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Database: UniProt
Entry: A0A2B4R313_STYPI
LinkDB: A0A2B4R313_STYPI
Original site: A0A2B4R313_STYPI 
ID   A0A2B4R313_STYPI        Unreviewed;       657 AA.
AC   A0A2B4R313;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
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=HYAL1 {ECO:0000313|EMBL:PFX12011.1};
GN   ORFNames=AWC38_SpisGene24099 {ECO:0000313|EMBL:PFX12011.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX12011.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D.,
RA   Flot J.-F., Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and
RT   Acropora digitifera provides evidence for extensive differences
RT   between species of corals.";
RL   bioRxivorg 0:0-0(2017).
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: 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:PFX12011.1}.
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DR   EMBL; LSMT01001658; PFX12011.1; -; Genomic_DNA.
DR   Proteomes; UP000225706; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000225706};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32    657       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012451117.
SQ   SEQUENCE   657 AA;  74562 MW;  2B418126599AE10E CRC64;
     MSFVQGLFAA RLSRLLHPLL LLVGISLLGD ALDIKNSYCK CEEFPIEDRP FVAIWNAPTG
     GCSVNFSINI NLRDFDILEN PKQTWNGKYV TVFYNAQLGL YPYFTNEQGT NSYNGGMPQL
     INLAAHLDKM KRDIIKKIPD PDYNGLAIID WEGWRPTWER NFDSKRIYQS RSVELVQDKH
     PEWSMENVIE EARKEFERTA RVFMESSIKL ARQIRPKGLW GFYGFPDCFG SNETNYRCSD
     DVKYIKRRDM GKLNYTSSEK QNVCSDQSSF SPGILAPKDG QPATNCKRSQ DCRGEDSIVD
     EYYGTLTTDY SFKRSAQAVT MASKSSVKID NDQVQVDPQL LFQRLVIACD NSHLEALPQY
     ELCTYPTALF DSPFMLRQPQ KPALADALWT RLTPEAKTQA EGNVQYVLDV GALLYRVPWP
     RGSPTYKEVC NMYCTYVQRK YGRAIVMFDG YDEMSTKAMT QQRHASGKVA VTVTFTESMS
     VTMKKDNFLS NPKNKQCFLL MLIGDDTDLL VLLCHHATED GCDLYFRPEP KANARSGRAW
     HMKRVKEQLG KEVYRNLLFL HAINGCDTTS CLYGVGKATA LKKFENVLHF KQQAGIFSRH
     STVSDFVSAG ENALVSLFSG RQGVGLNALR CQRYFEKLAN KTSHIEPQNL PPTTAAA
//
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