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Database: UniProt
Entry: C9S5F7_VERA1
LinkDB: C9S5F7_VERA1
Original site: C9S5F7_VERA1 
ID   C9S5F7_VERA1            Unreviewed;       229 AA.
AC   C9S5F7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   22-FEB-2023, entry version 63.
DE   SubName: Full=3-chlorobenzoate-3,4-dioxygenase reductase subunit {ECO:0000313|EMBL:EEY14229.1};
GN   ORFNames=VDBG_00336 {ECO:0000313|EMBL:EEY14229.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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DR   EMBL; DS985214; EEY14229.1; -; Genomic_DNA.
DR   RefSeq; XP_003008655.1; XM_003008609.1.
DR   AlphaFoldDB; C9S5F7; -.
DR   STRING; 526221.C9S5F7; -.
DR   GeneID; 9528845; -.
DR   KEGG; val:VDBG_00336; -.
DR   eggNOG; ENOG502SEJJ; Eukaryota.
DR   HOGENOM; CLU_1210588_0_0_1; -.
DR   OMA; CGTCETD; -.
DR   OrthoDB; 1781076at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR   PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Dioxygenase {ECO:0000313|EMBL:EEY14229.1};
KW   Iron {ECO:0000256|ARBA:ARBA00022714};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   DOMAIN          146..229
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  25383 MW;  E4A667233F3A99E0 CRC64;
     MPGPDGVVQG GQVHKRRSPT LTRRATTSLS LAESVLQRFW LRWRHTTASI TTLSCISAVR
     SAADVPFRQR IEKLGTSVKV YDKSKGQHLD IREIVRTLKW NSQLYFCGPT RMIESGRRAV
     QEFGVDENEV HYEAFSADTT GDPFDAEVSN RAGKIVHVTR EETLLEVLKR EFGGDQVESS
     CEVGNCGTCK INLKDGTVEH RGTALTTEQK GSSMLSCVSR GIGRIVVEV
//
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