to the component (iii) or is intended to apply to both the components (iii) and (iv). If applicant intends for the term “optionally” to apply only to the component (iii), it is suggested that the phrase “(iii) optionally, at least one additional polypeptide…and (iv) a surfactant” be amended to recite “(iii) a surfactant; and (iv) optionally, at least one additional polypeptide…”
Claim Rejections - 35 USC § 112(a)
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.
Claims 1, 26, 27, and 31 are rejected under 35 U.S.C. 112(a) 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 at the time the application was filed, had possession of the claimed invention.
MPEP 2163.II.A.2.(a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention”.
For claims drawn to a genus, MPEP § 2163 states the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
According to MPEP 2163.II.A.3.(a).ii), [s]atisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’"
The factors considered in the Written Description requirement are (1) level of skill and knowledge in the art, (2) partial structure, (3) physical and/or chemical properties, (4) functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the (5) method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient." MPEP § 2163.
Claim 1 is drawn to a genus of isolated polypeptides or active fragments thereof having lysozyme activity, wherein the polypeptide has at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1.
Claim 26 (claims 27 and 31 dependent therefrom) is drawn to a detergent composition comprising a genus of polypeptides having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity.
Given that the genus of recited polypeptides includes species having amino acid modifications of up to 40% of the amino acids of SEQ ID NO: 1, the genus is considered to encompass polypeptides with widely variant amino acid sequences.
The specification discloses the following single representative species of the genus of recited polypeptides – a polypeptide comprising the amino acid sequence of SEQ ID NO: 1.
Regarding the level of skill and knowledge in the art of amino acid modification, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached Form PTO-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see p. 7, column 1, top). The unpredictability associated with amino acid modification is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892), which discloses that even a mutation that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1). In view of Singh et al. and Zhang et al., one of skill in the art would recognize a high level of unpredictability in the art of amino acid modification.
Given that the specification discloses only a single representative species of a widely variant genus of polypeptides, and there is a high level of unpredictability in the art of amino acid modification, the single disclosed representative species is considered to be insufficient to describe the widely variant genus. One of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the recited genus. The claimed subject matter is not supported by an adequate written description because a representative number of species has not been described.
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, 26, 27, and 31 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Applicant’s attention is directed to the "Guidance for Determining Subject Matter Eligibility Of Claims Reciting Or Involving Laws of Nature, Natural Phenomena, & Natural Products”, released on December 16, 2014.
Claim 1
Claim Interpretation: Claim 1 is drawn to an isolated polypeptide or active fragment thereof having lysozyme activity, wherein the polypeptide has at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1.
UniProt Database Accession Number A4Z8Q1 (December 11, 2019, 2 pages; cited on the attached Form PTO-892) discloses a lysozyme from Bubalus bubalis, i.e., domestic water buffalo, with an amino acid sequence that is identical to instant SEQ ID NO: 1 (see attached Appendix A for sequence alignment).
Given a broadest reasonable interpretation, claim 1 encompasses a naturally-occurring lysozyme.
Patent Eligibility Analysis Step 1: The claim is drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claim recites a naturally occurring polypeptide, which is considered to be a law of nature or a natural phenomenon (a natural product). The polypeptide of claim 1 is not considered to have markedly different characteristics from what occurs in nature, and is considered to be a “product of nature” exception. Accordingly, the polypeptide of claim 1 is directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claims beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claim only recites the product of nature, without more and does not include any additional elements that could add significantly more to the judicial exception.
Claim 26
Claim Interpretation: Claim 26 is drawn to a detergent composition comprising a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity.
The specification describes “detergent composition” as a composition intended for use in a wash medium (e.g. a wash liquor) for the cleaning of soiled or dirty objects, including particular textile or non-textile objects or items (paragraph [0087]).
The recitation of “detergent composition” in the preamble of claim 26 is interpreted as intended use or purpose of the claimed composition and does not further limit the structure and/or function of the claimed composition.
The only required component of the composition of claim 26 is a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity.
