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Database: UniProt
Entry: A0A010QDV3_9PEZI
LinkDB: A0A010QDV3_9PEZI
Original site: A0A010QDV3_9PEZI 
ID   A0A010QDV3_9PEZI        Unreviewed;      1066 AA.
AC   A0A010QDV3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   25-APR-2018, entry version 21.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CFIO01_04388 {ECO:0000313|EMBL:EXF78042.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78042.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF78042.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF78042.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
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:EXF78042.1}.
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DR   EMBL; JARH01000671; EXF78042.1; -; Genomic_DNA.
DR   RefSeq; XP_007598382.1; XM_007598320.1.
DR   EnsemblFungi; EXF78042; EXF78042; CFIO01_04388.
DR   KEGG; cfj:CFIO01_04388; -.
DR   Proteomes; UP000020467; 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:UP000020467};
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:EXF78042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT   DOMAIN      460    636       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1066 AA;  117102 MW;  291FE318FD3B7A76 CRC64;
     MASSLAPDTC GLPFDYTLQG PAEELRDDTG EATTGSLRYS HARHAVYTGT ATGIPRNENA
     TPFSLDPHIY EPGSYRGGAV 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 TGYSLSSSSA
     FSWVLRNPDT QAGFTVVQQA STKSMTPIQF DVTLNTTAGP VTVPNVVLNG RQSKILVTDY
     VFGKHTLLYA SADIATYGLF DTEVLVFYLQ EGQTGEFAFR DSGDLTFEVF GDTDLQETTN
     GNYSAFTWKQ VAGSTVVKFS NGALVYLLEQ KSAWRFWAPP TTSNPTVKPD EQLFIQGPYL
     VRSASISHGV LHVSGDSDKA TTIEAYVGDK PIETIDWNGL RLAATKTAYG SFTAQIPGAE
     DRAVTLPELS NWRAAEALPE AAPDYDDSRW TVCNKTTTPS PYAPVTLPVL YSSDYGFYSG
     AKIYRGYFDG ANATSVNITA SGGLAFGWSA WVNGQFLGGD VGSASATTTN KTLTFPRAAL
     GEKNNVVTVV VDYHGHDQAS TAQGINNPRG ILGAQLQPGS TRTNTGFKLW KLAGAAGGEA
     NIDPVRGPMN EGGLYPERLG WHLPGFAPTG SSWKPESPLV GLSGAGIRFY VTDFTLNIDS
     DLDAPLGIEF SAPAGTTARV MFWINGYQYG KYVPHIGPQT RFPVPPGVLN NRGRNTLAVS
     LWAQTDAGAK LDGLKLVRYG QYQTDFKFNR DWTYLQPGWE DRQEYA
//
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