ID A0A0D1Y9J2_9EURO Unreviewed; 544 AA.
AC A0A0D1Y9J2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN ORFNames=PV08_10958 {ECO:0000313|EMBL:KIW11656.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11656.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW11656.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11656.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847499; KIW11656.1; -; Genomic_DNA.
DR RefSeq; XP_016231872.1; XM_016385270.1.
DR AlphaFoldDB; A0A0D1Y9J2; -.
DR STRING; 91928.A0A0D1Y9J2; -.
DR GeneID; 27338041; -.
DR VEuPathDB; FungiDB:PV08_10958; -.
DR HOGENOM; CLU_003291_4_2_1; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000053328; 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; 1.
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:UP000053328}.
FT DOMAIN 7..106
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 544 AA; 58284 MW; 3EFEBE031FFBC927 CRC64;
MAQEWKLKDL TTLDLKDLDK VEVEVEGIEG GKVLLVKVGD QISALNANCT HYGAPLKNGV
LTPEGRLTCP WHGACFNTKT GDVEDSPAPL ALNKFNVVEK DGGVYISGKE TDIKGGKRPV
NVKTTPSTPE RVVIVGGGSG TFGTILKLRE HGFQGHVTVI TGEGLPIDRT KLSKALITDA
SQIYLQPEQW YKDGSIEFYP DTVTSVDFDS REVKTKTGKA FPYTKLILAT GGTPRTLPLP
GFKELSNIFL LRQVSDTQAI MNAVGDGNKK IVIIGSSFIG MEVANALAKN NSVSIVGMES
APMERVMGAE VGKIFQRMLE KNGGKFYLNA GVDSAVPASN LANAVGLSSV RAVKLKDGAE
LEADLVILGI GVKPATEYLE NNASIKLEKD GSVAVDQNFA VKGLSDVYAI GDIATYPYNG
PGASDTPVRI EHWNVAQNMG RTVGQLIARP GSKPKPFIPI FWSALGSQLR YCGSTSNGWD
DVVIKGEPEN GKFAAYYCKG DAVVAVASMM MDPVMVKSAE LMRHNKMPSK KEIQGGEDVL
QASL
//
