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Database: UniProt
Entry: B8M3B6_TALSN
LinkDB: B8M3B6_TALSN
Original site: B8M3B6_TALSN 
ID   B8M3B6_TALSN            Unreviewed;      1011 AA.
AC   B8M3B6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=TSTA_095370 {ECO:0000313|EMBL:EED22288.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 /
OS   NRRL 1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22288.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomeA.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962653; EED22288.1; -; Genomic_DNA.
DR   RefSeq; XP_002479251.1; XM_002479206.1.
DR   ProteinModelPortal; B8M3B6; -.
DR   STRING; 441959.XP_002479251.1; -.
DR   EnsemblFungi; EED22288; EED22288; TSTA_095370.
DR   GeneID; 8103864; -.
DR   EuPathDB; FungiDB:TSTA_095370; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; B8M3B6; -.
DR   OMA; GGEDYVD; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000001745; 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:UP000001745};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888, ECO:0000313|EMBL:EED22288.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:EED22288.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002877261.
FT   DOMAIN      397    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  109983 MW;  1494FFD16029299F CRC64;
     MKFLLGTTVA ALACLSGQAL GRAVSHRSKP LTVLGHPDIE RRALLQDIVT WDNQSLYIHG
     EKLMIFSGEV HPFRLPVASL YIDIFHKIKA LGFNTVSFYV DWALLEGKPG TYRAEGIFDL
     QPFFDAAKQA GIYLLARPGP YINAEVSGGG FPGWLQRVNG TLRTRDPAYF DSTKNYANHI
     AGTIAKNQIT KGGPIILYQP ENEYSGWATG YSDDPQYMQD IEDTARNAGV IVPFISNDAG
     AYGHNAPGSG VGAVDIYGHD SYPLGFDCAN PSTWPAGDLP TYFRQTHVQQ SPSTPFSLVE
     FQGGSFDPWQ GPGFAKCTAL LGPEFERVFY KNNIAAGAVF LNLYMTFGGT NWGNLGYPDG
     YTSYDYGSAI SESRNITREK YSQLKLIGNF LKVSPSYLDA VPGSASNSTY SSTSALTVTP
     LIGRSTKSSF FVVRHSDYSS LASTSYTLKV PTSAGVLTLP QLSGSLSLNG RDSKIHVTDY
     NVAGTNILYS TAEVFTWKNF SDYKALVLYG GPGEHHELAI SSSSNAQISV VDGSKSGVTT
     KIQNGQAIIA WDVSSSRRVV KVDDLLVFLL DRNSAYSYWV PQVSTSNSSV EFSSQETVAN
     SIIVNAGYLV RYAYLQGNEL HLSADFNATT NVEVIGAPPS ATRLFVNGVQ YDHAKTSNGF
     WTASVKYNAP KISLPDFSKL TWKYVDSLPE IQATYDDSAW ISANHDWTNN TANPLKTPVS
     LYASDYGFNT GHLLYRGHFV ANGNEKYFNV QTIGGSGFGS SVWLNDKLLG SWTGSANNDS
     AASSYTLSAL KAGSSYNLTI LVANTGLEED WTVGTETMKT PRGILNFDLS GHSQSDVTWK
     LTGNLGGEDY VDLARGPLNE GGLYAERQGW HQPSPPSSDW KTSSPLEGIS QARVGFYSTS
     FTLDLPEGYD IPLYFAFGDS SGSLYRAQLY VNGYQYGTYV PQLGPQTEFP VPQGILNYQG
     ENWVAITLWA QESSGAKVDS FELINTTPVL TALTGIESSP QPAYSQRKGA Y
//
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