ID D2V6S6_NAEGR Unreviewed; 312 AA.
AC D2V6S6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit mitochondrial {ECO:0000313|EMBL:EFC47627.1};
GN ORFNames=NAEGRDRAFT_78817 {ECO:0000313|EMBL:EFC47627.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC47627.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47627.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000256|ARBA:ARBA00010651}.
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DR EMBL; GG738854; EFC47627.1; -; Genomic_DNA.
DR RefSeq; XP_002680371.1; XM_002680325.1.
DR AlphaFoldDB; D2V6S6; -.
DR STRING; 5762.D2V6S6; -.
DR EnsemblProtists; EFC47627; EFC47627; NAEGRDRAFT_78817.
DR GeneID; 8849121; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_78817; -.
DR eggNOG; KOG1671; Eukaryota.
DR InParanoid; D2V6S6; -.
DR OrthoDB; 166674at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR NCBIfam; TIGR01416; Rieske_proteo; 1.
DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF81502; ISP transmembrane anchor; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 223..311
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 312 AA; 34470 MW; 11CE1E4A575FA5CE CRC64;
MLNQSYRLKT VLTLPIKNLG SSFSAHKACS ASLINKTLSA FDIQAFPGVT AEHQEPTFIF
QSSSKTTAIP EIKPQQIFTN TFSVNKSFRH KTLLTAQPVR FYSTQIGSEK TLKRNELPEA
VQRLVETAPK TGYHGDNINE YLKEGDYDKR QFAYFVANSS RFVVAAGLRL AVLRFLYSWS
AAADVLAVSK IEVDISNVPK GKTITVTWRG KPVFIKHRTE DETKSLAETD LSTLKDPQAD
SDRTKNDEWT VILAICTHLG CVPVTDAGVM NAFFCPCHGS HYDASGRIVK GPAPLNMEVP
KHSLDGSILT LG
//