As stated above, UniProt Database Accession Number A4Z8Q1 (December 11, 2019, 2 pages; cited on the attached Form PTO-892) discloses a lysozyme from Bubalus bubalis, i.e., water buffalo with an amino acid sequence that is identical to instant SEQ ID NO: 1 (see attached Appendix A for sequence alignment).
Given a broadest reasonable interpretation, the polypeptide of the composition of claim 26 encompasses a naturally-occurring lysozyme and the detergent composition of claim 26 encompasses a naturally-occurring composition.
Patent Eligibility Analysis Step 1: The claim is drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claim recites a naturally-occurring composition, which is considered to be a law of nature or a natural phenomenon (a natural product). The composition of claim 26 is not considered to have markedly different characteristics from what occurs in nature, and is considered to be a “product of nature” exception. Accordingly, the composition of claim 26 is directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claims beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claim only recites the product of nature, without more and does not include any additional elements that could add significantly more to the judicial exception.
Claims 27 and 31
Claim Interpretation: Claims 27 and 31 are drawn to a detergent composition comprising a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity, and a polypeptide having protease activity.
The only required components of the composition of claims 27 and 31 are a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity and a polypeptide having protease activity.
As stated above, UniProt Database Accession Number A4Z8Q1 (December 11, 2019, 2 pages; cited on the attached Form PTO-892) discloses a lysozyme from Bubalus bubalis, i.e., water buffalo with an amino acid sequence that is identical to instant SEQ ID NO: 1 (see attached Appendix A for sequence alignment).
Given a broadest reasonable interpretation, the polypeptides of the composition of claims 27 and 31 encompass a naturally-occurring lysozyme and a naturally-occurring protease and the detergent composition of claims 27 and 31 encompasses a composition of naturally-occurring polypeptides.
Patent Eligibility Analysis Step 1: The claims are drawn to a composition of matter, which is one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claims recite a composition comprising a combination of naturally occurring components, which is considered to be a law of nature or a natural phenomenon (a natural product). There is no evidence of record of a naturally occurring counterpart to the claimed composition, so the composition is compared to the individual components as they occur in nature (see MPEP 2106.04(c).II.A). There is no indication in the specification or evidence of record that the individual components have any characteristics (structural, functional, or otherwise) that are different from the corresponding individual components as each occurs in nature. Furthermore, there is no indication in the specification or evidence of record that combining these components changes the structure, function, or other properties of the naturally occurring components. In other words, the overall combination of polypeptides does not render the resulting composition different from each of the individual polypeptides. Thus, the detergent composition of claims 27 and 31 is not considered to have markedly different characteristics from what occurs in nature, and is considered to be a “product of nature” exception. Accordingly, the detergent composition of claims 27 and 31 is directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claims beyond the judicial exception.
Patent Eligibility Analysis Step 2B: The claims only recite the products of nature, without more and do not include any additional elements that could add significantly more to the judicial exception.
As such, the claims do not qualify as eligible subject matter. For these reasons the claim is rejected under section 101 as being directed to non-statutory subject matter.
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.
Claim 1 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt Database Accession Number A4Z8Q1 (December 11, 2019, 2 pages; cited on the attached Form PTO-892; hereafter “UniProt A4Z8Q1”) in view of Hussain et al. (International Journal of Food Properties 18:1288-1297, 2015; cited on the attached Form PTO-892; hereafter “Hussain”).
Claim 1 is drawn to an isolated polypeptide or active fragment thereof having lysozyme activity, wherein the polypeptide has at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1.
UniProt A4Z8Q1 teaches a buffalo (Bubalus bubalis) lysozyme from mammary gland tissue (p. 1, top). The amino acid sequence disclosed by UniProt A4Z8Q1 is identical to instant SEQ ID NO: 1 (see Appendix A sequence alignment).
UniProt A4Z8Q1 does not teach isolating the buffalo lysozyme.
Hussain teaches lysozyme is a commercially valuable enzyme applied in foods and drugs (p. 1288, Abstract) and teaches there has been increasing demand for lysozyme due to its potent antimicrobial activity against a wide range of microorganisms (p. 1289, bottom). Hussain teaches a method for isolating buffalo milk lysozyme (p. 1288, Abstract; p. 1291, top).
