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Database: UniProt
Entry: A0A182FPP5_ANOAL
LinkDB: A0A182FPP5_ANOAL
Original site: A0A182FPP5_ANOAL 
ID   A0A182FPP5_ANOAL        Unreviewed;       206 AA.
AC   A0A182FPP5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   18-SEP-2019, entry version 12.
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 albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|Proteomes:UP000069272, ECO:0000313|VectorBase:AALB008512-PA};
RN   [1] {ECO:0000313|Proteomes:UP000069272, ECO:0000313|VectorBase:AALB008512-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|Proteomes:UP000069272,
RC   ECO:0000313|VectorBase:AALB008512-PA};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles albimanus ALBI9_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:AALB008512-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|VectorBase:AALB008512-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|RuleBase:RU610713}.
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DR   VectorBase; AALB008512-RA; AALB008512-PA; AALB008512.
DR   Proteomes; UP000069272; 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:UP000069272};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069272}.
SQ   SEQUENCE   206 AA;  23770 MW;  88D75FCB58F24C1E CRC64;
     MCAWHFSLQA TRRFEATGRE FMERTLRLAK ERRPRAAWGY YAFPYCFNMN GGANSRTENC
     SPEVQRENNR ILWLFDGSDI VFPSVYLRES LSPGEREQLI RGRVREAVRV AQRTIGAKAR
     RKVLTYLRYV YTDTIQYLTE SDWINALAAM KSTGSDGIVL WGSSFDLNTR QECVNFKAYL
     ESTLGPVLSS LQPRYMVENL PDPAIN
//
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