ID   A0A3B3U1R2_9TELE        Unreviewed;       183 AA.
AC   A0A3B3U1R2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Lysozyme g {ECO:0000256|ARBA:ARBA00016485, ECO:0000256|PIRNR:PIRNR001065};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|PIRNR:PIRNR001065};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000006536.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000006536.1}
RP   IDENTIFICATION.
RG   Ensembl;
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         ECO:0000256|PIRNR:PIRNR001065};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family.
CC       {ECO:0000256|ARBA:ARBA00008902, ECO:0000256|PIRNR:PIRNR001065}.
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DR   RefSeq; XP_014904843.1; XM_015049357.1.
DR   AlphaFoldDB; A0A3B3U1R2; -.
DR   Ensembl; ENSPLAT00000006078.1; ENSPLAP00000006536.1; ENSPLAG00000009245.1.
DR   GeneID; 106957840; -.
DR   KEGG; plai:106957840; -.
DR   GeneTree; ENSGT00390000017614; -.
DR   OrthoDB; 2964133at2759; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd01021; GEWL; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR31698:SF8; LYSOZYME G; 1.
DR   PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 1.
DR   Pfam; PF01464; SLT; 1.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001065};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001065}.
FT   DOMAIN          52..159
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
SQ   SEQUENCE   183 AA;  20418 MW;  BF40A0A57278346E CRC64;
     MSYGDITRVS ASGASEKTSQ QDRLGYSGVE ASEKMAQMDS GRMNKYKSKI NSVGSQCGID
     PALIAAIISR ESRAGNALDD GWGDHGNAWG LMQVDIRYHQ KEGDWDSEEH LRQATGILVH
     FIKRIQNKFP NWSREQQLKG GIAAYNMGDG NVHSYENLDA ITTGKDYSND VVARAKWYKR
     YGY
//