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UniProtKB - Q9WZ31 (CORA_THEMA)

Entry version 133 (23 Feb 2022)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
Add a publicationFeedback
Protein

Cobalt/magnesium transport protein CorA

Gene

corA

Organism
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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 influx of magnesium ions (PubMed:18276588, PubMed:22722933, PubMed:23781956, PubMed:23112165).

Mediates Co2+ uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532).

Has high selectivity for Co2+ (PubMed:21454699, PubMed:23425532).

Alternates between open and closed states. Activated by low cytoplasmic Mg2+ levels. Inactive when cytoplasmic Mg2+ levels are high (PubMed:23112165, PubMed:23425532, PubMed:26871634).

1 Publication7 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

Inhibited by cobalt hexaammine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei288Essential for ion permeation1 Publication1
Sitei294Important for closing the ion permeation pathway in the closed state4 Publications1
Sitei295Threonine that confers selectivity for Co(2+) transport1 Publication1

<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

Biological processIon transport, Transport
LigandCobalt, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		7.2.2.14, 6331

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.35.3.2, the cora metal ion transporter (mit) family

<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:
Cobalt/magnesium transport protein CorACurated
<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:corA
Ordered Locus Names:TM_0561
<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>OrganismiThermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
<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 identifieri243274 [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 lineageiBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga ›
<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
  • UP000008183 <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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 292CytoplasmicCuratedAdd BLAST292
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei293 – 313Helical6 PublicationsAdd BLAST21
Topological domaini314 – 324ExtracellularCuratedAdd BLAST11
Transmembranei325 – 345Helical6 PublicationsAdd BLAST21
Topological domaini346 – 351CytoplasmicCurated6

Keywords - Cellular componenti

Cell inner membrane, 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

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>Mutagenesisi89D → F or K: Decreases ion transport. 2 Publications1
Mutagenesisi253D → K: Increases protein stability. Decreases ion transport. 2 Publications1
Mutagenesisi280L → A: Decreases ion transport. 1 Publication1
Mutagenesisi288N → L: Abolishes Co(2+) uptake. 2 Publications1
Mutagenesisi291M → A: No effect on ion transport. 1 Publication1
Mutagenesisi294L → A or V: Increases ion transport by suppression of an obstruction in the transmembrane ion permeation pathway. 1 Publication1
Mutagenesisi295T → L: Strongly reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-299. 1 Publication1
Mutagenesisi295T → M: Strongly reduces Co(2+) uptake. 1 Publication1
Mutagenesisi295T → S: No significant decrease of Co(2+) uptake, but abolishes selectivity for Co(2+). 1 Publication1
Mutagenesisi299T → L: Reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-295. 1 Publication1
Mutagenesisi299T → M: No effect on Co(2+) uptake. 1 Publication1
Mutagenesisi299T → S: Abolishes Co(2+) uptake. 1 Publication1
Mutagenesisi303P → A, G or I: Increases ion transport by suppression of a kink in the transmembrane ion permeation pathway. 1 Publication1
Mutagenesisi305T → L: Abolishes Co(2+) uptake. 1 Publication1
Mutagenesisi310I → A: Increases ion transport. 1 Publication1
Mutagenesisi311Y → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi311Y → F: No effect on pentamerization. No effect on ion transport. 1 Publication1
Mutagenesisi312G → A: No effect on pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi312G → F: No effect on pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi313M → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi313M → C, I, L or V: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → A: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → D, E or T: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → Q: No effect on pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi315F → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi315F → W: No effect on pentamerization. Increases ion transport. 1 Publication1
Mutagenesisi318M → A: Impairs pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi318M → I, L or V: No effect on pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → A: Impairs pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → I: No effect on pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → V: No effect on pentamerization. No effect on ion transport. 1 Publication1
Mutagenesisi327Y → A: Abolishes pentamerization. Strongly decreases ion transport. 2 Publications1
Mutagenesisi327Y → F: No effect on pentamerization. Increases ion transport. 1 Publication1
Mutagenesisi327Y → W: Abolishes pentamerization. Mildly decreases ion transport. 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_00002390491 – 351Cobalt/magnesium transport protein CorAAdd BLAST351

<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

Homopentamer (PubMed:22722933, PubMed:23781956, PubMed:16902408, PubMed:16598263, PubMed:16857941, PubMed:23112165, PubMed:23425532, PubMed:26871634). In the absence of Mg2+, interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (PubMed:22722933, PubMed:26871634).

