ID A0CXY6_PARTE Unreviewed; 590 AA.
AC A0CXY6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Chromosome undetermined scaffold_30, whole genome shotgun sequence {ECO:0000313|EMBL:CAK75653.1};
GN ORFNames=GSPATT00011285001 {ECO:0000313|EMBL:CAK75653.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK75653.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK75653.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK75653.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; CT868208; CAK75653.1; -; Genomic_DNA.
DR RefSeq; XP_001443050.1; XM_001443013.1.
DR AlphaFoldDB; A0CXY6; -.
DR STRING; 5888.A0CXY6; -.
DR EnsemblProtists; CAK75653; CAK75653; GSPATT00011285001.
DR GeneID; 5028835; -.
DR KEGG; ptm:GSPATT00011285001; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_2_1; -.
DR InParanoid; A0CXY6; -.
DR OMA; MYGIVTD; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 49..148
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 590 AA; 64505 MW; 8C6724B0522A2B99 CRC64;
MRKILSSAIA ITLRRTPLVV PQRTQRIAAT LISLPLIRYG FQTLNLNDAY EVSIEDNLNE
GEMREVQVGP KKEDAVLVCK VDGQIYCVSN SCPHVGAPLS AGFLVGDKVK CPFHNASFSV
KDGVHEEGPM FRGLQTFPVK QENGQLVIRV EKQLLNAPRT LNMVTKGDDP THVVIVGGGV
SGQSAAETLR QAGFRGKITL ITAEDSLPYD RTPMSKMTFF GQIIGPQQFY EQYGIDVLTN
TTVESIDINN QDVVVGKEKI HYDKLLLATG GTARRPQLDG VNLGNVHTLR QFNDLESIRD
KAKTAKNIVV VGASFIGMET ASAIKKEFKD QVNITVVDST TVPFERVLGK EVGGSLQKLH
EANGVEFELN AGVKRIGGVG QVQRVDLLNG KSLQADLVIL GTGIQPNNKL VKDQLKISPN
GGIETDVFLK AAKNVYASGD ISSYPYWATG EHVRIEHQNE AVRQGYVAAL NILGKPTPLT
DVPFFWTRQW DRTLAYSGVG QGFDEVIVDG DLTQQKFVAY YARKGRVVAS ASMNTPNAQM
IISEALRLNV MPSAEDLKEK KVSLDDIKKI VLSKGSSCHC KRAGQCQAQL
//
