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Entry version 151 (12 Aug 2020)
Sequence version 6 (23 Jan 2007)
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Protein

Ornithine carbamoyltransferase, anabolic

Gene

argF

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.1 Publication

Miscellaneous

It interacts physically with carbamoyl-phosphate synthetase (CKase), forming a channeling cluster for carbamoyl phosphate. This prevents the thermodenaturation of carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate (PubMed:9501170).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by the bisubstrate delta-N-phosphonoacetyl-L-ornithine (PALO).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. KM=0.13 mM for L-ornithine1 Publication
  2. KM=0.13 mM for carbamoyl phosphate1 Publication

    pH dependencei

    Optimum pH is 6.5 (at 55 degrees Celsius).2 Publications

    Temperature dependencei

    Extreme thermal stability. It maintains about 50% of its activity after heat treatment for 60 min at 100 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase, anabolic (argF), Ornithine carbamoyltransferase (argF)
    2. Argininosuccinate synthase (argG), Argininosuccinate synthase (argG)
    3. Argininosuccinate lyase (argH), Argininosuccinate lyase (argH)
    This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei84Carbamoyl phosphate1 Publication1
    Binding sitei108Carbamoyl phosphateUniRule annotation1
    Binding sitei166OrnithineUniRule annotation1
    Binding sitei230OrnithineUniRule annotation1
    Binding sitei298Carbamoyl phosphateUniRule annotation1

    <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 functionTransferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    PFUR186497:G1FZR-621-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.3.3, 5243

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

    More...
    UniPathwayi
    UPA00068;UER00112

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Ornithine carbamoyltransferase, anabolic1 Publication (EC:2.1.3.3UniRule annotation)
    Short name:
    OTCase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:argF1 Publication
    Ordered Locus Names:PF0594
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri186497 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000001013 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    <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

    GO - Cellular componenti

    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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi22W → A: Decreased heat stability. 1 Publication1
    Mutagenesisi26E → Q: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi30M → A: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi34W → A: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi228Y → C: Becomes active at low temperatures; when associated with G-278. 1 Publication1
    Mutagenesisi241A → D: Becomes active at low temperatures; when associated with G-278. 1 Publication1
    Mutagenesisi278E → G: Becomes active at low temperatures; when associated with C-228 or D-241. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00001130732 – 315Ornithine carbamoyltransferase, anabolicAdd BLAST314

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q51742

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homododecamer (tetramer of trimers).

    1 Publication1 Publication

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-48301N

    Protein interaction database and analysis system

    More...
    IntActi
    Q51742, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    186497.PF0594

    <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

    1315
    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
    Q51742

    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
    Q51742

    <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

    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>Regioni57 – 60Carbamoyl phosphate bindingUniRule annotation4
    Regioni135 – 138Carbamoyl phosphate bindingUniRule annotation4
    Regioni234 – 235Ornithine bindingUniRule annotation2
    Regioni270 – 271Carbamoyl phosphate bindingUniRule annotation2

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The monomer folds into two domains of similar size. The N-terminal domain is the carbamoylphosphate-binding domain; ornithine binds to the C-terminal domain.1 Publication

    <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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00912, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_043846_3_2_2

    KEGG Orthology (KO)

    More...
    KOi
    K00611

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DGNNVCN

    Database of Orthologous Groups

    More...
    OrthoDBi
    43727at2157

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1370, 2 hits

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01109, OTCase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006132, Asp/Orn_carbamoyltranf_P-bd
    IPR006130, Asp/Orn_carbamoylTrfase
    IPR036901, Asp/Orn_carbamoylTrfase_sf
    IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
    IPR002292, Orn/put_carbamltrans
    IPR024904, OTCase_ArgI

