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Database: UniProt
Entry: A0A1U8DHF1_ALLSI
LinkDB: A0A1U8DHF1_ALLSI
Original site: A0A1U8DHF1_ALLSI 
ID   A0A1U8DHF1_ALLSI        Unreviewed;       221 AA.
AC   A0A1U8DHF1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Lysozyme g {ECO:0000256|ARBA:ARBA00016485};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
DE   AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000256|ARBA:ARBA00031262};
GN   Name=LOC102379687 {ECO:0000313|RefSeq:XP_014376650.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014376650.1};
RN   [1] {ECO:0000313|RefSeq:XP_014376650.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family.
CC       {ECO:0000256|ARBA:ARBA00008902}.
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DR   RefSeq; XP_014376650.1; XM_014521164.1.
DR   GeneID; 102379687; -.
DR   KEGG; asn:102379687; -.
DR   InParanoid; A0A1U8DHF1; -.
DR   OrthoDB; 2964133at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR31698:SF8; LYSOZYME G; 1.
DR   PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 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:ARBA00022638};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   ACT_SITE        109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
SQ   SEQUENCE   221 AA;  24417 MW;  24164B5584C11805 CRC64;
     MEHFDSTALL KETVSLSTSL HLESVTDPDT SADTSSQSGC YGNINRVDTT GASCQTARPE
     RLPYCGVAAS EKIAEKDLGR MNRYKNIIXS AGQSLCVDPA VIAGIISRES HVGSSLKNGW
     GDRGNGFGLM QVDKRYHKIV GQWNSKTHVL QGTQILVNMI RTIQRKFPRW TKEEQLKGGI
     SAYNAGPRNV QTYARMDIGT THNDYANDVV ARAKFYKRNG Y
//
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