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Protein

Ribonucleoside-diphosphate reductase large chain 1

Gene

RNR1

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

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.1 Publication

Miscellaneous

Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 (By similarity).By similarity
Present with 293000 molecules/cell in log phase SD medium.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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the R1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site. Inhibited by SML1.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

    1. Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: DNA replication

    This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
    View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei5Allosteric activatorBy similarity1
    Binding sitei53Allosteric activatorBy similarity1
    Binding sitei88Allosteric activatorBy similarity1
    Binding sitei202Substrate1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei218Important for hydrogen atom transferBy similarity1
    Sitei226Allosteric effector binding, determines substrate specificity1
    Binding sitei247Substrate; via amide nitrogen1
    Sitei256Allosteric effector binding, determines substrate specificity1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei426Proton acceptor1
    Active sitei428Cysteine radical intermediate1
    Active sitei430Proton acceptor1
    Sitei443Important for hydrogen atom transferBy similarity1
    Sitei741Important for electron transferBy similarity1
    Sitei742Important for electron transferBy similarity1
    Sitei883Interacts with thioredoxin/glutaredoxinBy similarity1
    Sitei886Interacts with thioredoxin/glutaredoxinBy similarity1

    <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

    GO - Biological processi

    <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 functionAllosteric enzyme, Oxidoreductase
    Biological processDNA replication
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YER070W-MONOMER
    YEAST:YER070W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.17.4.1 984

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00326

    <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:
    Ribonucleoside-diphosphate reductase large chain 1 (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase R1 subunit 1
    Ribonucleotide reductase large subunit 1
    <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:RNR1
    Synonyms:CRT7, RIR1, SDS12
    Ordered Locus Names:YER070W
    <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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <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
    S000000872 RNR1

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <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>Mutagenesisi428C → A: Completely abolishes reductase activity. 1 Publication1

    <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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001872031 – 888Ribonucleoside-diphosphate reductase large chain 1Add BLAST888

    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 bondi218 ↔ 443Redox-active1 Publication
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei227PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei816PhosphoserineBy similarity1
    Modified residuei837PhosphoserineCombined sources1
    Cross-linki853Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei887PhosphoserineCombined sources1

    Keywords - PTMi

    Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P21524

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

    More...
    PaxDbi
    P21524

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P21524

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P21524

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Cell cycle-regulated with highest activity in S phase. Moderately induced by DNA-damage.1 Publication

    <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

    Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with the ribonucleotide reductase inhibitor SML1.4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    36813, 76 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1102 Ribonucleoside-diphosphate reductase variant 1
    CPX-1103 Ribonucleoside-diphosphate reductase variant 2

    Database of interacting proteins

    More...
    DIPi
    DIP-6299N

    Protein interaction database and analysis system

    More...
    IntActi
    P21524, 13 interactors

    Molecular INTeraction database

    More...
    MINTi
    P21524

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YER070W

    <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

    1888
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P21524

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

    More...
    SMRi
    P21524

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P21524

    <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>Domaini1 – 92ATP-conePROSITE-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>Regioni11 – 17Allosteric activator bindingBy similarity7
    Regioni217 – 218Substrate binding2
    Regioni285 – 288Allosteric effector binding, determines substrate specificity4
    Regioni426 – 430Substrate binding5
    Regioni607 – 611Substrate binding5

    <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

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00910000144246

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000057035

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P21524

    KEGG Orthology (KO)

    More...
    KOi
    K10807

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GEFIVVN

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C0QYB

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005144 ATP-cone_dom
    IPR013346 NrdE_NrdA
    IPR000788 RNR_lg_C
    IPR013509 RNR_lsu_N
    IPR008926 RNR_R1-su_N
    IPR039718 Rrm1

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11573 PTHR11573, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03477 ATP-cone, 1 hit
    PF02867 Ribonuc_red_lgC, 1 hit
    PF00317 Ribonuc_red_lgN, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01183 RIBORDTASEM1

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48168 SSF48168, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02506 NrdE_NrdA, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51161 ATP_CONE, 1 hit
    PS00089 RIBORED_LARGE, 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>.<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.

    P21524-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG
    60 70 80 90 100
    VTTIELDNLA AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED
    110 120 130 140 150
    LYRYVNAATG KPAPMISDDV YNIVMENKDK LNSAIVYDRD FQYSYFGFKT
    160 170 180 190 200
    LERSYLLRIN GQVAERPQHL IMRVALGIHG RDIEAALETY NLMSLKYFTH
    210 220 230 240 250
    ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL ISKTAGGIGL
    260 270 280 290 300
    HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY
    310 320 330 340 350
    LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL
    360 370 380 390 400
    FSPTSAPGLS DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG
    410 420 430 440 450
    TPFVVYKDAC NRKSNQKNLG VIKSSNLCCE IVEYSAPDET AVCNLASVAL
    460 470 480 490 500
    PAFIETSEDG KTSTYNFKKL HEIAKVVTRN LNRVIDRNYY PVEEARKSNM
    510 520 530 540 550
    RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY HASMEASCEL
    560 570 580 590 600
    AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS
    610 620 630 640 650
    LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV
    660 670 680 690 700
    DLGIWDEGMK QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA
    710 720 730 740 750
    DRSVYIDQSH SLNLFLRAPT MGKLTSMHFY GWKKGLKTGM YYLRTQAASA
    760 770 780 790 800
    AIQFTIDQKI ADQATENVAD ISNLKRPSYM PSSASYAASD FVPAAVTANA
    810 820 830 840 850
    TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE VPEVPAPTKN
    860 870 880
    EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG
    Length:888
    Mass (Da):99,561
    Last modified:February 1, 1995 - v2
    <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:i56BE1B077916E419
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti329F → L in CAA49151 (PubMed:8121398).Curated1
    Sequence conflicti587 – 589TLR → NLK in CAA49150 (PubMed:8121398).Curated3
    Sequence conflicti666Q → E no nucleotide entry (PubMed:2199320).Curated1
    Sequence conflicti679E → Q no nucleotide entry (PubMed:2199320).Curated1

