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Database: UniProt
Entry: A0A084R123_STAC4
LinkDB: A0A084R123_STAC4
Original site: A0A084R123_STAC4 
ID   A0A084R123_STAC4        Unreviewed;      1007 AA.
AC   A0A084R123;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 20.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=S40285_07457 {ECO:0000313|EMBL:KFA69908.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Stachybotryaceae;
OC   Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA69908.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA69908.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA69908.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene
RT   clusters in the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(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; KL659328; KFA69908.1; -; Genomic_DNA.
DR   EnsemblFungi; KFA69908; KFA69908; S40285_07457.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000028524; 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:UP000028524};
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:UP000028524};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1007       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001779934.
FT   DOMAIN      392    580       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1007 AA;  111705 MW;  034EE5886DB80D00 CRC64;
     MLFSRPLQAL SVALSLIAGS QARVVSNDDL GVQLLNARQQ DIVTWDDHSL FVNGERLMVL
     SGEIHPFRMP VQALWLDVLQ KVKASGYSAV SIYINWHLLE AKRGEFRANG IFSLEPFFEA
     AQKAGLYIIA RPGPYINAEV SGGGFPGWLT RVPGALRTNT DEFIEATDLY TSEIGSIIEA
     AQITNGGPVL LFQLENEYQH AMPGYPMPEY EYWQSVTDQY RNASIVVPYI NNEAHMYGWI
     TAHTPASVDI YGFDGYPLGF DCENPSMWPD NGLPTDWLAV NNELAPDTPL TIPESKFQGG
     GFQHWGQAGF ENCALLLNME FERVLYKNNY AAGATIFNIY MVFGGTNWGN LGHADGFTSY
     DYGAQITEER QLWREKYSEV KLQANFFHVS PAYLEADRFN ASLEYTNNDA ITVTPATTDT
     TKFYISRHTE YDTTSAVPYK LRVSTVNHGD IEIPQLGGDL ILTRRDSKIH VSDYPVGDEH
     LIYSSAEVFT WKKYDDKTVL VLYGGPNEHH EIAVEGRSGN DKRQEGFEVE GENVTVEQAA
     DGDYTIISWD ISDDVEDRKV VRVNGNFYIY MLNRNEAYNF WVPPTGSGSD FGTSDIILKA
     GYLIRTAQRE GQIINLVGDV NATTPIEIIG GAPDGLESLT FNGEPLEFEQ NALGVVTATV
     DFVAPEISLP CFSQMEWKKV DSLPEISADY DDSDWVDANF EVSPNDAFPP TTYVSLYASD
     YGFHAGSVLF RGHFTANGEE TTFNLTTQGG RAFGASVWLG STFVGSWVGE SQSHFASVLL
     ELPELEAGED YVFTIVMDHM GLNGNYVIGE DNLKTPRGIL EYDLAGHEAS DIRWKITGNL
     GGEDYADLIR GPLNEGGMFA ERQGFHQPSP PSSDWETGRP TEGVSEPGIT FYTASFDLDL
     PRGYDIPLAI RFDRDVSAGA FRVQLFVNGY QYGKFIPHIG PQARFPIPEG ILNHHGQNTI
     GLTIWALEEG GAKLNGMGWD VSMATMTGFG EIELAPAPEW EEREGAY
//
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