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Database: UniProt
Entry: A0A0D1Y8Q7_9EURO
LinkDB: A0A0D1Y8Q7_9EURO
Original site: A0A0D1Y8Q7_9EURO 
ID   A0A0D1Y8Q7_9EURO        Unreviewed;      1009 AA.
AC   A0A0D1Y8Q7;
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=PV11_09006 {ECO:0000313|EMBL:KIV77184.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77184.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV77184.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77184.1,
RC   ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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; KN846954; KIV77184.1; -; Genomic_DNA.
DR   EnsemblFungi; KIV77184; KIV77184; PV11_09006.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053599; 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:UP000053599};
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:UP000053599};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     28       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        29   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002246742.
FT   DOMAIN      396    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  110110 MW;  AFB7564B1F67C812 CRC64;
     MKLISASILG LLAAQLVAFA VPSHNVGGLR IIEHPDPEKR ALLQNLVTWD QTSLFVRGER
     IMIWSGEVHP FRLPVPSLWF DIFQKVKALG FNCVSFYVDW ALVEGKPGNY SAEGVFALEP
     FFEAASSAGI YLLARPGPYI NAEASGGGFP GWLQRIKGRL RTTDADYLNA TQNYASHVAA
     TIAKSQITNG GPIILYQPEN EYSGFCCGLT GPDGQYMQDV MNQARAAGVV IPFLSNDAGT
     HGYNVPGSGV GSVDIYGHDG YPLGFDCANP TVWPSGNLPT TWWQLHLQQS PTTPYSITEF
     QAGSFDPWGG PGFAKCGVLI NSEFERVFYK NDLSFSVKIL NLYMTYGGTN WGNLGHPGGY
     TSYDYAAPIA EGRQVYREKY SQLKLMGNFI KVSPAYFDAT SMPNSTTLYT NTADLTVTPV
     KANSSATTFY VLRHANYTSQ NSTSYKLNLP TSAGNLSIPQ LGGTLTLNGR DSKIHVTDYD
     VNGTNILYST AEIFTWKDFG PRKVLLVYGG PGEHHEISVS STVSPTLLEG SQSGLTFRNG
     SSVVVAWDTS AQRRIVQVGD LEIYILDRNS AYNYWVPELS KSASNTSFSS QESTASSIIV
     QAGYLVRAAL LNGTELHLSA DFNDTTLVEV IGAPSSAKTL FINGQSVGYT TSSVGDWTET
     VNLPAQNMTP PSLNNSEWKY IDSLPEIHPG YDDSLWSTAN HPTTNNTVRN LTTPTSLYAA
     DYGFHTGSLL YRGHFVAQGN ESSIYLNTQG GWAFGSSVWL NQTFLGSWAG VSTQNNTNAT
     YNLTHIQAGQ PYVFTVLIDH MGLEENGVVG ADTMKTPRGI LNYALAGRDD TAITWKLTGN
     LGGENYRDPV RGPLNEGAMY AERQGWHLPR PPNQNWTSGS PYVGISQPGV GFFSTQFDLN
     IPSGWDVPMS FTFTNMTQPP SEYRVQLFVN GFQYGKYINH IGPQTSYPVP PGVLNYQGTN
     WLALTLWAHQ PGGAKLEGFQ LVYDTPIKSA LANIEFVGQA GYEPRPGAY
//
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