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Database: UniProt
Entry: A0A017SRB5_9EURO
LinkDB: A0A017SRB5_9EURO
Original site: A0A017SRB5_9EURO 
ID   A0A017SRB5_9EURO        Unreviewed;      1008 AA.
AC   A0A017SRB5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, 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=EURHEDRAFT_470637 {ECO:0000313|EMBL:EYE99099.1};
OS   Aspergillus ruber CBS 135680.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1388766 {ECO:0000313|EMBL:EYE99099.1, ECO:0000313|Proteomes:UP000019804};
RN   [1] {ECO:0000313|Proteomes:UP000019804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 135680 {ECO:0000313|Proteomes:UP000019804};
RX   PubMed=24811710; DOI=10.1038/ncomms4745;
RA   Kis-Papo T., Weig A.R., Riley R., Persoh D., Salamov A., Sun H.,
RA   Lipzen A., Wasser S.P., Rambold G., Grigoriev I.V., Nevo E.;
RT   "Genomic adaptations of the halophilic Dead Sea filamentous fungus
RT   Eurotium rubrum.";
RL   Nat. Commun. 5:3745-3745(2014).
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; KK088412; EYE99099.1; -; Genomic_DNA.
DR   EnsemblFungi; EYE99099; EYE99099; EURHEDRAFT_470637.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000019804; 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:UP000019804};
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:UP000019804};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1008       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001499557.
FT   DOMAIN      395    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  111112 MW;  4D7B696B44934155 CRC64;
     MKLLTLCAMA SLATQAVSAA IKHKLNGFTI TEHPDPVKRD LLQKYVTWDD KSLSINGERI
     MIFSGEFHPY RLPVPSLWLD VLQKVKALGF NCISFYTDWA LLEGKPGDYR AEGIFALEPF
     FEAAKEAGIY LLARPGPYVN AESSGGGFPG WLQRVNGTLR TADKGFLDAT DNYIATIGAA
     IAKAQITNGG PVILYQPENE YTNGCCGEEF PDPDYFQYVI NQARNAGIVV PMISNDASPD
     GHNAPSTGKG AADIYGHDSY PLGFDCANPS VWPEGNLPTS FWALHEEQSP TTPYSLVEFQ
     AGAYDPWGGP GFAACADLVN HEFERVFYKN NFSFRVAIFN LYMIFGGTNW GNLGHPGGYT
     SYDYGSVLSE TRNITREKYS ELKLFGNFVK VSPSYLLADP GNQTTGYTNT SNLTVTPLKA
     EGLTSYYVVR HTDYSSQAST PYKLRLATSS GNVTVPQLEG ELSLNGRDSK VHVADYNVSG
     TNIVYSTAEV FTWKQFADSK VLILYGGPGE HHELAIASKS EASVIEGSES DINSKHIGSN
     VVISWDVSST RRIIQVDDLK IFLLDRNTAY NYWVPEIPAE GTTPGYSNEK NTASSIIVKA
     GYLVRTAYLK DSGLYLTADF NTTTPIEVIG APESAQALYI NNEKVSHKVD KNGIWTSEVK
     FTAPKIDLPS LEDLEWKYLD TLPEIQSSYD DSAWPKADKP ITDNDHRPLD TPTSLYSSDY
     GFHTGYLVYR GSFVAQGNES TFFIRTQGGQ AFGSSVWLNQ TLLGSWSGLN QDSDNNSTYK
     LPSLQQGKNY VFIVVIDNMG LDENLDVGAD VMKNPRGILN YSLSGRSQDA ITWKLTGNLG
     GEDYQDKTRG PLNEGGLYAE RYGFHQPEPP SADWKSSSPL EGLSKPGIGF YSTNFDLSIP
     SEYDVPIYFN FGNSTDSNPA PFRAQLYVNG YQYGKYVSNI GPQTSFPVPE GILNHRGTNW
     VAVSVWALGK EGARLSSFEL SHERPVKTGL KEVKAAEQPK YEARKRVY
//
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