GenomeNet

Database: UniProt
Entry: A0A165GGV2_EXIGL
LinkDB: A0A165GGV2_EXIGL
Original site: A0A165GGV2_EXIGL 
ID   A0A165GGV2_EXIGL        Unreviewed;      1038 AA.
AC   A0A165GGV2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=EXIGLDRAFT_118999 {ECO:0000313|EMBL:KZV90500.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90500.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV90500.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90500.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KV426047; KZV90500.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV90500; KZV90500; EXIGLDRAFT_118999.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077266};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KZV90500.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN      422    606       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1038 AA;  111684 MW;  59468FC9B946A702 CRC64;
     MRHLPDDVPS AHKAAADLEK PGLAPPQRSS SSPDFRRVKL NMRTILGGLA SLLLSGALLQ
     TTGRVPSTLK RATSNGLQDI VTWDEYSLLI NGERIMIFSG EVHPYRMPST SLYLDIFQKI
     KSMGFNAVSF YTFWGMHEPK RGEISFAGFR DLDPFFDAAM EAGIYLIARP GPYINAETTG
     GGFPGWGTYD PAIWRTSNTS FVDAYQLYMK EMGARIAAAQ ITNGGPVILF QAENEYTGWA
     SGYFEDFVFE KELLDTIHDT GIVVPTTHND ASPGGHYLSV DLWGYDSYAL GFDCSHPTVW
     SSNAVPESFW SAHMKYTPDK PNAVYEFQGG AFDGWGGSGY ETCAQLTGPG FERVFYKNEL
     SMSTTILSLY MTYGGTNWGG IAHPGVYTSY DYGSALAEDR TLRDKFFENK LIASFAHSTP
     AFLTSRPQNV GNTAGAFTGN SALKTTQTLD VVGNKTGFYT VRHSDSSSFD TQTYQLNVKT
     SAGTLTIPVL GGSLSLTGKD AKIHVVDYVA GSTQLVYSSA EVMTWATIDG RDVVVLYGDA
     GELHETAIAF SGTAPTAKVV SGSGTIKQQT VGTGALAIQF KTTGQTVVQV GKTLLFLVDR
     ANAYQFWVLH PPTTGAFARF STANPILVKG GYFLRTVDIS GSTLALRGDL NGTSSFEIIA
     PAAQSKTVTF NGARLQTKKT AYGTITASKS VSLPAVTVPN LSALTWKTAD SLPEISASYS
     DAKWVVANHT TTVNPTQPTT PVVLFAGDYG FHTGNILWRA HFTSSGGETG FTVNVQGGAA
     FGYSVWLDSA FIGSWEGNGP TGAKTSTFSF PGGALKSGSA HIITILQDHM GYEEDWTAAS
     ETFKAPRGIL SYAFVGNTAT TVSTWKLTGN LGGEDIVDKD RGPLNEGGLF GERQGWHLPG
     FDDSKWASGK PTTGIAKPGV SFFRTKFNLN VPAGVDYPIA LVTSNATSSP HFRAQFYVNG
     WQFGKYVNAI GPQKVFPVPQ GILNYNGANT LAVSLWAHDS AGAKLDSLSL QVTKKVQSSM
     APVKNQAMTA WTKRANAY
//
DBGET integrated database retrieval system