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Entry version 131 (26 Feb 2020)
Sequence version 1 (01 Oct 1994)
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Protein

Protein-arginine kinase

Gene

mcsB

Organism
Bacillus subtilis (strain 168)
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

Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.5 Publications

<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

Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB (By similarity). The McsB kinase is inhibited in nonstressed cells by direct interaction with ClpC; upon heat exposure, the interaction of McsB with ClpC is dramatically decreased, leading to McsB release and activation during heat stress. Its kinase activity is counteracted by the protein-arginine-phosphatase YwlE in vivo. Requires McsA for full kinase activity.UniRule annotation4 Publications

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 sitei92ATPUniRule annotation1
Binding sitei125ATPUniRule annotation1

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 bindingi27 – 31ATPUniRule annotation5
Nucleotide bindingi176 – 180ATPUniRule annotation5
Nucleotide bindingi207 – 212ATPUniRule annotation6

<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, Kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU00850-MONOMER

<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:
Protein-arginine kinaseUniRule annotation (EC:2.7.14.1UniRule annotation1 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:mcsBUniRule annotation
Synonyms:yacI
Ordered Locus Names:BSU00850
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene show a defect in the delocalization of competence proteins that is not related to altered expression of the com genes on the levels of either transcription or translation. Inactivation of mcsB also decreases transformability (PubMed:19226326). CtsR is no more degraded (PubMed:30962626).2 Publications

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>Mutagenesisi121E → A: Stabilizes quantity of CtsR to an extent comparable to that observed for the mcsB deletion, indicating a loss of protein phosphorylation activity of McsB in vivo. 1 Publication1
Mutagenesisi210Y → A: Stabilizes quantity of CtsR to an extent a little lower to that observed for the mcsB deletion, indicating a decrease of protein phosphorylation activity of McsB in vivo. 1 Publication1
Mutagenesisi272R → A: Stabilizes quantity of CtsR to an extent a little lower to that observed for the mcsB deletion, indicating a decrease of protein phosphorylation activity of McsB in vivo. 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_00002120171 – 363Protein-arginine kinaseAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei29Phosphoarginine; by autocatalysis1 Publication1
Modified residuei40Phosphoarginine; by autocatalysis1 Publication1
Modified residuei86Phosphoarginine; by autocatalysis1 Publication1
Modified residuei190Phosphoarginine; by autocatalysis1 Publication1
Modified residuei255Phosphoarginine; by autocatalysis2 Publications1
Modified residuei269Phosphoarginine; by autocatalysis1 Publication1
Modified residuei272Phosphoarginine; by autocatalysis1 Publication1
Modified residuei346Phosphoarginine; by autocatalysis1 Publication1

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

Autophosphorylated on Arg residues. Phosphorylation on Arg-40 and Arg-86 are up-regulated upon stress conditions.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P37570

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

More...
PaxDbi
P37570

PRoteomics IDEntifications database

More...
PRIDEi
P37570

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P37570

<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

Is repressed by the transcriptional regulator CtsR. Forms part of an operon with ctsR, mcsA and clpC.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%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

Interacts with CtsR in its autophosphorylated form.

Interacts with McsA in nonstressed as well as in heat-stressed cells, whereas strongly interacts with ClpC only in nonstressed cells.

2 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P37570, 1 interactor

Molecular INTeraction database

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MINTi
P37570

STRING: functional protein association networks

More...
STRINGi
224308.BSU00850

<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

3D structure databases

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

More...
SMRi
P37570

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini24 – 254Phosphagen kinase C-terminalUniRule annotationAdd BLAST231

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi337 – 342RDXXRA motif of the pArg binding pocket involved in allosteric regulationUniRule annotation6

<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 ATP:guanido phosphotransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG41066A3 Bacteria
COG3869 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P37570

KEGG Orthology (KO)

More...
KOi
K19405

Identification of Orthologs from Complete Genome Data

More...
OMAi
ACPTNVG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P37570

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07930 bacterial_phosphagen_kinase, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00602 Prot_Arg_kinase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023660 Arg_Kinase
IPR000749 ATP-guanido_PTrfase
IPR022415 ATP-guanido_PTrfase_AS
IPR022414 ATP-guanido_PTrfase_cat
IPR014746 Gln_synth/guanido_kin_cat_dom

The PANTHER Classification System

More...
PANTHERi
PTHR11547 PTHR11547, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00217 ATP-gua_Ptrans, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55931 SSF55931, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00112 PHOSPHAGEN_KINASE, 1 hit
PS51510 PHOSPHAGEN_KINASE_C, 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.

