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Database: UniProt
Entry: S0EGQ2_GIBF5
LinkDB: S0EGQ2_GIBF5
Original site: S0EGQ2_GIBF5 
ID   S0EGQ2_GIBF5            Unreviewed;      1002 AA.
AC   S0EGQ2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   16-JAN-2019, entry version 32.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=FFUJ_09341 {ECO:0000313|EMBL:CCT73835.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
OS   (Bakanae and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT73835.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J., Huss K., Michielse C., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K.,
RA   Bald T., Wingfield B., Ophir R., Freeman S., Hippler M., Smith K.M.,
RA   Brown D.W., Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U.,
RA   Guldener U., Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice
RT   pathogen Fusarium fujikuroi reveal complex regulation of secondary
RT   metabolism and novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(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; HF679031; CCT73835.1; -; Genomic_DNA.
DR   ProteinModelPortal; S0EGQ2; -.
DR   EnsemblFungi; CCT73835; CCT73835; FFUJ_09341.
DR   Proteomes; UP000016800; Chromosome 9.
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:UP000016800};
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:UP000016800};
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_5004496000.
FT   DOMAIN      389    565       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  110421 MW;  C05ECBE880623E43 CRC64;
     MKLSNFFLVA LAASTHAQNV LPRGTRPSNI LDSRALLQDV VTFDEHSLFI RGERVTIFSA
     EIHPFRLPVA SLYPDLFQKV KAMGFNMVSF YVDWALLEGK PGEFRSEGAL DLQPFIDAAH
     EAGIYLLARP GPYINAEVSG GGFPGWLQRV KGLLRTNATD YLEATDNYVA HVAKIIAKAQ
     ITNGGPVILY QPENEYSAAQ GTPFPNHDYL KYVNDQVRKA GVVVPLINND AWPGGTGAPG
     TGPGAVDIYG HDGYPVGFDC KNPYNWPKDG LPTTWHAEHE KISPNTPYSI VEFQGGAFDP
     PGGYGFSNCY ELTNHEFARV FYKNNIAAGV TIFNIYMTWG GTNWGNLGHS DGYTSYDYGA
     AIKEDRTIAR EKYSEIKLQG QFLRVSPNYA IAEASNFTTT EYTDNKNIAV TALTTKKDDA
     FYVVRHADYR TTDSASYKLR VKTSAGTLTI PQLGGSLSLH RRDSKIHVVD YPVGKYKLLY
     STAEVFTWKV LGDKTVLVLY GGPDEAHEVA VKGQETLKVV EGDGVKIEKK KGAGVFQFKT
     STKRRVVQAG SLYIYLLDRN AAYKYWVPTI PSKKSGEYGS SAMNPDAVII NGPYLVRSVA
     VEGSKLSVQA DFNTTTAVEI IGAPKGTSRL SINGKDTSFT KSKLGNWLVN PDIKLPTVKV
     PDLKSLDWHY IDGLPEVKKD YDDSKWRTAD IKNTFNSKWP LNNSVSLYSG DYGFNAGALI
     FRGHFTASGS ESKLKLWTFG GRAYGSSVWL DDKFLGSVTG RGNNNNDTST YKLPKTEKGK
     KHIVTVIVDN MGLNGNWVPG VDESKQPRGI LDWHITSDSG KETKVTKWKI TGNLGGENYK
     DKFRGPLNEG GFFFERQGYH LPSPPLTSFK PGSPFKGLSK PGVSFFTAKL QFNLPSSTHD
     IPLSFTFKNN TSSTGAYRAI LYVNGFQYGK YVANVGPQTD FPVPEGIWNY KGDNWIGIAL
     WALEKSANVD GLSLTAGVPV QTGRKPVKVV EGPKYSRRQD AY
//
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