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Database: UniProt
Entry: A0A0D1YYV6_9EURO
LinkDB: A0A0D1YYV6_9EURO
Original site: A0A0D1YYV6_9EURO 
ID   A0A0D1YYV6_9EURO        Unreviewed;      1009 AA.
AC   A0A0D1YYV6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PV08_01036 {ECO:0000313|EMBL:KIW20461.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20461.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW20461.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20461.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847492; KIW20461.1; -; Genomic_DNA.
DR   RefSeq; XP_016240677.1; XM_016375401.1.
DR   EnsemblFungi; KIW20461; KIW20461; PV08_01036.
DR   GeneID; 27328119; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053328; 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:UP000053328};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002237424.
FT   DOMAIN      395    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  110843 MW;  1C70084D3E5E50D9 CRC64;
     MKLACASIVG LLATQLAALA VPSQDFGHFK ITEHRDPEKR ALLQDLVTWD KTSMFVRGER
     LMIFSGEFHP FRLPVPSLWL DVLQKVKALG FNCVSFYVDW ALLEGKHGNY TAGGIFALEP
     FFEAATSAGL YLLARPGPYI NAEASGGGFP GWLQRVKGTL RTSDPSYIEA TENYMSHVAG
     TIAEAQITNG GPIILYQPEN EYSKFCCGID GPDGNYMQIV EDQARDAGVV VPFLSNDGAP
     NGYNTPGTGE GSVDIYGHDN YPLGFDCANP TIWPAGQLPT DYWQRHLRQS PSTPYSIPEL
     QGGSFDPWGG PGFQKCGVLV GSEFERVFYK NYISFGIKFL NLYMIYGGTN WGNLGHPNGY
     TSYDYAAAIA EGRQVDREKY SQLKLIGSFV KASPAYLDAD PLHNSTTLYT DSKDLLVTPL
     MSNSSVTTFY VLRHANYTSQ ASTSYKLILR TSAGNITVPQ SGGTLALHGR DSKVHVTDYD
     INGTNVLYST AEIFTWKDFG QKKVLLVYGG PGEHHEISIS SASTPSLVEG PEAGVTMKCG
     SQAVVAWDTA PQRRIVKVDN LEIFILDRNS AYNYWVPELS SNSQTAGFSS KETTAGSIIV
     KAGYLVRGAY LEGSNLYLAA DFNATTPIEV IGVPNSANAL FVNGQPSQYT TSSNGDWATT
     VTWADPKFTL PTLSSLDWKY VDTLPEIQPG YDDWLWPFAD LTTTNNTWRD LTTPTSLYAS
     DYGFHSGSLL YRGHFVSQGN ESILYINTRG GKAYGHSIWL NQTFVGSWAG VSTQNNTNVT
     YNLPPLQAGK AYVFSILIDH MGYDESGFIG SDLMKTPRGI LDYSLAGQEK TAITWKLTGN
     LGGEDYRDRT RGPLNEGGMY AERQGWHLPN PPSQNWESRS PFDGVSEAGV GFFSTQFDLD
     IPAGWDVPLS FKFGNSTQPP AQYRVQFYIN GFQYGKYVNH IGPQTTFPVP QGVLNYKGTN
     WLALTLWAHQ PEGAKLEIFR LESDTPVMSA LGKVDFVGES GYSPREGAY
//
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