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UniProtKB - P58301 (RAD50_PYRFU)

Entry version 151 (25 May 2022)
Sequence version 1 (26 Sep 2001)
Previous versions | rss
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Protein

DNA double-strand break repair Rad50 ATPase

Gene

rad50

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

Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair (PubMed:11029422, PubMed:18957200).

The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200).

Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex (PubMed:24493214).

The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity (PubMed:24493214).

ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity (PubMed:24493214).

Has also reversible adenylate kinase activity (PubMed:17349953).

4 Publications

<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

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per homodimer.UniRule annotation1 Publication

<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

The adenylate kinase inhibitor P1,P5-di(adenosine-5') pentaphosphate (Ap5A) inhibits adenylate kinase activity, but does not affect ATPase activity.1 Publication

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 sitei12ATPCombined sources3 Publications1
Binding sitei140ATPCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi444ZincUniRule annotation1 Publication1
Metal bindingi447ZincUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 38ATPCombined sources3 Publications7
Nucleotide bindingi60 – 64ATPCombined sources3 Publications5
Nucleotide bindingi763 – 764ATPCombined sources2 Publications2
Nucleotide bindingi791 – 796ATPCombined sources2 Publications6

<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

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 functionHydrolase
Biological processDNA damage, DNA repair
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<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:
DNA double-strand break repair Rad50 ATPaseUniRule annotationCurated
Alternative name(s):
pfRad501 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:rad501 PublicationUniRule annotation
Ordered Locus Names:PF1167
<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 lineageiArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›
<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 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>Mutagenesisi793S → R: Prevents ATP binding and disrupts the communication among the other ATP-binding loops. Prevents also Rad50 dimerization. Decreases both ATPase and adenylate kinase activities. 3 Publications1
Mutagenesisi797R → G: Decreases ATP-induced dimerization. Increases DNA end tethering. 1 Publication1
Mutagenesisi802L → W: Destabilizes the ATP-dimerized state. Promotes HerA/NurA activity. 1 Publication1
Mutagenesisi805R → E: Increases ATP-induced dimerization. Increases DNA end tethering. Fails to promote HerA/NurA 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001386611 – 882DNA double-strand break repair Rad50 ATPaseAdd BLAST882

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P58301

<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

Homodimer (PubMed:10892749, PubMed:14698290).

Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits (PubMed:11371344, PubMed:21441914, PubMed:22102415). Homodimerization is promoted by ATP binding (PubMed:10892749).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-54373N

Protein interaction database and analysis system

More...IntActi		P58301, 2 interactors

Molecular INTeraction database

More...MINTi		P58301

STRING: functional protein association networks

More...STRINGi		186497.PF1167

<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

1882
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P58301

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

More...SMRi		P58301

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		P58301

<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%5Fand%5Fdomains%5Fsection">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>Domaini399 – 496Zinc-hookUniRule annotationAdd BLAST98

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili257 – 588UniRule annotationAdd BLAST332
Coiled coili629 – 735UniRule annotationAdd BLAST107

<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

Binding of ATP induces a closed, compact conformation of the Rad50/Mre11 complex. ATP hydrolysis opens the complex.1 Publication
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.UniRule annotation1 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

Belongs to the SMC family. RAD50 subfamily.UniRule annotationCurated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		arCOG00368, Archaea

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004785_0_2_2

Identification of Orthologs from Complete Genome Data

More...OMAi		VNFIYGP

Database of Orthologous Groups

More...OrthoDBi		1771at2157

Database for complete collections of gene phylogenies

More...PhylomeDBi		P58301

Family and domain databases

Conserved Domains Database

More...CDDi		cd03240, ABC_Rad50, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.300, 2 hits

HAMAP database of protein families

More...HAMAPi		MF_00449, RAD50, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR045171, ABC_Rad50
IPR003959, ATPase_AAA_core
IPR027417, P-loop_NTPase
IPR038729, Rad50/SbcC_AAA
IPR022982, Rad50_ATPase_archaeal
IPR013134, Zn_hook_RAD50

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13304, AAA_21, 1 hit
PF13476, AAA_23, 1 hit
PF04423, Rad50_zn_hook, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51131, ZN_HOOK, 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.