    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
    U18813 Genomic DNA Translation: AAB64606.1
    X69216 Genomic DNA Translation: CAA49150.1
    X69217 Genomic DNA Translation: CAA49151.1
    BK006939 Genomic DNA Translation: DAA07729.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S50573

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_010993.1, NM_001178961.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YER070W_mRNA; YER070W_mRNA; YER070W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    856801

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YER070W

    <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
    U18813 Genomic DNA Translation: AAB64606.1
    X69216 Genomic DNA Translation: CAA49150.1
    X69217 Genomic DNA Translation: CAA49151.1
    BK006939 Genomic DNA Translation: DAA07729.1
    PIRiS50573
    RefSeqiNP_010993.1, NM_001178961.1

    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
    1ZYZX-ray2.90A/B1-888[»]
    1ZZDX-ray2.60A1-888[»]
    2CVSX-ray2.60A1-888[»]
    2CVTX-ray3.20A1-888[»]
    2CVUX-ray2.90A1-888[»]
    2CVVX-ray2.90A1-888[»]
    2CVWX-ray2.40A1-888[»]
    2CVXX-ray2.20A1-888[»]
    2CVYX-ray2.40A1-888[»]
    2EUDX-ray2.30A1-888[»]
    2ZLFX-ray2.59A1-888[»]
    2ZLGX-ray2.52A1-888[»]
    3K8TX-ray2.10A1-888[»]
    3PAWX-ray6.61A/B/C/D1-888[»]
    3RSRX-ray2.30A1-888[»]
    3S87X-ray2.25A1-888[»]
    3S8AX-ray2.90A1-888[»]
    3S8BX-ray2.80A1-888[»]
    3S8CX-ray2.77A1-888[»]
    3TB9X-ray2.53A1-888[»]
    3TBAX-ray2.80A1-888[»]
    ProteinModelPortaliP21524
    SMRiP21524
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36813, 76 interactors
    ComplexPortaliCPX-1102 Ribonucleoside-diphosphate reductase variant 1
    CPX-1103 Ribonucleoside-diphosphate reductase variant 2
    DIPiDIP-6299N
    IntActiP21524, 13 interactors
    MINTiP21524
    STRINGi4932.YER070W

    PTM databases

    iPTMnetiP21524

    Proteomic databases

    MaxQBiP21524
    PaxDbiP21524
    PRIDEiP21524

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYER070W_mRNA; YER070W_mRNA; YER070W
    GeneIDi856801
    KEGGisce:YER070W

    Organism-specific databases

    SGDiS000000872 RNR1

    Phylogenomic databases

    GeneTreeiENSGT00910000144246
    HOGENOMiHOG000057035
    InParanoidiP21524
    KOiK10807
    OMAiGEFIVVN
    OrthoDBiEOG092C0QYB

    Enzyme and pathway databases

    UniPathwayi
    UPA00326

    BioCyciMetaCyc:YER070W-MONOMER
    YEAST:YER070W-MONOMER
    BRENDAi1.17.4.1 984

    Miscellaneous databases

    EvolutionaryTraceiP21524

    Protein Ontology

    More...
    PROi
    PR:P21524

    Family and domain databases

    InterProiView protein in InterPro
    IPR005144 ATP-cone_dom
    IPR013346 NrdE_NrdA
    IPR000788 RNR_lg_C
    IPR013509 RNR_lsu_N
    IPR008926 RNR_R1-su_N
    IPR039718 Rrm1
    PANTHERiPTHR11573 PTHR11573, 1 hit
    PfamiView protein in Pfam
    PF03477 ATP-cone, 1 hit
    PF02867 Ribonuc_red_lgC, 1 hit
    PF00317 Ribonuc_red_lgN, 1 hit
    PRINTSiPR01183 RIBORDTASEM1
    SUPFAMiSSF48168 SSF48168, 1 hit
    TIGRFAMsiTIGR02506 NrdE_NrdA, 1 hit
    PROSITEiView protein in PROSITE
    PS51161 ATP_CONE, 1 hit
    PS00089 RIBORED_LARGE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiRIR1_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: P21524
    Secondary accession number(s): D3DLX5
    <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: May 1, 1991
    Last sequence update: February 1, 1995
    Last modified: December 5, 2018
    This is version 187 of the entry and version 2 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, Complete proteome, 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
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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