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UniProtKB - P08067 (UCRI_YEAST)

Entry version 206 (29 Sep 2021)
Sequence version 1 (01 Aug 1988)
Previous versions | rss
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Protein

Cytochrome b-c1 complex subunit Rieske, mitochondrial

Gene

RIP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544).

It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q0 site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable).

2 Publications3 Publications

Miscellaneous

The Rieske protein is a high potential 2Fe-2S protein.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[2Fe-2S] cluster4 PublicationsNote: Binds 1 [2Fe-2S] cluster per subunit.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi159Iron-sulfur (2Fe-2S)Combined sources4 Publications1
Metal bindingi161Iron-sulfur (2Fe-2S); via pros nitrogenCombined sources4 Publications1
Metal bindingi178Iron-sulfur (2Fe-2S)Combined sources4 Publications1
Metal bindingi181Iron-sulfur (2Fe-2S); via pros nitrogenCombined sources4 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: GO_Central
  • ubiquinol-cytochrome-c reductase activity Source: SGD
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processElectron transport, Respiratory chain, Transport
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-611105, Respiratory electron transport

Protein family/group databases

Transport Classification Database

More...TCDBi		3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC:7.1.1.82 Publications)
Alternative name(s):
Complex III subunit 5
Rieske iron-sulfur protein
Short name:
RISP
Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RIP1
Ordered Locus Names:YEL024W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000000750, RIP1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YEL024W

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini31 – 50Mitochondrial matrix2 PublicationsAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei51 – 80Helical2 PublicationsAdd BLAST30
Topological domaini81 – 215Mitochondrial intermembrane2 PublicationsAdd BLAST135

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi157G → D: Loss of activity. 1 Publication1
Mutagenesisi159C → S: Loss of activity. 1 Publication1
Mutagenesisi161H → R: Loss of activity. 1 Publication1
Mutagenesisi163G → D: Partial loss of activity. 1 Publication1
Mutagenesisi164C → S: Loss of activity. 1 Publication1
Mutagenesisi166P → L: Partial loss of activity. 1 Publication1
Mutagenesisi178C → S or Y: Loss of activity. 2 Publications1
Mutagenesisi179P → L: Partial loss of activity. 1 Publication1
Mutagenesisi180C → S: Loss of activity. 1 Publication1
Mutagenesisi181H → R: Loss of activity. 1 Publication1
Mutagenesisi183S → L: Loss of activity. 1 Publication1
Mutagenesisi184H → R: No loss of activity. 1 Publication1
Mutagenesisi186D → N: Partial loss of activity. 1 Publication1
Mutagenesisi189G → D: Loss of activity. 1 Publication1
Mutagenesisi195P → S: No loss of activity. 1 Publication1
Mutagenesisi196A → T: No loss of activity. 1 Publication1
Mutagenesisi203P → S: Loss of activity. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 22Mitochondrion2 PublicationsAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044919523 – 30Removed in mature form2 Publications8
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003068331 – 215Cytochrome b-c1 complex subunit Rieske, mitochondrialAdd BLAST185

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi164 ↔ 180PROSITE-ProRule annotationCombined sources3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1.2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08067

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P08067

PRoteomics IDEntifications database

More...PRIDEi		P08067

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:1657998, PubMed:2538628, PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III2IV and III2IV2) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554). RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598556, PubMed:30598554).

9 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		36705, 253 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-567, Mitochondrial respiratory chain complex III

Database of interacting proteins

More...DIPi		DIP-6616N

Protein interaction database and analysis system

More...IntActi		P08067, 4 interactors

STRING: functional protein association networks

More...STRINGi		4932.YEL024W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P08067, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P08067

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08067

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini123 – 214RieskePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni90 – 93Hinge1 Publication4

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Rieske iron-sulfur protein family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1671, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000001014

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_055690_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08067

Identification of Orthologs from Complete Genome Data

More...OMAi		VEYKKMM

Family and domain databases

Database of protein disorder

More...DisProti		DP00687

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.5.270, 1 hit
2.102.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR037008, bc1_Rieske_TM_sf
IPR017941, Rieske_2Fe-2S
IPR036922, Rieske_2Fe-2S_sf
IPR014349, Rieske_Fe-S_prot
IPR005805, Rieske_Fe-S_prot_C
IPR004192, Rieske_TM
IPR006317, Ubiquinol_cyt_c_Rdtase_Fe-S-su