P37570-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLKHFIQDA LSSWMKQKGP ESDIVLSSRI RLARNFEHIR FPTRYSNEEA
60 70 80 90 100
SSIIQQFEDQ FSEQEIPGIG KFVLIRMNDA QPLEKRVLVE KHLISPNLTE
110 120 130 140 150
SPFGGCLLSE NEEVSVMLNE EDHIRIQCLF PGFQLLEAMK AANQVDDWIE
160 170 180 190 200
EKVDYAFNEQ RGYLTSCPTN VGTGLRASVM MHLPALVLTR QINRIIPAIN
210 220 230 240 250
QLGLVVRGIY GEGSEAVGNI FQISNQITLG KSEQDIVEDL NSVAAQLIEQ
260 270 280 290 300
ERSAREAIYQ TSKIELEDRV YRSYGVLSNC RMIESKETAK CLSDVRLGID
310 320 330 340 350
LGIIKGLSSN ILNELMILTQ PGFLQQYSGG ALRPNERDIR RAALIRERLH
360
LEMNGKRQED ESI
Length:363
Mass (Da):41,124
Last modified:October 1, 1994 - 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:i923E4A6445A752EF
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D26185 Genomic DNA Translation: BAA05319.1
AL009126 Genomic DNA Translation: CAB11861.1
U02604 Unassigned DNA Translation: AAA19232.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S66114

NCBI Reference Sequences

More...
RefSeqi
NP_387966.1, NC_000964.3
WP_003235007.1, NZ_JNCM01000029.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB11861; CAB11861; BSU00850

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
936939

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU00850

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.86

<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
D26185 Genomic DNA Translation: BAA05319.1
AL009126 Genomic DNA Translation: CAB11861.1
U02604 Unassigned DNA Translation: AAA19232.1
PIRiS66114
RefSeqiNP_387966.1, NC_000964.3
WP_003235007.1, NZ_JNCM01000029.1

3D structure databases

SMRiP37570
ModBaseiSearch...

Protein-protein interaction databases

IntActiP37570, 1 interactor
MINTiP37570
STRINGi224308.BSU00850

PTM databases

iPTMnetiP37570

Proteomic databases

jPOSTiP37570
PaxDbiP37570
PRIDEiP37570

Genome annotation databases

EnsemblBacteriaiCAB11861; CAB11861; BSU00850
GeneIDi936939
KEGGibsu:BSU00850
PATRICifig|224308.179.peg.86

Phylogenomic databases

eggNOGiENOG41066A3 Bacteria
COG3869 LUCA
InParanoidiP37570
KOiK19405
OMAiACPTNVG
PhylomeDBiP37570

Enzyme and pathway databases

BioCyciBSUB:BSU00850-MONOMER

Family and domain databases

CDDicd07930 bacterial_phosphagen_kinase, 1 hit
HAMAPiMF_00602 Prot_Arg_kinase, 1 hit
InterProiView protein in InterPro
IPR023660 Arg_Kinase
IPR000749 ATP-guanido_PTrfase
IPR022415 ATP-guanido_PTrfase_AS
IPR022414 ATP-guanido_PTrfase_cat
IPR014746 Gln_synth/guanido_kin_cat_dom
PANTHERiPTHR11547 PTHR11547, 1 hit
PfamiView protein in Pfam
PF00217 ATP-gua_Ptrans, 1 hit
SUPFAMiSSF55931 SSF55931, 1 hit
PROSITEiView protein in PROSITE
PS00112 PHOSPHAGEN_KINASE, 1 hit
PS51510 PHOSPHAGEN_KINASE_C, 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 nameiMCSB_BACSU
<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: P37570
<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: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 26, 2020
This is version 131 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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