ID K2R790_MACPH Unreviewed; 548 AA.
AC K2R790;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN ORFNames=MPH_04496 {ECO:0000313|EMBL:EKG18236.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG18236.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18236.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18236.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG18236.1}.
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DR EMBL; AHHD01000212; EKG18236.1; -; Genomic_DNA.
DR AlphaFoldDB; K2R790; -.
DR STRING; 1126212.K2R790; -.
DR VEuPathDB; FungiDB:MPH_04496; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_2_1; -.
DR InParanoid; K2R790; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000007129; 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:UP000007129}.
FT DOMAIN 7..106
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 548 AA; 58551 MW; 87F529B779FB927F CRC64;
MAQEFKLKGI DSLNLKNGDK QEVEVEGIEN GKVLLVKVND RIRATSANCT HYGAPLVKGV
LTGEGRLTCP WHGACFNVAT GDVEDAPALD PLATFEVVQK DGGVFIKGDE ETIKANKRPL
GFKCSAQGSE KVLVIGGGSG TLGAVEGLRG GGYTGHITVL SKEGYRPIDR TKLSKALLAD
VSKVAWRSED WYKNASIDII NDEASGVDFD AKKVSTKSGN TYDYTKLVLA TGGTPRWLPL
PGLKGDLGNV FVLRSVPDAQ NIVKTVGENG KKIVVIGSSF IGMEVANCLA GKKNDVTVIG
MEKAPMERVM GEKVGQIFRG LLEKNGVKFH MEASVDKATP SKSDSSKVGA VHLKDGTVLE
ADLVIEGVGV SPATEYLKGN KAIELLKDGS ISTDESFAVK GLKDVFAIGD IATYPYHGPG
GNGSPIRIEH WNVAQNAGRS VANSINNPGA KPKPFIPVFW SALGSQLRYC GNTVGGYDDV
VIQGEPEKPS FIAYYTKGEE VVAMASMMKD PYMTQTAELM RRGKMPTKSE LQKGVDILEI
SVPAEIRI
//
