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Database: UniProt
Entry: A0A0F4Z133_TALEM
LinkDB: A0A0F4Z133_TALEM
Original site: A0A0F4Z133_TALEM 
ID   A0A0F4Z133_TALEM        Unreviewed;      1008 AA.
AC   A0A0F4Z133;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, 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=T310_1743 {ECO:0000313|EMBL:KKA24204.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA24204.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA24204.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA24204.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z.,
RA   Wu L., Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) 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:KKA24204.1}.
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DR   EMBL; LASV01000072; KKA24204.1; -; Genomic_DNA.
DR   RefSeq; XP_013330816.1; XM_013475362.1.
DR   EnsemblFungi; KKA24204; KKA24204; T310_1743.
DR   GeneID; 25314094; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053958; 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:UP000053958};
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:UP000053958};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1008       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002482102.
FT   DOMAIN      394    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  109998 MW;  5BF1140B444BB3D9 CRC64;
     MKLLSSFAAA YLAVQAAGAA VSPRPNGYTI TEHPDLEQRA QLQNIITWDN QSLYINGERI
     MILSGEMHPY RLPVSSLYLD LFQKVKALGF NCVSFYVDWA LLEGKPGTYR ADGIFGLEPW
     FDAASKAGVY LLARPGPYIN AESSGGGFPG WLQRITGTLR TRAPDYMNAT KNYATNVAAT
     LAKAQITNGG PVILYQPENE YTGFTNGQQF DPQYMQDVMD TARAAGIVVP FINNDAAPDG
     HDAPGSGVGA VDIYGHDSYP LGFDCANPTS WPSNGLPTNF RQLHLEQSPS TPYSLVEFQG
     GAFDPWGGSG YDKCTALLNQ EFERVFYKNN LAAGVAIMNF YMIFGGTNWG NIPYPGVYTS
     YDYGSAISES RNVTREKYSE LKLFANFIRA SPSYLDTVPQ NASTGVYTDT TDLTVTPLVG
     RSSASSFYVV RHTDYTSEAS TSYKLKLPTS AGQLTIPQLG GSLTLNGRDS KIHVTDYDVA
     GTNILYSTAE VFTWKNFTDY KVLLVYGGPN EHHELAISSK ANVSVVEGSS SGVTIKSLDG
     TAVIGWDVSS TRRILKVDNL LVFLLDRNSA YNYWVPELST NGPTPGFSSP ETTANSIVVK
     AGYLVRTVYL QGSELHLTAD FNSTTPVEVI GVPKTAKSLY INGAQYKPTV NANGFWSTTV
     TYDSPDIKLP SLKDLEWRYV DSLPEIQPSY DDSAWVAADH KTTNNSVAPL KTPTSLYASD
     YGFHTGSLIY RGHFVATGNE TTFTVHTQGG SAFGSSVWLN QTYLGSWTGD SASSDNNSTY
     KLPKLSAGKP YVLTVVVDNM GLEEDWTVGS EQMKEPRGIL DYQLSGRSQS AISWKLTGNL
     GGEDYQDLVR GPLNEGGLYA ERQGWHQPEP PSQQWKSSSP LEGISQAGVG FYSASFDLNI
     PSGWDVPLYF TFGNTTTPPE AYRAQLYVNG YQFGKYVNNV GPQTAFPVPQ GILNYQGTNW
     VAVTLWAQQS EGAKLDNFEL VAETPVLTAL TGITSSPQPK YTKREGAY
//
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