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Database: UniProt
Entry: B8MPA3_TALSN
LinkDB: B8MPA3_TALSN
Original site: B8MPA3_TALSN 
ID   B8MPA3_TALSN            Unreviewed;       663 AA.
AC   B8MPA3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   28-FEB-2018, entry version 50.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=TSTA_105530 {ECO:0000313|EMBL:EED14342.1};
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:EED14342.1, 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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; EQ962658; EED14342.1; -; Genomic_DNA.
DR   RefSeq; XP_002486580.1; XM_002486535.1.
DR   ProteinModelPortal; B8MPA3; -.
DR   STRING; 441959.XP_002486580.1; -.
DR   EnsemblFungi; EED14342; EED14342; TSTA_105530.
DR   GeneID; 8100412; -.
DR   EuPathDB; FungiDB:TSTA_105530; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; B8MPA3; -.
DR   OMA; GWGKGIV; -.
DR   OrthoDB; EOG092C23N6; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 3.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 2.
DR   PIRSF; PIRSF006336; B-gal; 2.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   ProDom; PD001821; CBD_fun; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 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};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    663       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002877617.
FT   DOMAIN       16     52       CBM1. {ECO:0000259|PROSITE:PS51164}.
FT   ACT_SITE    214    214       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    291    291       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   663 AA;  71693 MW;  77A2A75D0D67A4CC CRC64;
     MKLSTSLITL IATVQAQQTA WGQCGGTGWT GPTACVSGWT CNYVNPYYSQ CIEGQSTSSS
     PSTTSTPSTT TSPVSSSSSS SSSAIPFSYN SKSFLLNNQP FQIIGGQMDP QRIPRAYWRQ
     RLQMARAMGL NTVFSYVYWH SLEPSQGVFD FTGNNDLITW FQTVQEVGLK AVLRAGPYPF
     LTAASSYMQR LAQELHDQQT TQGGPIIMVQ VENEYGNYGS DHSYTQVIGN IFKQNWQVTL
     YTNDGGNQGA LSGGQIPGIL AEIDGNPQGG FAARNQYVTD QSSLGPLLDG EYYVTWFDTW
     GPHSGYSTDE GNQGAINGVI NDLSWILSNN DSFSIYMFHG GTSFGYGNGG ENYGNLTPFI
     TSYDYGAPLD ESGRITPIYN DIRNMISNHV PSGTIPSVPS VPTMWSMPTT TLQPVARLFD
     QLPSATNSSL PQTMEQLGQS FGYVLYSHQA TSSISGAVKS GDHARDRVIV YKNGVKQGVI
     DSIYSHPATV NVQLSSGDTL WLLVENLGRV DYGSPIVDQR KGIVGNVTIG GSVISNWEIY
     SYPLNTPPST VDTSNSSISI PSGSQPVFYK GSFVAPSSDS ASDTYLTLPG GIKGVVWVNG
     NNLGRYWIIG PQQSLYLPGC FMKTGSNEIV VLELEPQAGT RVAYGVTSRT WGNNPDPDCN
     NCS
//
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