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Database: UniProt
Entry: A0A0D2CDV1_9EURO
LinkDB: A0A0D2CDV1_9EURO
Original site: A0A0D2CDV1_9EURO 
ID   A0A0D2CDV1_9EURO        Unreviewed;       982 AA.
AC   A0A0D2CDV1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 20.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PV07_08096 {ECO:0000313|EMBL:KIW28430.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28430.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW28430.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28430.1,
RC   ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847043; KIW28430.1; -; Genomic_DNA.
DR   RefSeq; XP_016248646.1; XM_016395227.1.
DR   EnsemblFungi; KIW28430; KIW28430; PV07_08096.
DR   GeneID; 27347290; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054466; 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; 2.
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:UP000054466};
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:UP000054466};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    982       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002239622.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   982 AA;  107567 MW;  046DEFEF51C40864 CRC64;
     MRLTIVSVFA CLAAWVAALA LPGQNFGGLK IIEHPDPEKR QLLQDIVTWD ETSLFIHGQR
     IMIFSGEFHP FRLPVPSLWL DVFQKVKALG FNCVSFYLDW AVLEGKPGNF SAEGVFALEP
     FYEAASAAGV YLIARPGPYI NAEASGGGFP GWLARLPDRL RTTDPGYLAS TENYVRNVAS
     SIAAAQITNG GPVILYQPEN EYSQGCCGVD FPDGQYMQDV MDQARQAGIV VPMISNDARP
     SGHNAPGTGV GAVDIYGHDG YPLGFDCSHP RAWPDGALPT TYWQTHLNES PTTPYSIDEF
     QGGSFDPWGG PGFDNCEILV NYEFVRVFYK NIIASGAKIF NIYMIYGGTN WGNLGHDGGY
     TSYDYAAAIS ENRQVDRQKY SETKLISNFV KASPAYLIAE PLQLNTTSVF TNTSDLTVTS
     VGGNESETTF YIVRHYNYSD LSATLYKLSV PTRSGNLTVP QLGGTLTLGG RDSKVHVVDY
     DLAGVNLLYS TAEIFTWKDL GGRTVLILYG GEGEHHELCV TSSSVPSVIE GDSSTVTTSQ
     TGSGVIVAWD ASSTRRVVQI GQLEVFLLGK NSAYDYWVLD LFTIGSRNRF ASAYTNASSV
     IVKTGYLARE IHLNRDELHL RADFNDTTSI EVIGVPTTAK SLFVNGVPVQ YKANSRGDWS
     AAFDYEDPNI TLPDIQSLEW KYIDSLPEIQ PASDYGYHGG SLIYRGHFTA QRSSTNLSLN
     TQGGWAFGHS LWLNQSFLGS YVGVSTENNT NATYLLSTLQ PGSNYVLTIL IDHMGLEENG
     YVGSDQMKTP RGILDYELAG YDDSAISWKL TGNLGGEDYV DRSRGPLNEG SMYAERQGWH
     LPNPPSLSWE SRSPLIGISD PGIGFFSTSF DLSIPDGWDL PVSFTFGNTT TPAEPYRTQL
     FVNGFQYGKH VNHIGPQTSY PVPQGILNYN GTNWLALTLW SQQPGGAKLD SLELVFDRPV
     ATALTRIGFV EGSVYTLRQG AY
//
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