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Database: UniProt
Entry: A0A135TY17_9PEZI
LinkDB: A0A135TY17_9PEZI
Original site: A0A135TY17_9PEZI 
ID   A0A135TY17_9PEZI        Unreviewed;       986 AA.
AC   A0A135TY17;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CSIM01_10931 {ECO:0000313|EMBL:KXH52993.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH52993.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH52993.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH52993.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) 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:KXH52993.1}.
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DR   EMBL; JFBX01000030; KXH52993.1; -; Genomic_DNA.
DR   EnsemblFungi; KXH52993; KXH52993; CSIM01_10931.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070328; 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:UP000070328};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KXH52993.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    986       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007804397.
FT   DOMAIN      380    556       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   986 AA;  108562 MW;  387B8A653B76650E CRC64;
     MRFHRALTAL IWLFASGAWA TDNGLTDVVS WDKYSLVIND TRTYILSAEF HYQRTPVPEL
     WPDILQKFKA NGFNTVSIYF FWSYHSAAEG VYDFETAGKN IQRLFDYCKE AGLYVIARAG
     PYCNAETNGG GLALWGSDGR FGKIRTSDER YQAGWLPFIT QVGKIIAANQ ITNGGPVILN
     QVENEYQESV YSPDHTSVIY MEQLKKAFHD AGIVVPLTHN EKGMRSRSWS TDYNNVGGAV
     NVYGLDSYPG ALSCTDPTVG FNVVRTYFQW FSNYSFTQPS YLAEFEGGWF SNWGSPTFYD
     QCASEHDPAF ADVYYKNNIG QRVTLLSIYM SYGGTNWGHS AAPQVYTSYD YSAPLRETRE
     QWTKLFQTKL IGLFTRVSSD LLKVEMIGNG TGYGLSSSSA FSWVLRNPDT QAGFTVVQQA
     STKSMTPIQF DVTLNTTAGP VTVPNVVLNG RQSKILVTDY VFGKHTLLYA SADIATYGLF
     DTEVLVFYLQ EGQTGEFAFK DAGDLTFEVF GDTDLQETTN GNHSAFTWKQ VAGSTVVKFS
     NGALVYLLEQ KSAWRFWAPP TTSNPTVKPD EQLFIQGPYL VRSASISHGV LHISGDSDKA
     TTIEAYVGDK PIETIDWNGL RLAATKTAYG SFTAQIPGAE DRAVTLPELS NWRAAEALPE
     AAPDYDDSRW TVCNKTTTPS PYAPVTLPVL YSSDYGFYSG AKIYRGYFDG ANATSVNITA
     SGGLAFGWSA WVNGQFLGGD VGSASATTTN KTLTFPRSAL VEKNNVVTVV VDYHGHDQAS
     TAQGINNPRG ILGAQLQPGS TRTNTGFKLW KLAGAAGGEA NIDPVRGPMN EGGLYPERLG
     WHLPGFAPTG SSWKPESPLV GLSGAGVRFY VTDFTLNIDS DLDAPLGIEF SAPAGTTARV
     MFWINGYQYG KYVPHIGPQT RFPVPPGVLN NRGRNTLAVS LWAQTDAGAK LDGLKLVRYG
     QYQTDFKFNR DWSYLQPGWK DRQEYA
//
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