ID Q0U508_PHANO Unreviewed; 557 AA.
AC Q0U508;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=3-chlorobenzoate-3,4-dioxygenase reductase subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_13156 {ECO:0000313|EMBL:EAT79483.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT79483.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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DR EMBL; CH445349; EAT79483.1; -; Genomic_DNA.
DR RefSeq; XP_001803368.1; XM_001803316.1.
DR AlphaFoldDB; Q0U508; -.
DR STRING; 321614.Q0U508; -.
DR EnsemblFungi; SNOT_13156; SNOT_13156; SNOG_13156.
DR GeneID; 5980283; -.
DR KEGG; pno:SNOG_13156; -.
DR VEuPathDB; FungiDB:JI435_131560; -.
DR eggNOG; ENOG502S8QJ; Eukaryota.
DR HOGENOM; CLU_003827_17_2_1; -.
DR InParanoid; Q0U508; -.
DR OMA; YLYHEKD; -.
DR OrthoDB; 1781076at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 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 Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03475; YiiM_3-alpha; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
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:UP000001055}.
SQ SEQUENCE 557 AA; 61841 MW; 8F5EFA846AC73543 CRC64;
MARSNWIPPT PPDPNTLTNP PPFAPFPLKQ LRAGKVKKFG PFQSAIFKTP LSGPIEITMG
GIKGDEHAYE AHRSPDNALL HYCTTHYDDW KKELPASESH FKPGAFGENF FNDEVSEKTL
CIGDRIAIGE VVVEVTEPRG PCYKLNHRFE VKDMAKRTQT LFRTGWLYRI IKPGFVQAGD
MIRLLERPYP EWTIARVMYY LFIDTKDLEM MKEIVKIGPL SADVKNKFQK RLATGTPEDQ
NGRMYGEESD KMDAWNEYCL VEKRQETSRV TAFVFEAVDD IANPSPVEPG SHVRLKLGGK
LVRAYSVVAG DSSRFELGIQ LSPESRGGSK YIHEQAKVGD VLIVGRFTAS FPLATDADEH
VIISAGIGIT AFLPAFKYLQ QTNQKFHLHY AHTGEVPYAS QIDALGSNAT IYDKTQSQRL
DVDKIISRTQ DRSHIYTCGP ERLMDDVGNT AKKYGVPEAC VHLEQFTVTT SGDPFTVELK
ESKKTLEVGA SQSLLDALKA IGMDIDSSCE VGNCGTCKVA VCSGRIEHRG TGLMEDEKAD
AMLSCVSRGV GTIILDL
//
