ID C3YDD3_BRAFL Unreviewed; 466 AA.
AC C3YDD3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_218240 {ECO:0000313|EMBL:EEN61744.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN61744.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61744.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61744.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666503; EEN61744.1; -; Genomic_DNA.
DR RefSeq; XP_002605734.1; XM_002605688.1.
DR AlphaFoldDB; C3YDD3; -.
DR STRING; 7739.C3YDD3; -.
DR eggNOG; KOG1336; Eukaryota.
DR InParanoid; C3YDD3; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
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; PR00469; PNDRDTASEII.
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}.
FT DOMAIN 1..51
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN61744.1"
SQ SEQUENCE 466 AA; 50130 MW; 4731B408B9519F0B CRC64;
PLPIGVLCNG RVRCPWHGAC FNSKTGDIED FPGLDSLPKF EVTVENDNVV VKTNKKVLEK
PKRMKEMSCH SPDNDTVYLI VGGGGAAITC AETLRQEGFK GKVVMATKEP HLPYDRPKLS
KALDSTGEAL ALRDKNFFSV YDIEVLTEKE ATSVDCPSKV VTFADGQTIA YDKLLIATGG
KPRPCTSPGS DLENVCLLRS PADGNYIAQQ GKGKNVVIVG TSFIGMEVAA YFAGKASSVS
VVGVSSTPFG RVLGEQVGSM LRKMHEEKGV KFYMNNGVVE FKGENGKLKE VVLQSGETLP
ADLCVVGIGV TPNTEFLSDS GIEMTRGALD VDKTMQTSQD HVFAAGDIAH FPLPMADGEK
VSIGHWQLAK AHGRCAALNM LGQGVEFNSV PFFWTMQYGK SLRYAGYGAG FEDVVIEGSL
DDMQFVAYYV KGDDVLAVAS MNRDPVVAQA AEIMHSGRTL SRADAE
//
