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Database: UniProt
Entry: A0A1V4K911_PATFA
LinkDB: A0A1V4K911_PATFA
Original site: A0A1V4K911_PATFA 
ID   A0A1V4K911_PATFA        Unreviewed;       318 AA.
AC   A0A1V4K911;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-FEB-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};
GN   Name=HYAL1 {ECO:0000313|EMBL:OPJ80841.1};
GN   ORFNames=AV530_004253 {ECO:0000313|EMBL:OPJ80841.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae;
OC   Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ80841.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ80841.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ80841.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ80841.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) 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|PIRNR:PIRNR038193, 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:OPJ80841.1}.
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DR   EMBL; LSYS01004144; OPJ80841.1; -; Genomic_DNA.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
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; 2.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190648};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    318       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012799168.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     94    108       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    241    252       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    246    300       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    302    311       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   318 AA;  35362 MW;  A5A353A8D8264F87 CRC64;
     MASGSFCCIL LLLLPAPAHA GGPGPVLINR PFVTIWNIPT ENCAENKMLG LLPYYTSEGL
     PATWDIKKSE ELTLQLGKTL RPDGYWGFYG FPDCYNDNFD SLPYTGTCPM VEQQRNAELG
     WLWESSRALY PSIYLPTRLN GTNKVLAYVR HRVAEAFAVF NGSIPVLPYS QIAFNCTVNF
     LSQEDLINTI GESAAQGTAG IVLWGSHIYS SSKEMCLRLK DYVEGPLGHY IVNVTASAEL
     CSQSLCSGQG RCVRRENKLG FLHLDPFRFA IDLQAGKPWV VAQSLEAIDD TIRLAKEFSC
     QCYNKWQGPR CDTQGFTE
//
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