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Database: UniProt
Entry: A0A1I7XEJ4_HETBA
LinkDB: A0A1I7XEJ4_HETBA
Original site: A0A1I7XEJ4_HETBA 
ID   A0A1I7XEJ4_HETBA        Unreviewed;       570 AA.
AC   A0A1I7XEJ4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   10-APR-2019, entry version 8.
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};
OS   Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC   Heterorhabditis.
OX   NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_15959};
RN   [1] {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_15959}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23874975; DOI=10.1371/journal.pone.0069618;
RA   Bai X., Adams B.J., Ciche T.A., Clifton S., Gaugler R., Kim K.S.,
RA   Spieth J., Sternberg P.W., Wilson R.K., Grewal P.S.;
RT   "A lover and a fighter: the genome sequence of an entomopathogenic
RT   nematode Heterorhabditis bacteriophora.";
RL   PLoS ONE 8:e69618-e69618(2013).
RN   [2] {ECO:0000313|WBParaSite:Hba_15959}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   WBParaSite; Hba_15959; Hba_15959; Hba_15959.
DR   Proteomes; UP000095283; Whole Genome Shotgun Assembly.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000095283};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713}.
FT   DOMAIN       81    105       C2H2-type. {ECO:0000259|PROSITE:PS00028}.
SQ   SEQUENCE   570 AA;  65199 MW;  E3911023974C9137 CRC64;
     MLIIRFSTIA LNKGLCYTNQ VLVLQVAWIV AVSCSQVKLT PGNRWRYEIR RCRKTSWLSA
     LFIFVATNAK SSSSRSLSCL CVCVSCRHFF IRDRTILGHL SSILHTVDSE SINATSAADS
     NDADRLIRWS PQNFPFFTVI QLARSSTTLL CTIFFLVTQE VHNSLPGALD DICNPLHRVT
     DHDFKGDQIV LFYEYDFGYF PYFNNSDPKQ PVNGGLPQKC PIWKHLLRVS EQIRVAIPRE
     DFAGIAVIDI EEWRPLYHLN WGRKKVYKSE SIQLIREQYP NISYKSADEL ARKEFNAYAR
     KIFLSTIGLA KRLRPYAKWG FYGFPYCNYG AGSQGDSMCN EQFRAYNDEL SFVTNSGNAI
     FPSIYLANND SHIEHFRYIQ AIMMECQRVA AFANPPLPIF PYDKFEYKPY EFLDSFYTKF
     EMWMFGEDIM DGIAKAIPTA SSVTQIIDNF ILNEDEDVSK ITADLGSLLL LIFVVPSTTD
     APSSLGSFAK SLISHFEYQS RAKLVEEAFE KVKKHIRVHS EYPQTALLSS KKQLERLFSI
     RVKALQLGYL NKENIYIQIS HPASSRSGAL
//
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