P58301-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLERVTVKN FRSHSDTVVE FKEGINLIIG QNGSGKSSLL DAILVGLYWP 
        60         70         80         90        100
LRIKDIKKDE FTKVGARDTY IDLIFEKDGT KYRITRRFLK GYSSGEIHAM 
       110        120        130        140        150
KRLVGNEWKH VTEPSSKAIS AFMEKLIPYN IFLNAIYIRQ GQIDAILESD 
       160        170        180        190        200
EAREKVVREV LNLDKFETAY KKLSELKKTI NNRIKEYRDI LARTENIEEL 
       210        220        230        240        250
IKENEQELIQ VLQEISKIEE VLPSKRSKVD MLRKEVLRLE ETKVEIENSE 
       260        270        280        290        300
RLLEKRRGDK RTLEERIKNT EEYLEKLKEK EKELEEQVKE ITSIKKDVDA 
       310        320        330        340        350
YLALKEFKNE YLDKKYKIEK ELTRVEELIN EIQKRIEELN EKESEKEKLE 
       360        370        380        390        400
NEKKEILNKL AILEKDHQLY EEIKAKKENL RQLKEKLGDK SPEDIKKLLE 
       410        420        430        440        450
ELETKKTTIE EERNEITQRI GELKNKIGDL KTAIEELKKA KGKCPVCGRE 
       460        470        480        490        500
LTDEHREELL SKYHLDLNNS KNTLAKLIDR KSELERELRR IDMEIKRLTP 
       510        520        530        540        550
LLTVAEQIRS IEEELNVVNL EKIEKNATEY EKLLEELRTL EGRIRGLAED 
       560        570        580        590        600
LKKLAPLEKK LAALIHKKQE LEKELKELNT KLESFGFKSV EDLDSKLREL 
       610        620        630        640        650
EEIYKRYLTL LNSKKELEIT QREIAKAKET LEMSFEELAE VEADIERIEK 
       660        670        680        690        700
KLSQLKQKYN EEEYKKKREE KEELEKELAR LEAQKKELEK RRDTIKSTLE 
       710        720        730        740        750
KLKAEKENRE RVKKEIKDLE KAKDFTEELI EKVKKYKALA REAALSKIGE 
       760        770        780        790        800
LASEIFAEFT EGKYSEVVVR AEENKVRLFV VWEGKERPLT FLSGGERIAL 
       810        820        830        840        850
GLAFRLAMSL YLAGEISLLI LDEPTPYLDE ERRRKLITIM ERYLKKIPQV 
       860        870        880 
ILVSHDEELK DAADHVIRIS LENGSSKVEV VS
Length:882
Mass (Da):103,840
Last modified:September 26, 2001 - 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:i3ADCBD250382A99E
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
AE009950 Genomic DNA Translation: AAL81291.1

NCBI Reference Sequences

More...RefSeqi		WP_011012307.1, NZ_CP023154.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAL81291; AAL81291; PF1167

Database of genes from NCBI RefSeq genomes

More...GeneIDi		41712975

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		pfu:PF1167

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|186497.12.peg.1227

<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
AE009950 Genomic DNA Translation: AAL81291.1
RefSeqiWP_011012307.1, 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
1F2TX-ray1.60A1-149[»]
B735-882[»]
1F2UX-ray1.60A/C1-149[»]
B/D735-882[»]
1II8X-ray3.02A1-195[»]
B709-882[»]
1L8DX-ray2.20A/B396-506[»]
1US8X-ray2.10A1-147[»]
B739-882[»]
3QKRX-ray3.40A1-195[»]
B704-882[»]
3QKSX-ray2.10A1-195[»]
B704-882[»]
3QKTX-ray1.90A/B/C/D1-177[»]
A/B/C/D726-882[»]
3QKUX-ray3.30A/B1-187[»]
A/B716-882[»]
4NCHX-ray2.30A/B1-177[»]
A/B726-882[»]
4NCIX-ray2.30A1-177[»]
A726-882[»]
4NCJX-ray2.00A/B/C/D1-177[»]
A/B/C/D726-882[»]
4NCKX-ray1.99A/B1-177[»]
A/B726-882[»]
6ZFFX-ray3.00A/B378-516[»]
AlphaFoldDBiP58301
SMRiP58301
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-54373N
IntActiP58301, 2 interactors
MINTiP58301
STRINGi186497.PF1167

Proteomic databases

PRIDEiP58301

Genome annotation databases

EnsemblBacteriaiAAL81291; AAL81291; PF1167
GeneIDi41712975
KEGGipfu:PF1167
PATRICifig|186497.12.peg.1227

Phylogenomic databases

eggNOGiarCOG00368, Archaea
HOGENOMiCLU_004785_0_2_2
OMAiVNFIYGP
OrthoDBi1771at2157
PhylomeDBiP58301

Miscellaneous databases

EvolutionaryTraceiP58301

Family and domain databases

CDDicd03240, ABC_Rad50, 1 hit
Gene3Di3.40.50.300, 2 hits
HAMAPiMF_00449, RAD50, 1 hit
InterProiView protein in InterPro
IPR045171, ABC_Rad50
IPR003959, ATPase_AAA_core
IPR027417, P-loop_NTPase
IPR038729, Rad50/SbcC_AAA
IPR022982, Rad50_ATPase_archaeal
IPR013134, Zn_hook_RAD50
PfamiView protein in Pfam
PF13304, AAA_21, 1 hit
PF13476, AAA_23, 1 hit
PF04423, Rad50_zn_hook, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51131, ZN_HOOK, 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 nameiRAD50_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: P58301
<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: September 26, 2001
Last sequence update: September 26, 2001
Last modified: May 25, 2022
This is version 151 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 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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