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Database: UniProt
Entry: A0A182UBN8_9DIPT
LinkDB: A0A182UBN8_9DIPT
Original site: A0A182UBN8_9DIPT 
ID   A0A182UBN8_9DIPT        Unreviewed;       362 AA.
AC   A0A182UBN8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 14.
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   Anopheles melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|Proteomes:UP000075902, ECO:0000313|VectorBase:AMEC017492-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075902, ECO:0000313|VectorBase:AMEC017492-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902,
RC   ECO:0000313|VectorBase:AMEC017492-PA};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:AMEC017492-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|VectorBase:AMEC017492-PA};
RG   VectorBase;
RL   Submitted (JUN-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   VectorBase; AMEC017492-RA; AMEC017492-PA; AMEC017492.
DR   Proteomes; UP000075902; 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   GO; GO:0006952; P:defense response; 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; IPR001329; Venom_Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00847; HYALURONDASE.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075902};
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:UP000075902};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    362       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008138066.
FT   ACT_SITE    130    130       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   DISULFID     38    330       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    206    220       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   362 AA;  42110 MW;  1CF522908908937F CRC64;
     MVYVSTRSAT LWMLLPLLQN LVTIKSFEVY WNIPTFMCNQ FGFEFSSVNR TYSVVQNRND
     TFRGNAVSIL YDPGKFPALL EKPSTKTLYK RNGGVPQEGN LTEHLEIFER HLDELIPDRN
     FSGIGIIDFE SWRPIYRQNF GSLQPYKDLS VKIERERHPY WSGNHLEREA TRRFEATGRE
     FMEQTLLLAK QRRPLAAWGY YAFPYCFNMN GAASTRSENC SPEVQRENNR IMWLFDGSDI
     IFPSVYLREK LSPSERQQLI RGRVREAVRV AQRTKPRRKV LTYLRYVYTD SIQYLTESDW
     INALAAMKST GSDGIILWGS SFDLNTRQKC TSFKAYLDST LGPVLSTLQP RYIVKNIPDT
     ST
//
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