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Database: UniProt
Entry: W6YQB3_COCMI
LinkDB: W6YQB3_COCMI
Original site: W6YQB3_COCMI 
ID   W6YQB3_COCMI            Unreviewed;      1008 AA.
AC   W6YQB3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=COCMIDRAFT_10271 {ECO:0000313|EMBL:EUC39668.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC39668.1, ECO:0000313|Proteomes:UP000054032};
RN   [1] {ECO:0000313|EMBL:EUC39668.1, ECO:0000313|Proteomes:UP000054032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC39668.1,
RC   ECO:0000313|Proteomes:UP000054032};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
RA   Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
RA   Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
RA   Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
RA   Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
RA   Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector
RT   coding capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR   EMBL; KI964284; EUC39668.1; -; Genomic_DNA.
DR   RefSeq; XP_007693816.1; XM_007695626.1.
DR   EnsemblFungi; EUC39668; EUC39668; COCMIDRAFT_10271.
DR   GeneID; 19118140; -.
DR   KEGG; bor:COCMIDRAFT_10271; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054032; 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:UP000054032};
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:EUC39668.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1008       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004886620.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  109608 MW;  1D81BC642404CEE5 CRC64;
     MKGFAGLGGA VALGCLAVEG AARAVGYTSP TDFIKPYKRG PLQDIVTWDK DSLFVNGERI
     FLYSGEVHPF RLPVPDLHLD VFQKIKALGF NGVSFYVDWA LLEGKPGVYR EEGVFSLQPF
     FDAAKEAGIY LLARPGPYIN AEASGGGFPG WIQRINGTLR TRAPDFLAAT DNYMKNIGAT
     IAKAQITNGG PIILIQPENE YTQATSAIKP FPDPVYMTYV EDQIRNASIV VPLISNDASP
     KGYNAPGTPA PVDIYGHDGY PLGFDCANPT RWPDNNLPTN WQQLHQQQSP TTPYSIVEFQ
     SGSFDPWGGP GFDKCGILVG AEFNRVFYKQ LYSFGVTILN LYMTFGGTNW GNLGHPGGYT
     SYDYAAPIEE DRQVKREKYS ELKLQANFWK VSPEYLTASR GAASTSTWTT SSDLSVTPAH
     GNKTSFYFLR HAKYNSLAST SYQLKISTQA FGNITVPQLN GTSLTLNGRD AKVHVADYDI
     GGTNIAYSTA EIFTWHKYND KTVLIVYGGP GETHELSVEV TGLEILEGDV KSVATRGHTL
     LSFKADATRK VVKLGTESPI YVYLLERNEA FKYWSIDQAP HDASNPVILK AGYLVRTAKV
     TGDALALTGD VNATTPIEII GGATGVSKLT FNGKDISFET SKQGTFTATI DLPKPNISIP
     KLNELEWKYI DSLPEIQPGY DDSKWTVADL KKTYNSLRRL TTPVSLYSSD YGYHTGTLLY
     RGTFTATGNE TTLQLSTQGG SAFGSSAWIG TQFLGSWRGY DAATNGNSTF TLPKLTAGTK
     YTITVVIDNQ GLDENWTIGT ETMKNPRGIL DYKLSGHDAS DVTWKLTGNL GGEDYRDISR
     GPLNEGGLFV ERQGLHLPGA LSASDLDWKP SAGPVTDGIG TPGIGFFATE FELDVPSGYD
     VPLSFTFTNA TSSSAGSSVP AYRVQLYVNG WQYGKYVNNV GPQTKFPVPE GILNYKGTNY
     LGVSLWGLDA GATKIGGFEL KVDAEIWSGL GDVAVVEGEG YEKREGAY
//
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