UCRI_BOVIN
ID UCRI_BOVIN Reviewed; 274 AA.
AC P13272; A3KN53; P07588; Q1LZH6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 5;
DE AltName: Full=Cytochrome b-c1 complex subunit 5;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=RISP;
DE AltName: Full=Rieske protein UQCRFS1;
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE Contains:
DE RecName: Full=Cytochrome b-c1 complex subunit 9 {ECO:0000303|PubMed:8386158};
DE Short=Su9 {ECO:0000303|PubMed:8386158};
DE Short=Subunit 9 {ECO:0000303|PubMed:8386158};
DE AltName: Full=8 kDa subunit 9 {ECO:0000303|PubMed:8386158};
DE AltName: Full=Complex III subunit IX;
DE AltName: Full=Cytochrome b-c1 complex subunit 11;
DE AltName: Full=UQCRFS1 mitochondrial targeting sequence;
DE Short=UQCRFS1 MTS;
DE AltName: Full=Ubiquinol-cytochrome c reductase 8 kDa protein {ECO:0000303|PubMed:8386158};
DE Flags: Precursor;
GN Name=UQCRFS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2157409; DOI=10.1016/0006-291x(90)92063-6;
RA Usui S., Yu L., Yu C.-A.;
RT "Cloning and sequencing of a cDNA encoding the Rieske iron-sulfur protein
RT of bovine heart mitochondrial ubiquinol-cytochrome c reductase.";
RL Biochem. Biophys. Res. Commun. 167:575-579(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION, SUBUNIT, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=8386158; DOI=10.1016/s0021-9258(18)52883-0;
RA Brandt U., Yu L., Yu C.-A., Trumpower B.L.;
RT "The mitochondrial targeting presequence of the Rieske iron-sulfur protein
RT is processed in a single step after insertion into the cytochrome bc1
RT complex in mammals and retained as a subunit in the complex.";
RL J. Biol. Chem. 268:8387-8390(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford;
RC TISSUE=Fetal brain, Fetal cerebellum, and Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1-78, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=2996928; DOI=10.1016/0014-5793(85)81007-3;
RA Borchart U., Machleidt W., Schagger H., Link T.A., von Jagow G.;
RT "Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of
RT beef heart ubiquinol:cytochrome c reductase.";
RL FEBS Lett. 191:125-130(1985).
RN [5]
RP PROTEIN SEQUENCE OF 79-274.
RX PubMed=3036596; DOI=10.1016/0014-5793(87)81210-3;
RA Schaegger H., Borchart U., Machleidt W., Link T.A., von Jagow G.;
RT "Isolation and amino acid sequence of the 'Rieske' iron sulfur protein of
RT beef heart ubiquinol:cytochrome c reductase.";
RL FEBS Lett. 219:161-168(1987).
RN [6]
RP SUBUNIT.
RX PubMed=11073949; DOI=10.1074/jbc.m007128200;
RA Deng K., Shenoy S.K., Tso S.C., Yu L., Yu C.A.;
RT "Reconstitution of mitochondrial processing peptidase from the core
RT proteins (subunits I and II) of bovine heart mitochondrial cytochrome bc(1)
RT complex.";
RL J. Biol. Chem. 276:6499-6505(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-274.
RX PubMed=8736555; DOI=10.1016/s0969-2126(96)00062-7;
RA Iwata S., Saynovits M., Link T.A., Michel H.;
RT "Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein
RT of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD
RT phasing at 1.5-A resolution.";
RL Structure 4:567-579(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9204897; DOI=10.1126/science.277.5322.60;
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RT "Crystal structure of the cytochrome bc1 complex from bovine heart
RT mitochondria.";
RL Science 277:60-66(1997).
RN [9]
RP ERRATUM OF PUBMED:9204897.
