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Database: UniProt
Entry: A0A1Q5UKI5_9EURO
LinkDB: A0A1Q5UKI5_9EURO
Original site: A0A1Q5UKI5_9EURO 
ID   A0A1Q5UKI5_9EURO        Unreviewed;      1011 AA.
AC   A0A1Q5UKI5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENSUB_1351 {ECO:0000313|EMBL:OKP12969.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP12969.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKP12969.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP12969.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OKP12969.1}.
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DR   EMBL; MNBE01000165; OKP12969.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000186955; 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:UP000186955};
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:UP000186955};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012637740.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  109694 MW;  0E8C80BC0C47C8C2 CRC64;
     MKLVSSWVVA ALAAQAASAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE HSLFINGERL
     MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA LLEGNPGHYS AEGIFDLQPF
     LDAAKGAGIY LLARPGPYIN AEVSGGGFPG WLQRVNGTLR TSDAAYLKST DNYASNIAAT
     IAKAQITNGG PVILYQPENE YSGACCGVSN FPDGSYMQYV ENQAREAGIV VPFINNDAWT
     GAHNAPGSGA GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFYNSHEQQS PSTPYSLVEF
     QGGAFDPWGG VGFAGCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN WGNLGHPGGY
     TSYDYGAAIS ESRDITREKY SELKLLGNFA KVSPAYLVAN PGSLTTSAYT NNANLAVTPL
     LGSNSSASSF FVIRHSDYTS QASAQYKLTV PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY
     DVAGTNILYS TAEVFTWKKI NNEKVLVLYG GPSEHHEFAV SGESSSSVVE GSSSGISSKE
     VSNALVVAWD TSSTRRIVQV GNLKVFLLSR NSAYNYWVPQ LPTKGKSPGF SNQETTASSI
     IIKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK KLVINGEKTQ FKVDKNGIWS
     TSVTYNAPKV RLPDLKKLKW NSIDTLPELK NTYDDSDWAT ADQAYTKNTA YPLKTPTSLF
     ASDYGFNTGT LLYRGHFAAN GKEKTFFVQT QGGSAYGHSV WINETYVGSW AGNSIDSNHT
     ATYTLPTLQS GNNYVITVVI DNMGLDENWI IGLEAMKSPR GILQYSLSGQ EASAISWKLT
     GNLGGENYRD TVRGPLNEGG LYAERQGFHQ PQPPTKGWGS NSPFTGLSKP GIHFYSASFD
     LDLPSGYDIP VYFNFGNDTS TPGEYRVQLY VNGYQYGKYV NHIGPQTSFP VPEGILNYCG
     TNWVALSLWA HGDNGAKLDS FELINTTPVL TSLGKVKSVN QPKYQARKGA Y
//
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