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Database: UniProt
Entry: E2ADC1_CAMFO
LinkDB: E2ADC1_CAMFO
Original site: E2ADC1_CAMFO 
ID   E2ADC1_CAMFO            Unreviewed;       342 AA.
AC   E2ADC1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   08-MAY-2019, entry version 29.
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   ORFNames=EAG_07137 {ECO:0000313|EMBL:EFN68537.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN68537.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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   EMBL; GL438749; EFN68537.1; -; Genomic_DNA.
DR   InParanoid; E2ADC1; -.
DR   OMA; GGEQCQW; -.
DR   Proteomes; UP000000311; 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:UP000000311};
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:UP000000311}.
FT   ACT_SITE    124    124       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   DISULFID     34    321       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    200    212       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   342 AA;  39976 MW;  C30DF7DA821DBAAD CRC64;
     MSYLVFLSSL GATTPEAGNP QQFDVYWNVP SFICHKYGVK FENLKNFGIH QNANDEFRGE
     EIVILYDPGM FPALLSDKNG TVTKRNGGVP QEGDLKEHLE IFRKHLIKQI PDESFNGIGV
     IDFESWRPIF RQNWASLEPY KTLSIKLERE KHPIWSDAAI KKEAKRRFEK YGRIFMEETL
     KIAKKLRPKA TWGYYGYPHC FNYTPGQRTA HCSHQTMVEN DEMSWLFTLE DVLMPSLYLR
     QEIREMDRMG FVKGRVSEAL RMTEKSKRQV LPYYWFKYQD HRDIFLSKED TENTINTIAS
     LGANGMIIWG SSEDTNTEEK CKNLQQYVKD VLGPAIKRIK QQ
//
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