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Database: UniProt
Entry: A0A0G2E0K0_9EURO
LinkDB: A0A0G2E0K0_9EURO
Original site: A0A0G2E0K0_9EURO 
ID   A0A0G2E0K0_9EURO        Unreviewed;       927 AA.
AC   A0A0G2E0K0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=UCRPC4_g06067 {ECO:0000313|EMBL:KKY15881.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae;
OC   Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY15881.1};
RN   [1] {ECO:0000313|EMBL:KKY15881.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15881.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell
RT   wall degradation and secondary metabolism in the genomes of grapevine
RT   trunk pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY15881.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15881.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKY15881.1}.
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DR   EMBL; LCWF01000171; KKY15881.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY15881; KKY15881; UCRPC4_g06067.
DR   OrthoDB; 179316at2759; -.
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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}.
FT   DOMAIN      361    542       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   927 AA;  102349 MW;  29D045C9BFC7C9AC CRC64;
     MDLLIQVKWD KDSVFVRGER VMLYSGEFHP FRLPVPGLWL DIFQKIKALG FNGVSFYTDW
     GLLEGNPGRV VVDGVWALDE FFDAASEAGI YLIARPGPYI NAETAAGGIP GWVLRINGTI
     RSMSQDYLDA TKNYVSTIGQ IIARAQITNG GPVILLQPEN EYSTWPGEND TTFPNDMNRL
     YMAFVERQFR DTGIVVPYVV NDNKNLGYFA PGSGEGAVDI YGIDSYPLRY DCANPYIWPT
     YRWPTGWQID HQKYSPTTPF TIGEFQGGSG GGWGGVTEEG CAILVNNEAV RVVYKNNYSF
     GVKVFNVYMT YGGTNWGNLG YEGGYTSYDY GAAITEGRHV RREKYSETKL EAIFLKSSPA
     YLTAIPGNET NGSYASTSAI GVTPLFGAEN NTNFYIVRHA DFTSTSNTTY KLSVPTSIGN
     VTIPQLGGAL SINGRDSKIH VTDYDVGGLN LIYSTADIYT WTKGPGVERV LIIYGGAAET
     HEFAVPVPLG RPDIIEGAFL TTKQVGAAWI VQWKVTPQRK VVQFGDGRLE VHLLWRNEAY
     NYWALELPAA EPIGNYTSPS KSSVIVQTGY LLRTAQIVDD ELRLTGDINS TTNIEIISAP
     TEKISLLKFN GQIIQTTKSP QGRIAGSVPF SAPNITLPSL SALEWKYFDS LPEIKPDYDD
     SLWIVCDHLN TTNPLKPSTP TSLYATDYGF HSGSLIYRGH FVSNGLETSF SANISGGYGF
     GYSIWLNSTF LGSFTGTNAP SFRIQTLPFP TPLTKNSHYI LTILIDHMGQ DEEAPGTDAI
     KSPFGILSYN LTAHPATDLT WKLTGNLGGE QYLDLIRGPR NEGAMAAERH GYHLPNAPDT
     NWPVSNPITH GLERDGVGFY ATHFDLHIPL GYDVPLNFVF SNTTASKSNY RIQLFVNGFQ
     YGKYSAIQPG PSNNVSRSRR NPQLQWK
//
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