In view of the combined teachings of UniProt A4Z8Q1 and Hussain, it would have been obvious to one of ordinary skill in the art before the effective filing date to isolate the buffalo lysozyme of UniProt A4Z8Q1. One would have been motivated to isolate the buffalo lysozyme of UniProt A4Z8Q1 because Hussain taught lysozyme is a commercially valuable enzyme applied in foods and drugs and teaches there has been increasing demand for lysozyme due to its potent antimicrobial activity against a wide range of microorganisms. One would have expected success because UniProt A4Z8Q1 taught a buffalo lysozyme from mammary gland tissue and Hussain taught a method for isolating a buffalo milk lysozyme. Therefore, the isolated polypeptide of claim 1 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 26, 27, and 31 are rejected under 35 U.S.C. 103 as being unpatentable over Carpenter et al. (U.S. Patent No. 5,041,236; cited on the attached Form PTO-892; hereafter “Carpenter”) in view of UniProt Database Accession Number A0A0C5AGQ3 (December 11, 2019, 2 pages; cited on the attached Form PTO-892; hereafter “UniProt A0A0C5AGQ3”).
Claims 26, 27, and 31 are drawn to a detergent composition comprising a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity.
Carpenter teaches an antimicrobial composition comprising a ruminant stomach lysozyme (column 6, lines 52-53) with ruminant stomach lysozyme C being preferred for use (column 5, lines 41-42). Carpenter teaches ruminant stomach lysozyme is a lysozyme characteristic of the stomach mucosa of mammals with foreguts (column 1, lines 24-25) and teaches “rumen (foregut)” (column 5, line 21), which one of ordinary skill in the art would recognize that Carpenter is teaching “rumen” as another name for “foregut.” Carpenter teaches the antimicrobial composition can be formulated as a laundry detergent (column 7, lines 24-25; column 10, lines 41-46).
The difference between claim 26 and Carpenter is that Carpenter does not teach a polypeptide having an amino acid sequence having at least 60% sequence identity with the amino acid sequence of SEQ ID NO: 1 and having lysozyme activity.
UniProt A0A0C5AGQ3 teaches a buffalo (Bubalus bubalis) lysozyme C from rumen tissue (see p. 1, top and middle). The amino acid sequence disclosed by UniProt A0A0C5AGQ3 is identical to instant SEQ ID NO: 1 (see Appendix B sequence alignment).
In view of the combined teachings of Carpenter and UniProt A0A0C5AGQ3, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the buffalo lysozyme of UniProt A0A0C5AGQ3 in the detergent composition of Carpenter. One would have been motivated and would have expected success to use the buffalo lysozyme of UniProt A0A0C5AGQ3 in the detergent composition of Carpenter because Carpenter taught the composition comprises a ruminant stomach lysozyme, preferably a ruminant stomach lysozyme C, Carpenter taught ruminant stomach lysozyme is a lysozyme characteristic of the stomach mucosa of mammals with rumens, and UniProt A0A0C5AGQ3 taught a lysozyme C from rumen tissue of a buffalo, which is a mammal.
Regarding claim 27, Carpenter teaches the antimicrobial composition comprises a detergent surfactant (column 7, lines 17-19) and teaches detergent composition components including proteases (column 8, lines 45-46).
Regarding claim 31, since the “at least one additional polypeptide” including nuclease in claim 27 is optional, the prior art need not teach the nuclease of claim 31. See MPEP 2111.04.
Therefore, the detergent composition of claims 26, 27, and 31 would have been obvious to one of ordinary skill in the art before the effective filing date.
Conclusion
Status of the claims:
Claims 1, 6, 8-11, 17-21, 23, 26, 27, and 31 are pending.
Claims 6, 8-11, 17-21, and 23 are withdrawn from consideration.
Claims 1, 26, 27, and 31 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, MANJUNATH N RAO can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
A4Z8Q1_BUBBU
ID A4Z8Q1_BUBBU Unreviewed; 148 AA.
