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Database: UniProt
Entry: A0A016WJU1_9BILA
LinkDB: A0A016WJU1_9BILA
Original site: A0A016WJU1_9BILA 
ID   A0A016WJU1_9BILA        Unreviewed;       300 AA.
AC   A0A016WJU1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   05-DEC-2018, entry version 14.
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=Acey_s0637.g946 {ECO:0000313|EMBL:EYC39881.1};
GN   ORFNames=Y032_0637g946 {ECO:0000313|EMBL:EYC39881.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC39881.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:EYC39881.1}.
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DR   EMBL; JARK01000237; EYC39881.1; -; Genomic_DNA.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000024635};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN      231    273       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DISULFID    263    272       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   300 AA;  34243 MW;  640216455EC86F3C CRC64;
     MLQANTPKNC VIQRNSIVKV FRNQSIALAR INNIGIHNES EIESIAEKDF NDAARNFFVK
     TIQMGRELRP HALWGFYGFP YCNYNAGQNG EYECSKPYRD WNDRMMFIFN ESSALYPSIY
     LGFNATSDQR FRYVQAILRE ARRVANKFTP PLPIYAYSKI EYNPLKEIAD FYDTRDLCST
     IKQPADLGID GIIFWSSSNN MTLRCPYIKD NMEKVIGPKV RTIISQQDAC GKIRCRSNGK
     CVLPTNTTCQ DFNMNTNLYK CECNEGFSGE DCSVQNTDGV AVAPQRSGRS ATLKRVIHLS
//
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