The PANTHER Classification System

More...PANTHERi		PTHR10134, PTHR10134, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00355, Rieske, 1 hit
PF02921, UCR_TM, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00162, RIESKE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50022, SSF50022, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01416, Rieske_proteo, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51296, RIESKE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08067-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGIRSSVKT CFKPMSLTSK RLISQSLLAS KSTYRTPNFD DVLKENNDAD 
        60         70         80         90        100
KGRSYAYFMV GAMGLLSSAG AKSTVETFIS SMTATADVLA MAKVEVNLAA 
       110        120        130        140        150
IPLGKNVVVK WQGKPVFIRH RTPHEIQEAN SVDMSALKDP QTDADRVKDP 
       160        170        180        190        200
QWLIMLGICT HLGCVPIGEA GDFGGWFCPC HGSHYDISGR IRKGPAPLNL 
       210 
EIPAYEFDGD KVIVG
Length:215
Mass (Da):23,365
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i21981BD8492E86F3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M23316 Genomic DNA Translation: AAA34980.1
M24500 Genomic DNA Translation: AAA34981.1
U18530 Genomic DNA Translation: AAB64501.1
AY558341 Genomic DNA Translation: AAS56667.1
BK006939 Genomic DNA Translation: DAA07628.1

Protein sequence database of the Protein Information Resource

More...PIRi		A29318

NCBI Reference Sequences

More...RefSeqi		NP_010890.3, NM_001178839.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YEL024W_mRNA; YEL024W; YEL024W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		856689

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YEL024W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23316 Genomic DNA Translation: AAA34980.1
M24500 Genomic DNA Translation: AAA34981.1
U18530 Genomic DNA Translation: AAB64501.1
AY558341 Genomic DNA Translation: AAS56667.1
BK006939 Genomic DNA Translation: DAA07628.1
PIRiA29318
RefSeqiNP_010890.3, NM_001178839.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30E31-215[»]
1KB9X-ray2.30E31-215[»]
1KYOX-ray2.97E/P31-215[»]
1P84X-ray2.50E31-215[»]
2IBZX-ray2.30E31-215[»]
3CX5X-ray1.90E/P31-215[»]
3CXHX-ray2.50E/P31-215[»]
4PD4X-ray3.04E31-215[»]
6GIQelectron microscopy3.23E/P1-215[»]
6HU9electron microscopy3.35E/P31-215[»]
6T0Belectron microscopy2.80E/P31-215[»]
6T15electron microscopy3.29E/P31-215[»]
6YMXelectron microscopy3.17E/P31-215[»]
SMRiP08067
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36705, 253 interactors
ComplexPortaliCPX-567, Mitochondrial respiratory chain complex III
DIPiDIP-6616N
IntActiP08067, 4 interactors
STRINGi4932.YEL024W

Protein family/group databases

TCDBi3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

Proteomic databases

MaxQBiP08067
PaxDbiP08067
PRIDEiP08067

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P08067, 1 sequenced antibody

Genome annotation databases

EnsemblFungiiYEL024W_mRNA; YEL024W; YEL024W
GeneIDi856689
KEGGisce:YEL024W

Organism-specific databases

SGDiS000000750, RIP1
VEuPathDBiFungiDB:YEL024W

Phylogenomic databases

eggNOGiKOG1671, Eukaryota
GeneTreeiENSGT00390000001014
HOGENOMiCLU_055690_0_1_1
InParanoidiP08067
OMAiVEYKKMM

Enzyme and pathway databases

ReactomeiR-SCE-611105, Respiratory electron transport

Miscellaneous databases

EvolutionaryTraceiP08067

Protein Ontology

More...PROi		PR:P08067
RNActiP08067, protein

Family and domain databases

DisProtiDP00687
Gene3Di1.20.5.270, 1 hit
2.102.10.10, 1 hit
InterProiView protein in InterPro
IPR037008, bc1_Rieske_TM_sf
IPR017941, Rieske_2Fe-2S
IPR036922, Rieske_2Fe-2S_sf
IPR014349, Rieske_Fe-S_prot
IPR005805, Rieske_Fe-S_prot_C
IPR004192, Rieske_TM
IPR006317, Ubiquinol_cyt_c_Rdtase_Fe-S-su
PANTHERiPTHR10134, PTHR10134, 1 hit
PfamiView protein in Pfam
PF00355, Rieske, 1 hit
PF02921, UCR_TM, 1 hit
PRINTSiPR00162, RIESKE
SUPFAMiSSF50022, SSF50022, 1 hit
TIGRFAMsiTIGR01416, Rieske_proteo, 1 hit
PROSITEiView protein in PROSITE
PS51296, RIESKE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUCRI_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08067
Secondary accession number(s): D3DLM4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 29, 2021
This is version 206 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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