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Database: UniProt
Entry: A0A2H3G8A2_FUSOX
LinkDB: A0A2H3G8A2_FUSOX
Original site: A0A2H3G8A2_FUSOX 
ID   A0A2H3G8A2_FUSOX        Unreviewed;      1021 AA.
AC   A0A2H3G8A2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-FEB-2019, entry version 6.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCD26731.1};
GN   ORFNames=AU210_013153 {ECO:0000313|EMBL:PCD26731.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD26731.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD26731.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD26731.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C.,
RA   Ma L.J., Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium
RT   oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD26731.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD26731.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection
RT   of multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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|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:PCD26731.1}.
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DR   EMBL; MABQ02000009; PCD26731.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000219602; Chromosome 11.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000219602};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1021       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013910753.
FT   DOMAIN      399    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1021 AA;  113543 MW;  E67011B9F8DC732E CRC64;
     MKLLSLSTVG LLALAGLSIG QETKDVPIQD NGLTNIVEWD DHSYLINGER IFVFSGEFHY
     WRLPVPELWR DLLEKIKAAG FTAFSIYNSW GYHEATPGVL DFENGAHDFV SIMTLAKELG
     LYLLIRPGPY VNAEANAGGF PLWVTTGEYG KLRNDDPRYT KAWSKYWTEI SKIIEPHLIT
     NGGNVAMFQI ENELGGQWKN DDKRILNEPT ANYMQLLKES ARKAGIDVPV FHNAPNTRTF
     SWSNDFERNA TGNVDVTGVD SYPSCWSCNL DECTGTNGEY VPYNIQDYVT YFNKQSPRQP
     HFLPEFQGGS YNPWGGPEGG CPGDIGPDFA NIFYRDLLAQ QATAISLYMM YGGTNWGWFA
     CPVVATSYDY SSPISENRAI WDKYYETKSL TLFTRVAHDL TKTTRVTNST SLSTNDAILI
     SELRHEENDA AFYVARHDHS PSGTKETFKL HVKTSEGKLT IPQNEGSITI NGHQSKVIPT
     DFHFGKKTLL YSTAEVLTYS IIDNKEVIVL WLPEGEQGEF TLKGHTELKH DKSLKGIKVK
     AGKKSVTVNY TQQKGLFTLN LKDGSTIVLA DRKTAYKFWA PTLDNNPFAP VNKTVLIHGP
     YLVRHATIKN GQLNIQGDLD SATETTVFAP ESLKSIAWNG EKVKVSSKEG HKYTIKLKGP
     SKVTLPKLES WKYADSLPEI KTDYKTSSSA WVVADKKNTT NAVLVPDQKN PVLYVDEYKI
     HYGNHIYRAT FPTTSSAPTG VYLNLTGGMA FGYSVWLNSD YIGSYLGEAT TGHAGQEFSF
     KNATLSKKEN VLVVLMDNSG HDLRDGALDP RGITNATLIG PAKGGYKFSE WKIAGHAGSI
     EGEVIDPIRG PLNEGGLYAE RIGAHLPGFS DKKWKSYSSK QGTLVNPSAG VRAYRTTVDL
     DIPDGLDVGV SFKLTAPSNT TFSATKKGYS NQVRVLLFVN GYQYGRFNPY IGNQISFPVP
     PGVLNYDGEN TIAVTVWSQS AQGGEVKVEW EVDYAHTSSF DVKFDSKYLR PDWTKERLQY
     A
//
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