AC A4Z8Q1;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 18-JUN-2025, entry version 71.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN Name=LYZ {ECO:0000313|EMBL:ABF20557.1};
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462 {ECO:0000313|EMBL:ABF20557.1};
RN [1] {ECO:0000313|EMBL:ABF20557.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mammary gland {ECO:0000313|EMBL:ABF20557.1};
RA Sudarshan S.K., Mohanty A.K., Pradeep M.A., Kaushik J.K.;
RT "Cloning and sequence analysis of lysozymes from different tissue of
RT ruminants.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents.
CC {ECO:0000256|ARBA:ARBA00002647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|ARBA:ARBA00010859, ECO:0000256|RuleBase:RU004440}.
CC ---------------------------------------------------------------------------
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DR EMBL; DQ480754; ABF20557.1; -; mRNA.
DR RefSeq; NP_001277843.1; NM_001290914.1.
DR AlphaFoldDB; A4Z8Q1; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GeneID; 102416255; -.
DR KEGG; bbub:102416255; -.
DR OrthoDB; 17373at2759; -.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:TreeGrafter.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd16897; LYZ_C; 1.
DR FunFam; 1.10.530.10:FF:000001; Lysozyme C; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; LYSOZYME C; 1.
DR PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..148
FT /note="lysozyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002678165"
FT DOMAIN 95..113
FT /note="Glycosyl hydrolases family 22 (GH22)"
FT /evidence="ECO:0000259|PROSITE:PS00128"
SQ SEQUENCE 148 AA; 16486 MW; 0DDBF855D33941EC CRC64;
Query Match 100.0%; Score 722; Length 148;
Best Local Similarity 100.0%;
Matches 130; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KVFERCELARALKRFGMDNFRGISLANWMCLARWESSYNTRATNYNAGDRSTDYGIFQIN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 19 KVFERCELARALKRFGMDNFRGISLANWMCLARWESSYNTRATNYNAGDRSTDYGIFQIN 78
Qy 61 SRWWCNDGKTPGAVNACGIPCSVLLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 79 SRWWCNDGKTPGAVNACGIPCSVLLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQD 138
Qy 121 LTSYIQGCGV 130
||||||||||
Db 139 LTSYIQGCGV 148
APPENDIX B
A0A0C5AGQ3_BUBBU
ID A0A0C5AGQ3_BUBBU Unreviewed; 148 AA.
AC A0A0C5AGQ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 38.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462 {ECO:0000313|EMBL:AJK28742.1};
RN [1] {ECO:0000313|EMBL:AJK28742.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Rumen {ECO:0000313|EMBL:AJK28742.1};
RA Gautam D., Mahanty S., Chopra M., Brahma B., Jaiswal L., Mishra P.,
RA Vats A., De B.C., Kumar S., De S.;
RT "Buffalo Lysozyme.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents.
CC {ECO:0000256|ARBA:ARBA00002647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|ARBA:ARBA00010859, ECO:0000256|RuleBase:RU004440}.
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DR EMBL; KP183907; AJK28742.1; -; mRNA.
DR AlphaFoldDB; A0A0C5AGQ3; -.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:TreeGrafter.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd16897; LYZ_C; 1.
DR FunFam; 1.10.530.10:FF:000001; Lysozyme C; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; LYSOZYME C; 1.
DR PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..148
FT /note="lysozyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002182833"
FT DOMAIN 95..113
FT /note="Glycosyl hydrolases family 22 (GH22)"
FT /evidence="ECO:0000259|PROSITE:PS00128"
SQ SEQUENCE 148 AA; 16486 MW; 8B384EE5D33FF75E CRC64;
Query Match 100.0%; Score 722; Length 148;
Best Local Similarity 100.0%;
Matches 130; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KVFERCELARALKRFGMDNFRGISLANWMCLARWESSYNTRATNYNAGDRSTDYGIFQIN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 19 KVFERCELARALKRFGMDNFRGISLANWMCLARWESSYNTRATNYNAGDRSTDYGIFQIN 78
Qy 61 SRWWCNDGKTPGAVNACGIPCSVLLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 79 SRWWCNDGKTPGAVNACGIPCSVLLQDDITQAVACAKRVVSDPQGIRAWVAWRSHCQNQD 138
Qy 121 LTSYIQGCGV 130
||||||||||
Db 139 LTSYIQGCGV 148