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RL Science 278:2037-2037(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9651245; DOI=10.1126/science.281.5373.64;
RA Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A.,
RA Ramaswamy S., Jap B.K.;
RT "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1
RT complex.";
RL Science 281:64-71(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=12269811; DOI=10.1021/bi026252p;
RA Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L.,
RA Xia D.;
RT "The crystal structure of mitochondrial cytochrome bc1 in complex with
RT famoxadone: the role of aromatic-aromatic interaction in inhibition.";
RL Biochemistry 41:11692-11702(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
RX PubMed=15312779; DOI=10.1016/j.jmb.2004.05.065;
RA Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.;
RT "Crystallographic studies of quinol oxidation site inhibitors: a modified
RT classification of inhibitors for the cytochrome bc(1) complex.";
RL J. Mol. Biol. 341:281-302(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=16024040; DOI=10.1016/j.jmb.2005.05.053;
RA Huang L.S., Cobessi D., Tung E.Y., Berry E.A.;
RT "Binding of the respiratory chain inhibitor antimycin to the mitochondrial
RT bc1 complex: a new crystal structure reveals an altered intramolecular
RT hydrogen-bonding pattern.";
RL J. Mol. Biol. 351:573-597(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
RX PubMed=16924113; DOI=10.1073/pnas.0601149103;
RA Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.;
RT "Surface-modulated motion switch: capture and release of iron-sulfur
RT protein in the cytochrome bc1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]:
CC Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit
CC transmembrane complex that is part of the mitochondrial electron
CC transport chain which drives oxidative phosphorylation. The respiratory
CC chain contains 3 multisubunit complexes succinate dehydrogenase
CC (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-
CC c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV,
CC CIV), that cooperate to transfer electrons derived from NADH and
CC succinate to molecular oxygen, creating an electrochemical gradient
CC over the inner membrane that drives transmembrane transport and the ATP
CC synthase. The cytochrome b-c1 complex catalyzes electron transfer from
CC ubiquinol to cytochrome c, linking this redox reaction to translocation
CC of protons across the mitochondrial inner membrane, with protons being
CC carried across the membrane as hydrogens on the quinol. In the process
CC called Q cycle, 2 protons are consumed from the matrix, 4 protons are
CC released into the intermembrane space and 2 electrons are passed to
CC cytochrome c. The Rieske protein is a catalytic core subunit containing
CC a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational
CC states during catalysis to transfer electrons from the quinol bound in
CC the Q(0) site in cytochrome b to cytochrome c1 (By similarity).
CC Incorporation of UQCRFS1 is the penultimate step in complex III
CC assembly (By similarity). {ECO:0000250|UniProtKB:P08067,
CC ECO:0000250|UniProtKB:P47985}.
CC -!- FUNCTION: [Cytochrome b-c1 complex subunit 9]: Component of the
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII). UQCRFS1 undergoes proteolytic processing once it is
CC incorporated in the complex III dimer. One of the fragments, called
CC subunit 9, corresponds to its mitochondrial targeting sequence (MTS)
CC (PubMed:8386158, PubMed:2996928). The proteolytic processing is
CC necessary for the correct insertion of UQCRFS1 in the complex III
CC dimer, but the persistence of UQCRFS1-derived fragments may prevent
CC newly imported UQCRFS1 to be processed and assembled into complex III
CC and is detrimental for the complex III structure and function (By
CC similarity). {ECO:0000250|UniProtKB:P47985,
CC ECO:0000250|UniProtKB:Q9CR68, ECO:0000269|PubMed:2996928,
CC ECO:0000269|PubMed:8386158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P08067};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:9651245};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the
CC Rieske protein is mediated by components of the iron sulfur (Fe-S)
CC cluster assembly machinery that reside in the mitochondrial matrix
CC (including HSC20 and LYRM7). {ECO:0000269|PubMed:9651245};
CC -!- SUBUNIT: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]:
CC Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII), a multisubunit enzyme composed of 11
CC subunits. The complex is composed of 3 respiratory subunits cytochrome
CC b, cytochrome c1 and Rieske protein UQCRFS1, 2 core protein subunits
CC UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular weight protein
CC subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10
CC and subunit 9, the cleavage product of Rieske protein UQCRFS1
CC (PubMed:8386158). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:27830641).
CC Incorporation of the Rieske protein UQCRFS1 is the penultimate step in
CC complex III assembly. Interacts with TTC19, which is involved in the
CC clearance of UQCRFS1 fragments (By similarity).
