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Database: UniProt
Entry: A0A2H3GYN9_FUSOX
LinkDB: A0A2H3GYN9_FUSOX
Original site: A0A2H3GYN9_FUSOX 
ID   A0A2H3GYN9_FUSOX        Unreviewed;       733 AA.
AC   A0A2H3GYN9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCD32918.1};
GN   ORFNames=AU210_009154 {ECO:0000313|EMBL:PCD32918.1};
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:PCD32918.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD32918.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD32918.1,
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:PCD32918.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD32918.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/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   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
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:PCD32918.1}.
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DR   EMBL; MABQ02000006; PCD32918.1; -; Genomic_DNA.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000219602; Chromosome 8.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|SAAS:SAAS00296904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000219602};
KW   Ligase {ECO:0000256|SAAS:SAAS00232059};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT   DOMAIN       43    495       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      159    359       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      649    724       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   733 AA;  80674 MW;  B93859FD40C37E98 CRC64;
     MRSTLRANRR LPLKPLPRFL STSASSASVS SVASSSSAPK HTPINSVLIA NRGEIAIRIN
     RTAERLGIRA TTVYTDVDAG SWHASSGFQS LALGPANAYL DGEKIIALAK QNGIQALHPG
     YGFLSENSKF AERCEEEGIV FVGPPATAMA DMGHKARSKE IMTAANVPCV PGYHGADQGE
     QELLEHAKNI TFPVLLKSVR GGGGKGMRIV LTEEEFLTQL RSARAEAKAS FGEGGEVMLV
     EKYIIRPRHV EVQVFADKWG NTVALGERDC SVQRRHQKIL EESPAPDLDL ATRHDLWDKA
     RKAASAVGYV GAGTVEFILD KDTNKFYFME MNTRLQVEHP VTEMVTGLDL VEWQFRVAAG
     EKLPLSQEEV EAQMNERGAA IEARIYAENP EKGFIPDSGK LVRAYLPTEL QNEDVRLDWG
     FRSGNTISEA YDGMIAKLIV RGDTRERAIA KLESVLRSYE IVGVATNIEF LKRLCETDAF
     VAGDVETGFI DKWREELFKP RPIKNEVVAQ AALGMINFEH RNSGPHGLTL GFGETNNIGE
     RKLNFKILDG YSKEEGEVVE ASVTQTGHNL YNVAVHRKGD ETPQVFINIA CQPEPEGEVM
     KLESYFPLER IQSSVVPQHT DNDTKVTVFQ HGVKTDLVLL PPKWYEKALG LKESSASVAA
     PMPCKILKNE VVEGQIVQKG APLVVIESMK METIIRSPQD GIIKKLAHKE GDICKAGTVL
     VLFEEGETKD GES
//
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