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Database: UniProt
Entry: A0A066XW05_COLSU
LinkDB: A0A066XW05_COLSU
Original site: A0A066XW05_COLSU 
ID   A0A066XW05_COLSU        Unreviewed;       957 AA.
AC   A0A066XW05;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CSUB01_09200 {ECO:0000313|EMBL:KDN69951.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN69951.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive
RT   pathogen of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(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}.
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:KDN69951.1}.
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DR   EMBL; JMSE01000431; KDN69951.1; -; Genomic_DNA.
DR   EnsemblFungi; KDN69951; KDN69951; CSUB01_09200.
DR   OMA; EFEGGWF; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000027238; 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:UP000027238};
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:KDN69951.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    957       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001630743.
FT   DOMAIN      350    526       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   957 AA;  105911 MW;  66AC45F46B15E733 CRC64;
     MRLFRALTAL IWLFVSDSLA TNNGLTDMVS WDKYSVMVKD TRTYILSAEF HYQRTPDILQ
     KFKANGFNAV SIYFFWSYHS ASEGVYDFET GGKNTQRLFD YCKEAGLYVI ARAGPYCNAE
     TSGARSSDER YRAGWLPFVT RIGKIIAANQ ITNGGPVILN QVENEYQQTV YQADHTSVIY
     MEQLEKAFRD AGIVVPLTHN EKGMRSRISW STDYNNVGGA VDMYGLDNYP GALSCTDITV
     GFNVNRGYYQ WLQNAAITQP GYLAEFEGGW FSNWGSPTFY DECASEHDPA FADVYYKNNI
     GQRITLLNIY MAYGGTNWGH YDAPLRETRE QGAKLFQTKL LGLFTRVSFD LLKTDMVGNG
     TGYSLSSTSA FSWVLRNPDT QAGFTIVQQN STNSMSPIQF DVKLNTTAGS VTVPNFVLNG
     RQSKILVTDY AFGKHTLLYA SADIATYGVF DTEVLVFYLE EGQTGEFAFK DGRDLTFEVF
     GDVVLEETTN GDHAAFMWKQ AAGSTVIKFS SGVLVYLLER KTAWRFWAPP TTSNPTVKPS
     KQLFFLGPYL VRSASISHGV LHISGDSDRS TTLEAYVGDE PIEPIDWNGK RLAATRTPYG
     SFTVRIPGAE DRVVSLPELK NWRAAEALPE AAPDYDDSRW VVCNKTATPS PYAPVTLPVL
     YSSDYGFYSG AKIYRGYFDG ANATSVNITA SGGLAFGWSA WVNGQFLGGD VGSASTTTTN
     KTLAFPRGAL RASNNVVTVV VDYHGHDQAS TAQGINNPRG ILGAQLQPGS ERADNTGFKM
     WKLTGAAGGE TNIDPVCGPM NEGGLYPERL GWHLPGFAPT GSSWKPETPL DGLSRAGIRF
     YVTDFTLNVD SDLDAPLGLE FSAPAGTTVR VMFWINGYQY GKFVPHIGPQ TRFPFPPGVL
     NNRGRNTLAV SLWAQTDAGA KLDGLKLVRY GQYHTDFKFN RDWSYLQPGW KDRREYA
//
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