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Database: UniProt
Entry: A0A182FUQ4_ANOAL
LinkDB: A0A182FUQ4_ANOAL
Original site: A0A182FUQ4_ANOAL 
ID   A0A182FUQ4_ANOAL        Unreviewed;       740 AA.
AC   A0A182FUQ4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 13.
DE   RecName: Full=Beta-glucuronidase {ECO:0000256|RuleBase:RU361154};
DE            EC=3.2.1.31 {ECO:0000256|RuleBase:RU361154};
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:AALB010289-PA};
RN   [1] {ECO:0000313|Proteomes:UP000069272, ECO:0000313|VectorBase:AALB010289-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|Proteomes:UP000069272,
RC   ECO:0000313|VectorBase:AALB010289-PA};
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:AALB010289-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|VectorBase:AALB010289-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in the degradation of dermatan
CC       and keratan sulfates. {ECO:0000256|RuleBase:RU361154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-
CC         glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411;
CC         EC=3.2.1.31; Evidence={ECO:0000256|RuleBase:RU361154};
CC   -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid.
CC       {ECO:0000256|RuleBase:RU361154}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361154}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|RuleBase:RU361154}.
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DR   VectorBase; AALB010289-RA; AALB010289-PA; AALB010289.
DR   Proteomes; UP000069272; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000069272};
KW   Glycosidase {ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|RuleBase:RU361154};
KW   Lysosome {ECO:0000256|RuleBase:RU361154};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     44     64       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       94    273       Glyco_hydro_2_N. {ECO:0000259|Pfam:
FT                                PF02837}.
FT   DOMAIN      276    387       Glyco_hydro_2. {ECO:0000259|Pfam:
FT                                PF00703}.
FT   DOMAIN      394    658       Glyco_hydro_2_C. {ECO:0000259|Pfam:
FT                                PF02836}.
SQ   SEQUENCE   740 AA;  84419 MW;  45B08825CAB6B521 CRC64;
     MVAPSSSDGE RKRLVAAIEQ EQRQKRRRKL ERLRQIQHDH RMRLLVTAAI VVTFLVMGVI
     GYMVNAVFGV MYTSGNESST EGLLYPIESE TRELKSLDGV WNFVRSESNN PSQGIREKWY
     NDDLARVRKT IPMPVPSSYN DVTEDAGLRD HVGTVWYDRK FFVPRSWADS GDRVLVRFGS
     VHYDTIVWIN GVQIVKHEFG HLPFEAEVTK VLKYGQENRI TVLCDNVLLQ VTVPQGKVDN
     QAIDNGVEMV QSYTFDFFNY AGIHRSVMLY TVPKLYIKDV AIRTGYDEDV GSGTVDYQIT
     TSANETDNLQ VTVKLYDRNG TLVGKDLAQG QLQGTASIPE VRLWWPYLMH PEPGYLYTME
     ITLATIGPVG DASPTVLDIY RMKVGIRTLE WNATAFLING KPIYFRGFGR HEDSDIRGKG
     LDLALLTKDF NLLKWVGANA YRTSHYPYSE ESMQFADEHG IMIIDECPSV DTDNYSQILL
     QKHKSSIEQL IHRDRNHPSV VMWSIANEPR TGRLDADAYF AAVAAYTKQL DPTRPITAAI
     AVNVNDDRAA QHLDIISFNR YNAWYANAGR LNMITNRVIE EAQAWNKKHN KPVLMSEYGA
     DTMEGLHMLP AYIWSEDYQT RVFSQHFKAF DALRKQHFFI GEFVWNFADF KTAQSKDKHH
     TGGTDGHGEA DDFPYLTAYT RVGGNKKGIF TRNRQPKAAA YLLRQRYYML GDLGKGQLPD
     DLFLYTAPEA LQQTKDREEL
//
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