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Database: UniProt
Entry: A0A094H4S2_9PEZI
LinkDB: A0A094H4S2_9PEZI
Original site: A0A094H4S2_9PEZI 
ID   A0A094H4S2_9PEZI        Unreviewed;       622 AA.
AC   A0A094H4S2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN   ORFNames=V502_08387 {ECO:0000313|EMBL:KFZ09972.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ09972.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ09972.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
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:KFZ09972.1}.
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DR   EMBL; JPKE01002898; KFZ09972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094H4S2; -.
DR   STRING; 1420915.A0A094H4S2; -.
DR   HOGENOM; CLU_003291_4_2_1; -.
DR   OrthoDB; 495825at2759; -.
DR   Proteomes; UP000029308; 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:UP000029308}.
FT   DOMAIN          87..186
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   622 AA;  66356 MW;  48497A60306C0A58 CRC64;
     MTELSTNEED MCMVLDRNTD TRAITSAHQY SSHHGLAFDV DDKLLQTGGA KPRIVGVSII
     RQSPRGSKKS LFAFTAQFRA MATEFKVKDL AALDLKPGEK REVEVDGVEG GKVLLLNVGG
     KTTAVGAKCT HYGAPLVKGV LTGDGRITCP WHGACFNAKT GDIENAPAID NLPVFGLVEK
     DGGVYVTGEQ EKIKGSRRKP NIRCSAVKPE NIVVVGGGSG AIGTVEALRE QGYKGSITLI
     SNEGYLPIDR TKLSKALIAD PVKIGLRDQQ WFDEAGITTV TDEVTEVDFL TKKVHTKSSS
     VYPYTKLVLA TGGTPRQLPL PGFKELGNIF VLRNIHNVKD ILAAIGEKNK KIVVIGSSFI
     GMEVAKATSK DNSVSVVGME KVPLERVMGE QVGSYLQKQL EATGVKFHMS AGVDKALPSS
     SDPSKVGAIQ LQDGTKLDAD LVILGVGVAP ATEYLKDNKS VQLAKDGSLT VDENFLVQGL
     DGVYAVGDIA TYPYHGPGGN GAPVRIEHWN VAQNSGRAAA AHIVAPTAAR KPFIPIFWSA
     LGAQLRYCGN TGSGFDGRVV QGLLEEYKFA VFYTRGEEVV AVATMGKDPV VSHASELMRK
     GVFPKKAELA KGLDILTIEV PA
//
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