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00185, OTCace, 1 hit
    PF02729, OTCace_N, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00100, AOTCASE
    PR00102, OTCASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53671, SSF53671, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00658, orni_carb_tr, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00097, CARBAMOYLTRANSFERASE, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q51742-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVVSLAGRDL LCLQDYTAEE IWTILETAKM FKIWQKIGKP HRLLEGKTLA
    60 70 80 90 100
    MIFQKPSTRT RVSFEVAMAH LGGHALYLNA QDLQLRRGET IADTARVLSR
    110 120 130 140 150
    YVDAIMARVY DHKDVEDLAK YATVPVINGL SDFSHPCQAL ADYMTIWEKK
    160 170 180 190 200
    GTIKGVKVVY VGDGNNVAHS LMIAGTKLGA DVVVATPEGY EPDEKVIKWA
    210 220 230 240 250
    EQNAAESGGS FELLHDPVKA VKDADVIYTD VWASMGQEAE AEERRKIFRP
    260 270 280 290 300
    FQVNKDLVKH AKPDYMFMHC LPAHRGEEVT DDVIDSPNSV VWDQAENRLH
    310
    AQKAVLALVM GGIKF
    Length:315
    Mass (Da):35,181
    Last modified:January 23, 2007 - v6
    <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:i14404FBDC2ECCB95
    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 conflicti206E → ER in CAA73260 (PubMed:9288929).Curated1
    Sequence conflicti209Missing in CAA67609 (PubMed:9288929).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
    X99225 Genomic DNA Translation: CAA67609.1
    Y12727 Genomic DNA Translation: CAA73260.1
    AE009950 Genomic DNA Translation: AAL80718.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T45077

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011011713.1, NZ_CP023154.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAL80718; AAL80718; PF0594

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    41712399

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pfu:PF0594

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|186497.12.peg.623

    <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
    X99225 Genomic DNA Translation: CAA67609.1
    Y12727 Genomic DNA Translation: CAA73260.1
    AE009950 Genomic DNA Translation: AAL80718.1
    PIRiT45077
    RefSeqiWP_011011713.1, NZ_CP023154.1

    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
    1A1SX-ray2.70A2-315[»]
    1PVVX-ray1.87A1-315[»]
    SMRiQ51742
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48301N
    IntActiQ51742, 1 interactor
    STRINGi186497.PF0594

    Proteomic databases

    PRIDEiQ51742

    Genome annotation databases

    EnsemblBacteriaiAAL80718; AAL80718; PF0594
    GeneIDi41712399
    KEGGipfu:PF0594
    PATRICifig|186497.12.peg.623

    Phylogenomic databases

    eggNOGiarCOG00912, Archaea
    HOGENOMiCLU_043846_3_2_2
    KOiK00611
    OMAiDGNNVCN
    OrthoDBi43727at2157

    Enzyme and pathway databases

    UniPathwayiUPA00068;UER00112
    BioCyciPFUR186497:G1FZR-621-MONOMER
    BRENDAi2.1.3.3, 5243

    Miscellaneous databases

    EvolutionaryTraceiQ51742

    Family and domain databases

    Gene3Di3.40.50.1370, 2 hits
    HAMAPiMF_01109, OTCase, 1 hit
    InterProiView protein in InterPro
    IPR006132, Asp/Orn_carbamoyltranf_P-bd
    IPR006130, Asp/Orn_carbamoylTrfase
    IPR036901, Asp/Orn_carbamoylTrfase_sf
    IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
    IPR002292, Orn/put_carbamltrans
    IPR024904, OTCase_ArgI
    PfamiView protein in Pfam
    PF00185, OTCace, 1 hit
    PF02729, OTCace_N, 1 hit
    PRINTSiPR00100, AOTCASE
    PR00102, OTCASE
    SUPFAMiSSF53671, SSF53671, 1 hit
    TIGRFAMsiTIGR00658, orni_carb_tr, 1 hit
    PROSITEiView protein in PROSITE
    PS00097, CARBAMOYLTRANSFERASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiOTCA_PYRFU
    <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: Q51742
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: August 12, 2020
    This is version 151 of the entry and version 6 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 programProkaryotic 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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