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Entry version 111 (25 May 2022)
Sequence version 1 (01 Oct 1996)
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Protein

Dynamin-like protein A

Gene

dynA

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

Mediates lipid mixing of vesicles and full mixing of their contents in the absence and presence of GTP. Tethers and mixes small vesicles better than larger ones, indicating a curvature preference. GTP slows down DynA-mediated lipid fusion, perhaps controlling its activity. Prefers phospholipid composition close to the B.subtilis membrane; requires phosphatidylglycerol for fusion has no activity on pure phosphatidylethanolamine vesicles (PubMed:31361971).

Regulates membrane lipid diffusion. Required to prevent membrane damage when exposed to low levels of membrane-damaging antibiotics or to bacteriophage. Probably surveys the cell membrane for stress; localizes to sites of membrane damage (treatment with nisin) and forms foci in cells treated with pore-forming compounds (CCCP). May assist membrane repair, possibly by membrane tethering and fusion (PubMed:26530236).

Probably functions both in early and late cell division, affects the proper formation of the FtsZ ring. Plays a non-redundant role with flottilin (floT) in membrane dynamics and cell shape. Probably able to bend membranes (PubMed:23249255).

Tethers liposomes and mediates their fusion; this does not require GTPase activity or the presence of GTP. Both GTPase domains (dynamin-type G) are required for GTPase activity (PubMed:21205012).

4 Publications

Has intrinsic affinity for membranes and membrane distortion capability; causes tubulation and membrane distortion when expressed in a Drosophila cell line.

1 Publication

Miscellaneous

Strain PSB025 / 25152 does not have the SP-beta prophage.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 '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

Mg2+1 PublicationNote: Requires Mg2+ for membrane fusion.1 Publication

<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

  • cell septum assembly Source: CACAO
  • regulation of cell shape Source: UniProtKB-KW

<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 processCell cycle, Cell division, Cell shape
LigandGTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU22030-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:
Dynamin-like protein A1 Publication
Short name:
DynA1 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:dynA1 Publication
Synonyms:ypbR
Ordered Locus Names:BSU22030
<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

Keywords - Cellular componenti

Cell membrane, Membrane

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

<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

No visible phenotype (PubMed:21205012). 5% of cells have a double septa, 2% of cells are very long. Double dynA-ezrA mutants have longer cells with more double septa than either deletion alone. Double dynA-floT deletions are highly elongated, filamentous and have strong defects in cell shape; cells grow very slowly with an extended lag phase. Double dynA-mreB deletions have strong cell shape defects (PubMed:23249255). Double dynA-floT deletions are less motile than single floT deletions (PubMed:26842743). Increased lipid mobility in the cell membrane. Severe decrease in growth on nisin (causes membrane pore formation) with significant membrane deformation and damage, intermediate decrease in growth on antibiotics acting on lipid II or the membrane (bacitracin and daptomycin). No effect on growth on vancomycin (blocks peptidoglycan cross-links) or gramicidin D (makes small pores). 20-50% increased susceptibility to phage phi29 and SPbeta (PubMed:26530236).4 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>Mutagenesisi56K → A: No change in membrane fusion. Still binds GTP, no GTPase activity. No longer binds GTP, no GTPase activity; when associated with A-56. Double mutant causes better vesicle and content mixing than wild-type. 2 Publications1
Mutagenesisi625K → A: No change in membrane fusion. Still binds GTP, no GTPase activity. No longer binds GTP, no GTPase activity; when associated with A-625. Double mutant causes better vesicle and content mixing than wild-type. 2 Publications1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000496821 – 1193Dynamin-like protein AAdd BLAST1193

Proteomic databases

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

More...
PaxDbi
P54159

PRoteomics IDEntifications database

More...
PRIDEi
P54159

<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 in solution (Probable). Both D1 and D2 domains interact with YwpG, YneK interacts only with D1 while RNase Y (rny) only interacts with whole protein (PubMed:23060960). Probably oligomerizes at damaged membrane sites (Probable).

2 Publications1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P54159, 1 interactor

STRING: functional protein association networks

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STRINGi
224308.BSU22030

<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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P54159

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

<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>Regioni1 – 609D1, associates with and fuses membranes, tethers lipsomes1 PublicationAdd BLAST609
Regioni50 – 57G1 motif D1PROSITE-ProRule annotationCurated8
Regioni76 – 78G2 motif D1PROSITE-ProRule annotationCurated3
Regioni141 – 144G3 motif D1PROSITE-ProRule annotationCurated4
Regioni199 – 202G4 motif D1PROSITE-ProRule annotationCurated4
Regioni561 – 1193D2, does not associate with membranes1 PublicationAdd BLAST633
Regioni619 – 626G1 motif D2Curated8
Regioni645 – 647G2 motif D2Curated3
Regioni774 – 777G3 motif D2Curated4
Regioni837 – 840G4 motif D2Curated4

<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

Has 2 similar domains, D1 (approximately residues 1-600) and D2 (approximately residues 601-1193). D1 is able to bind membranes, tether liposomes and cause membrane fusion in the absence of D2; both regions are required for GTPase activity. Possibly the fusion of 2 dynamin-like genes (PubMed:21205012). D1 alone promotes membrane tethering but requires D2 for stable tethering and content mixing (PubMed:31361971).2 Publications

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0699, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
FYVMDYN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P54159

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR045063, Dynamin_N
IPR027094, Mitofusin_fam
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR10465, PTHR10465, 2 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF00350, Dynamin_N, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits

<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.

