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Database: UniProt
Entry: A0A1I8CSD2_9BILA
LinkDB: A0A1I8CSD2_9BILA
Original site: A0A1I8CSD2_9BILA 
ID   A0A1I8CSD2_9BILA        Unreviewed;       361 AA.
AC   A0A1I8CSD2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   10-APR-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};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000740300.1};
RN   [1] {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000740300.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KR3021 {ECO:0000313|Proteomes:UP000095286,
RC   ECO:0000313|WBParaSite:RSKR_0000740300.1};
RX   PubMed=26829753; DOI=10.1038/ng.3495;
RA   Hunt V.L., Tsai I.J., Coghlan A., Reid A.J., Holroyd N., Foth B.J.,
RA   Tracey A., Cotton J.A., Stanley E.J., Beasley H., Bennett H.M.,
RA   Brooks K., Harsha B., Kajitani R., Kulkarni A., Harbecke D.,
RA   Nagayasu E., Nichol S., Ogura Y., Quail M.A., Randle N., Xia D.,
RA   Brattig N.W., Soblik H., Ribeiro D.M., Sanchez-Flores A., Hayashi T.,
RA   Itoh T., Denver D.R., Grant W., Stoltzfus J.D., Lok J.B., Murayama H.,
RA   Wastling J., Streit A., Kikuchi T., Viney M., Berriman M.;
RT   "The genomic basis of parasitism in the Strongyloides clade of
RT   nematodes.";
RL   Nat. Genet. 48:299-307(2016).
RN   [2] {ECO:0000313|WBParaSite:RSKR_0000740300.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000740300.1};
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|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713}.
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DR   WBParaSite; RSKR_0000740300.1; RSKR_0000740300.1; RSKR_0000740300.
DR   Proteomes; UP000095286; Genome Assembly.
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:UP000095286};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    361       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009317432.
FT   ACT_SITE    134    134       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   DISULFID     42    337       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    210    222       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   361 AA;  42361 MW;  D6CEA39C8856F7D9 CRC64;
     MPISRTSPNA SSIIFLLLFL QIKNQLAYEK TKIYWNSPSA TCTRHNETGI NLEKFHIISN
     VGQKFSGNEI VLFYEKDIGL YPAIRKYANG SHVWEHNGIP QNVNMTEHLA KVKKDVGKLI
     PSHSFRGLAI LDFEEWRPFY DQNWSSKRIY REASIDKVMK KHPKIKRVDA IKIAKDEFDR
     ASLDFLVKTL KECQLMRPNA KWGFYGFPIC DENGATRNNT FCYPEHDNRL VEFLKYADAL
     YPSAYLYPGR TYHDKHLFVE DVLKETARMN AMIVNEGFQA KHVFVFHKFE LDPYVDNPND
     ILFYDKYHLC ITMKQTFDYG VDGILLWSTS KNMAKRCKHI SNYIEYHLGP YLHELQTFHD
     E
//
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