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Database: UniProt
Entry: A0A0M9ER54_FUSLA
LinkDB: A0A0M9ER54_FUSLA
Original site: A0A0M9ER54_FUSLA 
ID   A0A0M9ER54_FUSLA        Unreviewed;      1007 AA.
AC   A0A0M9ER54;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=FLAG1_08977 {ECO:0000313|EMBL:KPA38189.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA38189.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA38189.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA38189.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A.,
RA   Kolseth A.-K., Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2
RT   mycotoxin producer.";
RL   Submitted (APR-2015) 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:KPA38189.1}.
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DR   EMBL; JXCE01000305; KPA38189.1; -; Genomic_DNA.
DR   EnsemblFungi; KPA38189; KPA38189; FLAG1_08977.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000037904; 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:UP000037904};
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:UP000037904};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1007       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5005835325.
FT   DOMAIN      393    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1007 AA;  110777 MW;  2846C01225C36208 CRC64;
     MKLSNLFLAA LAAGSCHATN IIPRGGRPSS IINNAHKREL LQDIVTFDQH SLFINGERVT
     MFSAEIHPFR LPVPSLYLDL FHKVKALGFN MVSFYVDWAL LEGKPGEFRS EGSLDLQPFI
     DAAQEAGVYL LARPGPYINA EVSGGGFPGW LQRVTGFLRT NATDYLASTD NYVAKVGAII
     AKAQITNGGP VILYQPENEY SAAEGTPFPN HDYLEYVNDQ VREAGIVVPL INNDAWQGGT
     GAPGTGPGAV DIYGHDGYPV GFDCTNPYKW PKDGLPTTWH AEHLDKSPNT PYSIIEFQGG
     AFDPPGGTGF DKCYELTNHE FARVFYKNNL AAGVTIFNIY MTWGGTNWGN LGHSDGYTSY
     DYGAAIREDR TITREKYSEI KLQGQFLAVS PNYAVATASN FTTTKYTSNN KIAVTALTTK
     NDDAFYVVRH ADYRTTSSAS YMLKVKTSAG QLTIPQLGGS LSLHGRDSKI HVVDYPVGKY
     KVLYSTAEVF TWKDLGDKTV LVLYGGPNEL HEVAIKTDSK LKVIEGDEVK TERRRGASVF
     QFKTSSKRSV VQIGSLHIYL LDRNSAYNYW VPTIPEKGDR AAFGSSVMNP KAVIFNGAHL
     IRSIDIEGSK LSVQADFNTT SPLEIIGAPE GTSRLVINGK GTPYKKSKIG NWLVNPAVEL
     PDVKITDLKS LDWKYVDSLP EVKKDYDDAK WPDADLKKTY NSKWPLNNSV SLYGGDYGFH
     SGALLFRGHF TAGGSESKFK VWTFGGLSYG SSVWLDDKFL GSVVGSGRGN NDTFTYSLPK
     MQKGKKYVLT IIVDNMGLNG NWVPGLEEGK QPRGIIDWSL ESSSGKETKI SKWKITGNLG
     GEDYIDKFRG PRNEGGFFFE RQGYHLPSPP LSNFKPGSPF KGISKPGVAF YTANLKLSLP
     SDRFDIPLSF EFKNNTASAG SYRALLYVNG FQYGRYVSHV GPQSVFPVPE GIFNYRGDNW
     IGLGLWALAK GANVEGLSLN AGVPVQTGRE PVKYVKGPKY THRRGAY
//
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