CC {ECO:0000250|UniProtKB:P47985, ECO:0000269|PubMed:27830641,
CC ECO:0000269|PubMed:8386158}.
CC -!- SUBUNIT: [Cytochrome b-c1 complex subunit 9]: Component of the
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII) (PubMed:8386158). Subunit 9 corresponds to the mitochondrial
CC targeting sequence (MTS) of Rieske protein UQCRFS1. It is retained
CC after processing and incorporated inside complex III, where it remains
CC bound to the complex and localizes between the 2 core subunits
CC UQCRC1/QCR1 and UQCRC2/QCR2 (PubMed:9651245).
CC {ECO:0000269|PubMed:8386158, ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZLR5}.
CC -!- PTM: Proteolytic processing is necessary for the correct insertion of
CC UQCRFS1 in the complex III dimer. Several fragments are generated
CC during UQCRFS1 insertion, most probably due to the endogenous matrix-
CC processing peptidase (MPP) activity of the 2 core protein subunits
CC UQCRC1/QCR1 and UQCRC2/QCR2, which are homologous to the 2
CC mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-
CC MPP respectively. The action of the protease is also necessary for the
CC clearance of the UQCRFS1 fragments. {ECO:0000250|UniProtKB:Q9CR68}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
CC -!- CAUTION: Several peptides are generated during UQCRFS1 insertion.
CC According to some authors, the identification of the transit peptide as
CC the subunit 9, does not necessary imply that it must be considered as a
CC structural subunit of the complex III dimer as additional fragments
CC from UQCRFS1 are also present. {ECO:0000250|UniProtKB:P47985}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30515.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M34336; AAA30515.1; ALT_SEQ; mRNA.
DR EMBL; S58789; AAB26197.1; -; mRNA.
DR EMBL; BC115994; AAI15995.1; -; mRNA.
DR EMBL; BC133620; AAI33621.1; -; mRNA.
DR EMBL; BC133632; AAI33633.1; -; mRNA.
DR PIR; A46063; A34660.
DR RefSeq; NP_777238.1; NM_174813.2.
DR PDB; 1BCC; X-ray; 3.16 A; A=192-195, E=79-274.
DR PDB; 1BE3; X-ray; 3.00 A; E=79-274, I=1-78.
DR PDB; 1BGY; X-ray; 3.00 A; E/Q=79-274, I/U=1-78.
DR PDB; 1L0L; X-ray; 2.35 A; E=79-274, I=1-78.
DR PDB; 1L0N; X-ray; 2.60 A; E=79-274, I=1-78.
DR PDB; 1NTK; X-ray; 2.60 A; E=79-274, I=1-57.
DR PDB; 1NTM; X-ray; 2.40 A; E=79-274, I=1-57.
DR PDB; 1NTZ; X-ray; 2.60 A; E=79-274, I=1-57.
DR PDB; 1NU1; X-ray; 3.20 A; E=79-274, I=1-57.
DR PDB; 1PP9; X-ray; 2.10 A; E/R=79-274, I/V=1-78.
DR PDB; 1PPJ; X-ray; 2.10 A; E/R=79-274, I/V=1-78.
DR PDB; 1QCR; X-ray; 2.70 A; E=79-274, I=21-48.
DR PDB; 1RIE; X-ray; 1.50 A; A=146-274.
DR PDB; 1SQB; X-ray; 2.69 A; E=79-274, I=1-78.
DR PDB; 1SQP; X-ray; 2.70 A; E=79-274, I=1-78.
DR PDB; 1SQQ; X-ray; 3.00 A; E=79-274, I=1-78.
DR PDB; 1SQV; X-ray; 2.85 A; E=79-274, I=1-78.
DR PDB; 1SQX; X-ray; 2.60 A; E=79-274, I=1-78.
DR PDB; 2A06; X-ray; 2.10 A; E/R=79-274, I/V=1-78.
DR PDB; 2FYU; X-ray; 2.26 A; E=79-274, I=1-78.
DR PDB; 2YBB; EM; 19.00 A; E/e=79-274, I/i=14-78.
DR PDB; 4D6T; X-ray; 3.57 A; E/I/R/V=1-274.
DR PDB; 4D6U; X-ray; 4.09 A; E/I/R/V=1-274.
