ID E3S4Q2_PYRTT Unreviewed; 548 AA.
AC E3S4Q2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN ORFNames=PTT_17566 {ECO:0000313|EMBL:EFQ87044.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ87044.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ87044.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; GL537177; EFQ87044.1; -; Genomic_DNA.
DR RefSeq; XP_003304857.1; XM_003304809.1.
DR AlphaFoldDB; E3S4Q2; -.
DR STRING; 861557.E3S4Q2; -.
DR EnsemblFungi; EFQ87044; EFQ87044; PTT_17566.
DR KEGG; pte:PTT_17566; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_2_1; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd03478; Rieske_AIFL_N; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 7..106
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 548 AA; 58882 MW; 149B182985A361F0 CRC64;
MAQEFKLKDV TSLQMKNGEK KEVEVEGVEG GKVLLLKIKD QVHATSSNCT HYGAPLVKGV
LTPEGRLTCP WHGACFNVST GDVEDAPALD PIAKYEVVEK DGAVYVKTTQ EALKANRRFL
NIKCSSVSED KVLVIGGGSG TLGAIEGLRG GGYTGKITVI SKEGYQPIDR TKLSKALLAD
ISKAAWRQKE FYKDASIDII EDEAKSIDFS GKKVSAKSGK EYDYSKLVLA TGGTPRWLPL
DGLKGDLGNV FLLRTLPDAQ NIVKAVGDNG KKIVVVGSSF IGMEVGNCLA SMKNDVTIIG
MEEQPMERVM GKKVGAIFRG LLEKNGVKFQ MSASVDKATP SKDDSSKVGA VHLKDGTVLE
ADVVIEGVGV APATEYLKGN SSVTLEKDGS LKTDEWFAVK GLKDVYAIGD IATYPYHGPG
GDGSPVRIEH WNVAQNAGRS VAHTINNPGS KPKPFIPVFW SALGSQLRYC GNTVGGYDDL
ILQGEPDKAS FVAYYTKGET VVAVASMMKD PYMTQAAELM RRKVMPSKSE LQKGADIMDI
GLPNEIKM
//
