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Database: UniProt
Entry: A0A093V867_TALMA
LinkDB: A0A093V867_TALMA
Original site: A0A093V867_TALMA 
ID   A0A093V867_TALMA        Unreviewed;       999 AA.
AC   A0A093V867;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-FEB-2019, entry version 23.
DE   SubName: Full=Putative beta-galactosidase C {ECO:0000313|EMBL:KFX46159.1};
GN   ORFNames=GQ26_0201240 {ECO:0000313|EMBL:KFX46159.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX46159.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular
RT   Mechanisms of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(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|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:KFX46159.1}.
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DR   EMBL; JPOX01000020; KFX46159.1; -; Genomic_DNA.
DR   EnsemblFungi; KFX46159; KFX46159; GQ26_0201240.
DR   Proteomes; UP000029285; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029285};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029285};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    999       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001888893.
FT   DOMAIN      380    556       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   999 AA;  110443 MW;  D12AC1A1C8911807 CRC64;
     MFFFRFLTTV LLLFNAKLLV AQSSNTSSPV HWDKYSLSIN GERLFVFAGE FHYIRLPVPE
     LWLDVFQKLK ANGFNAISVY FYWNHHSASE GVYDFETGGH NVQRLFDYAK QAGVYIIARP
     GPYANGELSA GGYALWAANG RLGGERTRDS QYYDLWSPWM TKIGKIIAAN QITEGGPVIL
     VQHENELQET THRANNTLVL YMEQITQILD AAGIVVPSTH NEKGMRSMSW SMDYEDVGGA
     VNIYGLDSYP GGLSCTNPNA GFNLIRTYYQ WFQNYSYTQP EYLAEFQGGY FTPWGGVFYD
     DCASMLQPEY ADVFYKNNIG NRVTLQSLYM AYGGTNWGHI AAPVVYTSYD YSAPLRETRE
     IRDKLKQTKL LGLFTRVSPD LLQTEMEGNG TSYTTGANIF TWALRNPETN AGFYVVAQDD
     SSSTTDVVFD LEVETSAGSV NITNIGLDGR QSKIITTDYK VGDTTLLYCS ADILTYATLD
     VDVLALYLNK GQTGTFVLAN AASHLKYTVY GNSTVTSSNS SQGTIYTYTQ GQGISAIKFS
     NRFLVYLLDK YTAWDFFAPP LQLSDPNVKP NEHIFVIGPY LVREATIKGR TLELTGDNQN
     TTSIEIYHGN PFITSITWNG KHLSTKRTAY GSLTATIPGA EAITITLPKL TSWKSHDMIP
     EIDPEYDDSN WVVCNKTTSF NAIAPLSLPV LYSGDYGYHA GPKIYRGRFG STNATGVTVT
     AQNGNAAGWS AWLNGIYIGG VTGDPSIEAT SAVLKFNSST TLKQEGSENV LIVLVDYTGH
     DEDNVKPARA QNPRGLLGVI FEGSTSTNFT SWKLQGNAGG EKNIDALRGP MNEGGFYGER
     LGWHLPGFEP STKSGWDTRA PSDGVDGGSH RFYITEFTLD LGPNSHALDV PIGIHLNASS
     TSGPAVAYVW LNGYKFAHYL PHIGPQTVFP FQPGVLNIQG SEGHKRKNTL AVSLWALTDQ
     PAALDVVELV AYGKYTSSFD FARDWSYLQP RWVDRSKYA
//
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