DR PDB; 5GPN; EM; 5.40 A; I/U=1-78.
DR PDB; 5KLV; X-ray; 2.65 A; E=79-274, I=1-78.
DR PDB; 5LUF; EM; 9.10 A; e/q=79-274, i/u=1-78.
DR PDB; 5NMI; X-ray; 3.50 A; E/I/R/V=1-274.
DR PDB; 6FO0; EM; 4.10 A; E/R=1-274.
DR PDB; 6FO6; EM; 4.10 A; E/R=1-274.
DR PDBsum; 1BCC; -.
DR PDBsum; 1BE3; -.
DR PDBsum; 1BGY; -.
DR PDBsum; 1L0L; -.
DR PDBsum; 1L0N; -.
DR PDBsum; 1NTK; -.
DR PDBsum; 1NTM; -.
DR PDBsum; 1NTZ; -.
DR PDBsum; 1NU1; -.
DR PDBsum; 1PP9; -.
DR PDBsum; 1PPJ; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1RIE; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2A06; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 4D6T; -.
DR PDBsum; 4D6U; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 6FO0; -.
DR PDBsum; 6FO6; -.
DR AlphaFoldDB; P13272; -.
DR SMR; P13272; -.
DR CORUM; P13272; -.
DR DIP; DIP-38974N; -.
DR IntAct; P13272; 3.
DR STRING; 9913.ENSBTAP00000054196; -.
DR TCDB; 3.D.3.2.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PeptideAtlas; P13272; -.
DR PRIDE; P13272; -.
DR Ensembl; ENSBTAT00000066053; ENSBTAP00000054196; ENSBTAG00000046786.
DR GeneID; 287020; -.
DR KEGG; bta:287020; -.
DR CTD; 7386; -.
DR VEuPathDB; HostDB:ENSBTAG00000046786; -.
DR VGNC; VGNC:53044; UQCRFS1.
DR eggNOG; KOG1671; Eukaryota.
DR GeneTree; ENSGT00390000001014; -.
DR InParanoid; P13272; -.
DR OMA; DFLLNMS; -.
DR OrthoDB; 1174160at2759; -.
DR EvolutionaryTrace; P13272; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000046786; Expressed in cardiac ventricle and 103 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IEA:Ensembl.
DR Gene3D; 1.20.5.270; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR037008; bc1_Rieske_TM_sf.
DR InterPro; IPR011070; Globular_prot_asu/bsu.
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; IPR004192; Rieske_TM.
DR InterPro; IPR015248; Ubiqinol_cyt_c_Rdtase_N.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF09165; Ubiq-Cytc-red_N; 1.
DR Pfam; PF02921; UCR_TM; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF56568; SSF56568; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..78
FT /note="Cytochrome b-c1 complex subunit 9"
FT /evidence="ECO:0000269|PubMed:3036596,
FT ECO:0000269|PubMed:8386158"
FT /id="PRO_0000030659"
FT CHAIN 79..274
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000030660"
FT TOPO_DOM 79..103
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TRANSMEM 104..140
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TOPO_DOM 141..274
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9651245"
FT DOMAIN 187..272
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT BINDING 219
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT BINDING 236
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT BINDING 239
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT BINDING 241
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT DISULFID 222..238
FT /evidence="ECO:0000269|PubMed:8736555,
FT ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3,
FT ECO:0007744|PDB:1BGY"
FT CONFLICT 150
FT /note="S -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1NTM"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5NMI"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1L0L"
FT HELIX 104..140
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1RIE"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5NMI"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1RIE"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1RIE"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2A06"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1L0L"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1RIE"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1SQP"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1RIE"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1BE3"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1RIE"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:1RIE"
SQ SEQUENCE 274 AA; 29547 MW; 7C5FC17D2A0DD1C9 CRC64;
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL CRESLRGQAA
GRPLVASVSL NVPASVRYSH TDIKVPDFSD YRRPEVLDST KSSKESSEAR KGFSYLVTAT
TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT
KKEIDQEAAV EVSQLRDPQH DLERVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
SHYDASGRIR KGPAPLNLEV PSYEFTSDDM VIVG
