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Database: UniProt
Entry: A0A010RML3_9PEZI
LinkDB: A0A010RML3_9PEZI
Original site: A0A010RML3_9PEZI 
ID   A0A010RML3_9PEZI        Unreviewed;       993 AA.
AC   A0A010RML3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CFIO01_05007 {ECO:0000313|EMBL:EXF79219.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF79219.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF79219.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF79219.1,
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:
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:EXF79219.1}.
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DR   EMBL; JARH01000561; EXF79219.1; -; Genomic_DNA.
DR   RefSeq; XP_007597111.1; XM_007597049.1.
DR   EnsemblFungi; EXF79219; EXF79219; CFIO01_05007.
DR   KEGG; cfj:CFIO01_05007; -.
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:EXF79219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    993       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001457173.
FT   DOMAIN      387    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   993 AA;  110075 MW;  EFB69CC7136D332C CRC64;
     MLLSRLKALS LLALAWLDGV HARAIGTDLK LLNGRQQDIV TWDDKSLFIN GERLMIFSAE
     FHAFRMPVPS LWLDILQKIK AAGYNSVSFY VNWGLLEAKP GEVRAEGIFA LEPLFEAAEK
     AGLYLFARPG PYINAEVTGG GFPGWLQRVQ GALRTSDEAY LKATDNYTAT LGSIIAKAQI
     TNGGPVVLFQ MENEYNAAID PYPFPDYDYW KYVDNQFRSH GVVVPYVNNE AWQLGAITAL
     TPAKVDIYGH DGYPLGFDCW NPTIWPENGL PTDWLTTNNA IAPTTPYTIV EFQGGGFQPW
     GGAGFEYCAA LLNHEFERVL YKNNYAVGVT IFNIYMTWGG TNWGNLGHSD GYTSYDYGAQ
     ITEERLVNRE KYSETKLQSN FLHVSPAYLV ADRFNASLEW TNHAAITVTP ATTNTTKFYI
     TRHTKYDSLE TTAYKLKVKT VKYGELEVPQ LSDSLYLTRR DSKIHVSDYP VGDKSLVYST
     AEIFTWKKYA DKTVLVVYGG ADEHHELAIE GEQADVTDAN VIEGSDVTIE QKDGYTVLGW
     AVSDERKVVR VHENFYVYLL TRNEAYNFWV PPAVGDFGTS DVIVKAGYLV RNVAVNGDSI
     SFSGDVNSTT AIEIIGGAPS SLKTLNFNGK SLDFKQDDHG AVTAKVEFST PEIKLPCISQ
     LSWKYVDSLP EIKSDYSDES WTAADLEKTF NTANPLKTPT SLYGGDYGYH TSSLLYRGHF
     TANGDETTFN ITTQGGNAYG ASVWLNDEFI GSWVGNAVSP AYNSTFTLPQ LTKDTDYVFT
     VVVDHMGLNG NWVVGEEQQK NPRGILNYNL AGHEQSDIKW KITGNLGGED YADEERGPLN
     EGGLFIERQG YHWPQPPSAS WEDSKGPSAG IEKPGIAYYS ATFDLDLPTG FDIPLSLTFA
     NTTATAYRAQ IFVNGYQFGK FVHHVGPQAR FPIPEGILNY QGSNHLGITL WAMEKGGAKV
     EGLKWEVGMV SATGFGKVTP APQPKWTERK GAY
//
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