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Database: UniProt
Entry: A0A0D2E9N0_9EURO
LinkDB: A0A0D2E9N0_9EURO
Original site: A0A0D2E9N0_9EURO 
ID   A0A0D2E9N0_9EURO        Unreviewed;      1009 AA.
AC   A0A0D2E9N0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-FEB-2018, entry version 18.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PV05_10095 {ECO:0000313|EMBL:KIW51365.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51365.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW51365.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51365.1,
RC   ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KN847322; KIW51365.1; -; Genomic_DNA.
DR   RefSeq; XP_013311949.1; XM_013456495.1.
DR   EnsemblFungi; KIW51365; KIW51365; PV05_10095.
DR   GeneID; 25332003; -.
DR   Proteomes; UP000054342; 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; -; 3.
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:UP000054342};
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:UP000054342};
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_5002241173.
FT   DOMAIN      395    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  110447 MW;  2B55609A744A139D CRC64;
     MKLILGSILA LAATHLAALA VPSHSLGGFR VIEHPDADKR ALLQDLVTWD ETSLFVRGER
     IMIFSGEVHP FRLPVPSLWL DVFQKVKALG FNCVSFYVDW ALVEGKPGNY TAEGVFALEP
     FFEAASSAGV YLLARPGPYI NAEASGGGFP GWLQRIKGRL RTTDPDYIAA TQNYVSHVAS
     TIAKAQITDG GPIILYQPEN EYSGFCCGLS KPDGQYMQDV MDQARDAGIV VPFLSNDAGV
     NGYNAPGTGV GSVDIYGHDN YPLGFDCANP TVWPAGKLPT DYWQRHLRQS PTTPYSITEF
     QAGSFDPWGG PGFAKCGVLV NSEFERVFYK NDLSFSVKIL NLYMTYGGTN WGNLGHAGGY
     TSYDYAAPIA EGRQVDREKY SQLKLIGNFV KVSPAYFEAD PLHNSTSLYT NTADLIVTPV
     KSNSSATTFF ILRHNNYTSQ ASTPYKLMLP TSAGNLSVPQ LGGTLSLNGR DSKIHVTDYD
     INGTNILYST AEIFTWKDFG HKKVLLVYGG PGEHHEMSIS SSSSPSLIEG TQSGLTLQSG
     SRAVIAWDTA PQRRIIQLDN LQIFILDRNS AYDYWVPELS SNGPTQDFSS QKSTAASIIV
     RAGYLVRTAY LSGSALHLTA DFNATSPIEV IGVPTAAKSL FVNGQCVQYT VGDTGDWSTN
     VAWTDPMLTL PTLSSLDWKF ADSLPEIQPA YDDSLWPLAN HPTTKNTWRN LTTPTSLYSS
     DYGFHSGSFL YRGHFSAQGN ESSIYLNTRG GTAYGHSVWL NQTFIGSWSG VSTANNTNVT
     YNLPQVQAGK PYVLTVLIDH MGYDENGAVG GDEMKTPRGI LDYNLAGRDK SAITWKLTGN
     LGGEDYRDRA RGPLNEGSMY AERQGWHLPN PPNENWESRS PLDGISQPGV GFFSTQFDLN
     IPQGWDVPLS FDFGNSTHPP SEYRVQLFVN GFQYGKYVNH IGPQTSFPVP PGVLNYQGTN
     WLALTLWAHQ PEGAKLESFQ LENDTPVMSA LGIIEFVGQS GYAQREGAY
//
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