P54159-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDQNRKELL HKTGELYKQF IENQDEQRAA KLAAVMKKAA DEEVYIAFTG
60 70 80 90 100
HYSAGKSSLL NCLLMENILP TSPIPTSANL VVIRNGEKRV RLHTTDGACA
110 120 130 140 150
ELEGTYQKDK VQQYCKDGEQ IESVEIFDRY TEIDSGVAYI DTPGIDSTDD
160 170 180 190 200
AHFLSAASIL HQADALFYVV HYNHVHAEEN VKFLRSIKES IPNVYFIVNQ
210 220 230 240 250
IDRHDETETK FGDYQAQVEE MLCNEGISRE ALYFTSVTEP DHPFNQMGAL
260 270 280 290 300
REELSRIEQQ SKSNMQALTE QKVRNLLKEH TEMLKKDETG APSFAEQLNI
310 320 330 340 350
HTGLVQSLRD QLDEAEKQMT EAEKRMQEEI NRILKNANLT PFEMRELAAA
360 370 380 390 400
FLESQEPSFK TGFFFSKAKT AQERDKRRNA FFSDVAKRTE AEADWHMIDT
410 420 430 440 450
LHKLAKVFDV YTAESEKLIQ AYRTPLDISI IEHAVKHGAA FSSEYVLQYT
460 470 480 490 500
KDLAELIRKE AKREAADIIK VLSAMVKERV SKDVQTINDR LVQESEKLVF
510 520 530 540 550
LQEQARLENN AREKTDRLWA IWEEESACPM HIDTEWFKSK KTRVAAPEQK
560 570 580 590 600
QGRSQLTAQP MPKSEIKMEQ EMPLQDQIKR FYTLSDILGE CSMLLKQTSA
610 620 630 640 650
FRERVKRLEE RKFTLALFGG FSSGKSSFAN ALVGERVLPS SPTPTTATIN
660 670 680 690 700
KITKPINGNL NKTANVVFKT EDDLTAEILQ LTGIPKEPAG RSFTEKWEKA
710 720 730 740 750
VKKNRLQEEH VKLISNFLLA YEKYQQYIQE QKKLTIPLSE LKPYVAEETT
760 770 780 790 800
ACAVKEVTVY YTCPLTEKGI TIVDTPGASS MNKRHTELAF QYIKDADAFF
810 820 830 840 850
YMTYYQHSFS KGDRSFLRKL GLVKESLSMD KMFFIINAAD LAKDKTELET
860 870 880 890 900
VTDYVSAELV KEGVYEPQLF TVSSKEELVG KPESFYNQFS KVRKHLDRFI
910 920 930 940 950
EVDVKKASAA QLSSEADKLC ETVFQLHQSQ HQSREEKEAQ KQCLMLSFER
960 970 980 990 1000
TAADIEKRRN SKTIIEKVKK DTREQLYHIA QRLSYFANDL LKSAFHPGLQ
1010 1020 1030 1040 1050
NGDWKKNVSK AMTTALHEYL FEYIQEIKTL DVRMSGFIER HINEEWLDHF
1060 1070 1080 1090 1100
QKTLNEDGYF SVYAGDQHSN GIQLKEVEPE IEERAFEQEL KEIKSPKQFF
1110 1120 1130 1140 1150
EQKGKATFIE AVRMKLTKIT EAWIKNEEES LISHYTAHLR RLQEDMGEKA
1160 1170 1180 1190
IAQITDQKET YLRGYAEGEH AKEIEMAYQA CISWKNSDNT IKM
Length:1,193
Mass (Da):137,385
Last modified:October 1, 1996 - 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:i33DCDE5B6E93D7AB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L77246 Genomic DNA Translation: AAA96615.1
AL009126 Genomic DNA Translation: CAB14120.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E69933

NCBI Reference Sequences

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RefSeqi
NP_390085.1, NC_000964.3
WP_003230755.1, NZ_JNCM01000036.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB14120; CAB14120; BSU_22030

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
939071

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU22030

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.2407

<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
L77246 Genomic DNA Translation: AAA96615.1
AL009126 Genomic DNA Translation: CAB14120.1
PIRiE69933
RefSeqiNP_390085.1, NC_000964.3
WP_003230755.1, NZ_JNCM01000036.1

3D structure databases

AlphaFoldDBiP54159
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Protein-protein interaction databases

IntActiP54159, 1 interactor
STRINGi224308.BSU22030

Proteomic databases

PaxDbiP54159
PRIDEiP54159

Genome annotation databases

EnsemblBacteriaiCAB14120; CAB14120; BSU_22030
GeneIDi939071
KEGGibsu:BSU22030
PATRICifig|224308.179.peg.2407

Phylogenomic databases

eggNOGiCOG0699, Bacteria
OMAiFYVMDYN
PhylomeDBiP54159

Enzyme and pathway databases

BioCyciBSUB:BSU22030-MONOMER

Family and domain databases

Gene3Di3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR045063, Dynamin_N
IPR027094, Mitofusin_fam
IPR027417, P-loop_NTPase
PANTHERiPTHR10465, PTHR10465, 2 hits
PfamiView protein in Pfam
PF00350, Dynamin_N, 2 hits
SUPFAMiSSF52540, SSF52540, 2 hits

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 nameiDYNA_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: P54159
<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, 1996
Last sequence update: October 1, 1996
Last modified: May 25, 2022
This is version 111 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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