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Database: UniProt
Entry: W2SPF9_NECAM
LinkDB: W2SPF9_NECAM
Original site: W2SPF9_NECAM 
ID   W2SPF9_NECAM            Unreviewed;       258 AA.
AC   W2SPF9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 20.
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=NECAME_14184 {ECO:0000313|EMBL:ETN71535.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Bunostominae; Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN71535.1};
RN   [1] {ECO:0000313|EMBL:ETN71535.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mitreva M.;
RT   "Draft genome of the hookworm Necator americanus.";
RL   Submitted (APR-2013) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KI667868; ETN71535.1; -; Genomic_DNA.
DR   RefSeq; XP_013293762.1; XM_013438308.1.
DR   GeneID; 25354211; -.
DR   KEGG; nai:NECAME_14184; -.
DR   CTD; 25354211; -.
DR   KO; K01197; -.
DR   OrthoDB; 1096692at2759; -.
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   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}.
FT   DOMAIN      201    248       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DISULFID    238    247       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   258 AA;  30676 MW;  47741A5E45A7714A CRC64;
     MKLVRSRHPT LRWKQIEQIA EKEYNRAAKT FLMKTLKKAR EVRPNALWGL YDFPFCNGKA
     GEEKGDFECS KEAQNYNDRM AFIYNTSRAF YPSIYLNGKK TFEQNFRFNR AIINEARRIA
     NDQQRRVDYY VYTKFEYDPY TRFDWFYKSE DICNTMKLPA DLGASGLVLW STSKNMRDRC
     GNIDRYMRNQ LLPYISTMRD QIGECRREMC SGNGNCVLKK QLKKCYQKMN YADYECRCDR
     GFDGPDCSLK KKSTTTIK
//
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