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Database: UniProt
Entry: A0A060A0J8_XENLA
LinkDB: A0A060A0J8_XENLA
Original site: A0A060A0J8_XENLA 
ID   A0A060A0J8_XENLA        Unreviewed;       153 AA.
AC   A0A060A0J8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN   Name=lyz.L {ECO:0000313|RefSeq:XP_018107197.1,
GN   ECO:0000313|Xenbase:XB-GENE-6252020};
GN   Synonyms=lyz {ECO:0000313|EMBL:AIA57285.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AIA57285.1};
RN   [1] {ECO:0000313|EMBL:AIA57285.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhao D., Ma L., Yang L., Zhang S.;
RT   "Molecular cloning, expression and bioactivity analysis of lysozyme in
RT   South African clawed frog, Xenopus laevis.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:XP_018107197.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018107197.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018107197.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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|RuleBase:RU004440}.
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DR   EMBL; KJ591621; AIA57285.1; -; mRNA.
DR   RefSeq; XP_018107197.1; XM_018251708.1.
DR   RefSeq; XP_018107197.1; XM_018251708.2.
DR   STRING; 8355.A0A060A0J8; -.
DR   PaxDb; 8355-A0A060A0J8; -.
DR   GeneID; 443604; -.
DR   KEGG; xla:443604; -.
DR   CTD; 443604; -.
DR   Xenbase; XB-GENE-6252020; lyz.L.
DR   OMA; GWRNHCQ; -.
DR   OrthoDB; 4825544at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 443604; Expressed in spleen and 15 other cell types or tissues.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   CDD; cd16897; LYZ_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   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..153
FT                   /note="lysozyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010899096"
FT   DOMAIN          96..114
FT                   /note="Glycosyl hydrolases family 22 (GH22)"
FT                   /evidence="ECO:0000259|PROSITE:PS00128"
SQ   SEQUENCE   153 AA;  17570 MW;  4EED629353AA7134 CRC64;
     MNSAVLILVG IFIFPATNGK LFERCELAGT MKKMGLDGYR GYSLPNWVCT AFFESSFYTD
     RTNFNRGDNS TDYGILQINS RWWCNDDKTP RSHNACNINC RDLLSDDITQ SVICAKRVVR
     DPQGMEAWVG WRNHCKGRDL SQWIKDCKLD ILL
//
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