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Entry version 129 (07 Oct 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Proteasome-activating nucleotidase

Gene

pan

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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

ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.UniRule annotation5 Publications

<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

ATPase activity is inhibited by EDTA, N-ethylmaleimide (NEM) and p-chloromercuriphenyl-sulfonic acid (PCMS) in vitro.2 Publications

<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=497 µM for ATP1 Publication
  2. KM=307 µM for CTP1 Publication
  1. Vmax=3.5 µmol/min/mg enzyme for ATPase activity1 Publication
  2. Vmax=5.8 µmol/min/mg enzyme for CTPase activity1 Publication

pH dependencei

Optimum pH is 7-8 for ATPase activity. Is more active at pH 8 to 10 than at pH 5.5.1 Publication

Temperature dependencei

Optimum temperature is 80 degrees Celsius for 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 sitei353ATP1

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 bindingi214 – 219ATP6

<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 functionChaperone
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MJAN243232:G1GKE-1275-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q58576

<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:
Proteasome-activating nucleotidaseUniRule annotation
Short name:
PANUniRule annotation
Alternative name(s):
Proteasomal ATPaseUniRule annotation
Proteasome regulatory ATPaseUniRule annotation
Proteasome regulatory particleUniRule annotation
<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:panUniRule annotation
Ordered Locus Names:MJ1176
<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>OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
<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 identifieri243232 [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 lineageiArchaeaEuryarchaeotaMethanomada groupMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
<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
  • UP000000805 <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, Proteasome

<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>Mutagenesisi113G → W: 7% of wild-type unfolding activity. 1 Publication1
Mutagenesisi153D → A: 2% of wild-type unfolding activity. 1 Publication1
Mutagenesisi156A → D: 1.5% of wild-type unfolding activity. 1 Publication1
Mutagenesisi157K → G: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi244F → A: 1% of wild-type unfolding activity. 1 Publication1
Mutagenesisi245I → A or W: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi246G → A: 5% of wild-type unfolding activity. 1 Publication1
Mutagenesisi250 – 251SL → AA: 4% of wild-type unfolding activity. 1 Publication2
Mutagenesisi271E → K: 9% of wild-type unfolding activity. 1 Publication1
Mutagenesisi285G → W: 1.6% of wild-type unfolding activity. 1 Publication1
Mutagenesisi286G → A: No effect on unfolding activity. 1 Publication1
Mutagenesisi286G → L or W: 4% of wild-type unfolding activity. 1 Publication1
Mutagenesisi428L → A, V or F: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi428L → I, Y or W: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi428L → R, D, C or P: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1
Mutagenesisi429Y → A, V, I, L, F, W, R or D: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1
Mutagenesisi430R → A or W: No effect on PAN's ability to stimulate gate opening. Still associates with the proteasome. 1 Publication1
Mutagenesisi430R → D: Loss of PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → G: Slightly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → L: Markedly decreased PAN's ability to stimulate gate opening. 1 Publication1
Mutagenesisi430R → RA: Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 1 Publication1
Mutagenesisi430Missing : Loss of PAN's ability to stimulate gate opening. Fails to associate with the proteasome. 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_00000847431 – 430Proteasome-activating nucleotidaseAdd BLAST430

<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

Homohexamer. The hexameric complex has a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Alone, can form a complex composed of two stacked hexameric rings in vitro. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets.

4 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243232.MJ_1176

<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

1430
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

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SMRi
Q58576

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
Q58576

<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>Regioni428 – 430Docks into pockets in the proteasome alpha-ring to cause gate opening3

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 coili9 – 89UniRule annotationAdd BLAST81

<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

Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.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 AAA ATPase family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG01306, Archaea

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000688_2_1_2

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q58576

KEGG Orthology (KO)

More...
KOi
K03420

Identification of Orthologs from Complete Genome Data

More...
OMAi
ARCKLRY

Database of Orthologous Groups

More...
OrthoDBi
30571at2157

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q58576

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00553, PAN, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005937, 26S_Psome_P45-like
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR023501, Nucleotidase_PAN
IPR027417, P-loop_NTPase
IPR032501, Prot_ATP_ID_OB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit
PF16450, Prot_ATP_ID_OB, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01242, 26Sp45, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00674, AAA, 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.

Q58576-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVFEEFISTE LKKEKKAFTE EFKEEKEIND NSNLKNDLLK EELQEKARIA
60 70 80 90 100
ELESRILKLE LEKKELEREN LQLMKENEIL RRELDRMRVP PLIVGTVVDK
110 120 130 140 150
VGERKVVVKS STGPSFLVNV SHFVNPDDLA PGKRVCLNQQ TLTVVDVLPE
160 170 180 190 200
NKDYRAKAME VDERPNVRYE DIGGLEKQMQ EIREVVELPL KHPELFEKVG
210 220 230 240 250
IEPPKGILLY GPPGTGKTLL AKAVATETNA TFIRVVGSEL VKKFIGEGAS
260 270 280 290 300
LVKDIFKLAK EKAPSIIFID EIDAIAAKRT DALTGGDREV QRTLMQLLAE
310 320 330 340 350
MDGFDARGDV KIIGATNRPD ILDPAILRPG RFDRIIEVPA PDEKGRLEIL
360 370 380 390 400
KIHTRKMNLA EDVNLEEIAK MTEGCVGAEL KAICTEAGMN AIRELRDYVT
410 420 430
MDDFRKAVEK IMEKKKVKVK EPAHLDVLYR
Length:430
Mass (Da):48,690
Last modified:November 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:i3FD2E94A68D483DD
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
L77117 Genomic DNA Translation: AAB99179.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G64446

NCBI Reference Sequences

More...
RefSeqi
WP_010870689.1, NC_000909.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAB99179; AAB99179; MJ_1176

Database of genes from NCBI RefSeq genomes

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GeneIDi
1452074

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mja:MJ_1176

<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
L77117 Genomic DNA Translation: AAB99179.1
PIRiG64446
RefSeqiWP_010870689.1, NC_000909.1

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
3H43X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L74-150[»]
3H4MX-ray3.11A/B/C155-430[»]
3IPMX-ray4.00O/P/Q/R/S/T/U424-430[»]
SMRiQ58576
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1176

Genome annotation databases

EnsemblBacteriaiAAB99179; AAB99179; MJ_1176
GeneIDi1452074
KEGGimja:MJ_1176

Phylogenomic databases

eggNOGiarCOG01306, Archaea
HOGENOMiCLU_000688_2_1_2
InParanoidiQ58576
KOiK03420
OMAiARCKLRY
OrthoDBi30571at2157
PhylomeDBiQ58576

Enzyme and pathway databases

BioCyciMJAN243232:G1GKE-1275-MONOMER
SABIO-RKiQ58576

Miscellaneous databases

EvolutionaryTraceiQ58576

Family and domain databases

HAMAPiMF_00553, PAN, 1 hit
InterProiView protein in InterPro
IPR005937, 26S_Psome_P45-like
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR023501, Nucleotidase_PAN
IPR027417, P-loop_NTPase
IPR032501, Prot_ATP_ID_OB
PfamiView protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit
PF16450, Prot_ATP_ID_OB, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR01242, 26Sp45, 1 hit
PROSITEiView protein in PROSITE
PS00674, AAA, 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 nameiPAN_METJA
<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: Q58576
<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: November 1, 1996
Last modified: October 7, 2020
This is version 129 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, Direct protein sequencing, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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