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Database: UniProt
Entry: X0C4Y9_FUSOX
LinkDB: X0C4Y9_FUSOX
Original site: X0C4Y9_FUSOX 
ID   X0C4Y9_FUSOX            Unreviewed;      1002 AA.
AC   X0C4Y9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=FOQG_07579 {ECO:0000313|EMBL:EXK89480.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK89480.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK89480.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK89480.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; JH658377; EXK89480.1; -; Genomic_DNA.
DR   EnsemblFungi; EXK89480; EXK89480; FOQG_07579.
DR   Proteomes; UP000030663; 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:UP000030663};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1002       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004937373.
FT   DOMAIN      389    565       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  110028 MW;  4C564D187CE3D765 CRC64;
     MKLSNFFFAA LAASSHAKNV LPRGTRPSNI LDSRALLQDI VTFDEHSLFI HGERVTIFSA
     EIHPFRLPVA SLYPDLFQKV KAMGFNMVSF YVDWALLEGK PGEFRSEGAL DLQPFIDAAH
     DAGIYLLARP GPYINAEVSG GGFPGWLQRV KGFLRTNATD YLAATDNYVA HVAKIIAKAQ
     ITNGGPVILY QPENEYSAAQ GTPFPNHDYL KYVNDQVRKA GVVVPLINND AWQGGTGAPG
     TGPGAVDIYG HDGYPVGFDC ANPYTWPKDG LPTTWHAEHE KISPNTPYSI IEFQGGGFDP
     PGGGGFDNCY ELTNHEFARI FYKNNLAAGV TIFNIYMTWG GTNWGNLGHS DGYTSYDYGA
     AIKEDRTITR EKYSEIKLQG QFLRVSPNYA IAEASNFTST KYTDNKNIAV TALTTKKDDA
     FYVVRHADYR TTDSASYTLK VKTSTGTLTI PQLGGSLSLH RRDSKIHVVD YPVGKFKLLY
     STAEVFTWKV LGDKTVLVLY GGADEVHEVA VKGQEKVKVV EGDGVKIEKK NGAVVFQFKT
     STKRRVVQAG SLYIYLLDRN AAYKYWVPTI PSKKSGEYGS SVMNPDAVII NGPYLVRSVA
     VEGSKLSVQA DFNITTPVEI IGAPKGTSRL SINGKDTSFT KSKLGNWLVN PEIKLPTVKV
     PDVKSLDWHY IDGLPEVKKD YDDSKWRTAD IKKTLNSKWP LNNSVSLYSG DYGFNAGALI
     FRGHFTASGS ESKLKLWTFG GRAYGSSVWL DDKFVGSVTG GGNNNNDTST YKLPKTEKGK
     KHVVTVIVDN MGLNGNWVPG VDETKQPRGI LDWHITSDSG KETKVSKWKL TGNLGGENYK
     DKFRGPLNEG GFFFERQGYH LPSPPLTSFK SGSPFKGLSK PGVSFYTAKL PLNLPSSTHD
     IPLSFTFKNN TSSTGAYRAI LYVNGFQYGK YVANVGPQTV FPVPEGILNY KGDNWIGIAL
     WALEKSANVD GLSLTAGVAV QTGRKPVKVV EGPKYSRRQD AY
//
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