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Database: UniProt
Entry: A0A0B2VJ59_TOXCA
LinkDB: A0A0B2VJ59_TOXCA
Original site: A0A0B2VJ59_TOXCA 
ID   A0A0B2VJ59_TOXCA        Unreviewed;       297 AA.
AC   A0A0B2VJ59;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-FEB-2019, entry version 12.
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   Name=HYAL4 {ECO:0000313|EMBL:KHN81598.1};
GN   ORFNames=Tcan_15442 {ECO:0000313|EMBL:KHN81598.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN81598.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN81598.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN81598.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J.,
RA   Yang Y., Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W.,
RA   Jex A.R., Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) 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|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KHN81598.1}.
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DR   EMBL; JPKZ01001481; KHN81598.1; -; Genomic_DNA.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031036};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT   ACT_SITE     30     30       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   DISULFID    107    119       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    255    266       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   297 AA;  34181 MW;  3451DBC005981C3F CRC64;
     MTAHLIKAEK DIEKAIPNAS FNGLAILDFE YWRPQYKLNW SSKRIYRNES DRIVRERTNS
     TLNETEVKRI AAEEFDKAAY KFMVETIQLA IKLRPGGKWG FYGLPYCNYN AGKGGEYNCS
     EEFQGYNDGI LNILNETTAL YPSIYLLNLT DTDLNFRYVH AILNETNRVL AMLNYSIPAY
     PYSGFEYLPK TDPLKYYSDD DLCNEVKQQA DFGMQGTIVW STSKNMTFRC PYIANYINTT
     YGPYVSRIES EFRNCSMRKC GGQGRCVLKT PQVQCNSTFN EADYECFPPS STITTLP
//
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