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Database: UniProt
Entry: A0A0M3JJA3_ANISI
LinkDB: A0A0M3JJA3_ANISI
Original site: A0A0M3JJA3_ANISI 
ID   A0A0M3JJA3_ANISI        Unreviewed;       104 AA.
AC   A0A0M3JJA3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000256|RuleBase:RU610713};
GN   ORFNames=ASIM_LOCUS7483 {ECO:0000313|EMBL:VDK29309.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0000772201-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0000772201-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ASIM_0000772201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDK29309.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35; Evidence={ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|RuleBase:RU610713}.
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DR   EMBL; UYRR01018172; VDK29309.1; -; Genomic_DNA.
DR   WBParaSite; ASIM_0000772201-mRNA-1; ASIM_0000772201-mRNA-1; ASIM_0000772201.
DR   Proteomes; UP000036680; Genome.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036680};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    104       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5018390620.
SQ   SEQUENCE   104 AA;  11938 MW;  6252F1E048710348 CRC64;
     MVAERICLWC SIFLYYLESA SSISVYWNVP TRVCIKRGID LELSRYGIRT NADERFYGNE
     VVTFYEGKIG LYPLYNVNQN ATYTINHGLP QVSSIVRSRA TNSP
//
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