8 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

Q9WZ31
With#Exp.IntAct
itself19EBI-15578365,EBI-15578365

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-59006N

STRING: functional protein association networks

More...STRINGi		243274.THEMA_01870

<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

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q9WZ31

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		Q9WZ31

<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

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 coili178 – 225Sequence analysisAdd BLAST48

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>Motifi312 – 314Probable selectivity filter4 Publications3

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

The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg2+ binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway (PubMed:23091000, PubMed:16902408, PubMed:16598263, PubMed:16857941, PubMed:23112165, PubMed:23425532, PubMed:26871634). Co2+ binding also induces a conformation change (PubMed:21454699). Low Mg2+ concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex (PubMed:23112165, PubMed:26871634).1 Publication7 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

Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family. [View classification]Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0598, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WZ31

Identification of Orthologs from Complete Genome Data

More...OMAi		QKYFRDV

Database of Orthologous Groups

More...OrthoDBi		822653at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR045861, CorA_cytoplasmic_dom
IPR045863, CorA_TM1_TM2
IPR004488, Mg/Co-transport_prot_CorA
IPR002523, MgTranspt_CorA/ZnTranspt_ZntB

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01544, CorA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF143865, SSF143865, 1 hit
SSF144083, SSF144083, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00383, corA, 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.

Q9WZ31-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEKRLSAKK GLPPGTLVYT GKYREDFEIE VMNYSIEEFR EFKTTDVESV 
        60         70         80         90        100
LPFRDSSTPT WINITGIHRT DVVQRVGEFF GIHPLVLEDI LNVHQRPKVE 
       110        120        130        140        150
FFENYVFIVL KMFTYDKNLH ELESEQVSLI LTKNCVLMFQ EKIGDVFDPV 
       160        170        180        190        200
RERIRYNRGI IRKKRADYLL YSLIDALVDD YFVLLEKIDD EIDVLEEEVL 
       210        220        230        240        250
ERPEKETVQR THQLKRNLVE LRKTIWPLRE VLSSLYRDVP PLIEKETVPY 
       260        270        280        290        300
FRDVYDHTIQ IADTVETFRD IVSGLLDVYL SSVSNKTNEV MKVLTIIATI 
       310        320        330        340        350
FMPLTFIAGI YGMNFEYMPE LRWKWGYPVV LAVMGVIAVI MVVYFKKKKW 

L
Length:351
Mass (Da):41,446
Last modified:November 1, 1999 - 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:i6A845EC612A4A0BA
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
AE000512 Genomic DNA Translation: AAD35646.1

Protein sequence database of the Protein Information Resource

More...PIRi		H72360

NCBI Reference Sequences

More...RefSeqi		NP_228371.1, NC_000853.1
WP_004081315.1, NZ_CP011107.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAD35646; AAD35646; TM_0561

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		tma:TM0561

<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
AE000512 Genomic DNA Translation: AAD35646.1
PIRiH72360
RefSeqiNP_228371.1, NC_000853.1
WP_004081315.1, NZ_CP011107.1

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
2BBHX-ray1.85A1-266[»]
2BBJX-ray3.90A/B/D/E/F1-351[»]
2HN2X-ray3.70A/B/C/D/E1-351[»]
2IUBX-ray2.90A/B/C/D/E/F/G/H/I/J1-351[»]
3JCFX-ray3.80A/B/C/D/E1-351[»]
3JCGX-ray7.06A/B/C/D/E1-351[»]
3JCHX-ray7.06A/B/C/D/E1-351[»]
4EEBX-ray3.80A/B/C/D/E26-351[»]
4EEDX-ray3.92A/B/C/D/E26-351[»]
4I0UX-ray2.70A/B/C/D/E/F/G/H/I/J1-351[»]
5JRWX-ray3.30A/B/C/D/E2-351[»]
5JTGX-ray3.05A/B/C/D/E2-351[»]
SMRiQ9WZ31
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59006N
STRINGi243274.THEMA_01870

Protein family/group databases

TCDBi1.A.35.3.2, the cora metal ion transporter (mit) family

Genome annotation databases

EnsemblBacteriaiAAD35646; AAD35646; TM_0561
KEGGitma:TM0561

Phylogenomic databases

eggNOGiCOG0598, Bacteria
InParanoidiQ9WZ31
OMAiQKYFRDV
OrthoDBi822653at2

Enzyme and pathway databases

BRENDAi7.2.2.14, 6331

Miscellaneous databases

EvolutionaryTraceiQ9WZ31

Family and domain databases

InterProiView protein in InterPro
IPR045861, CorA_cytoplasmic_dom
IPR045863, CorA_TM1_TM2
IPR004488, Mg/Co-transport_prot_CorA
IPR002523, MgTranspt_CorA/ZnTranspt_ZntB
PfamiView protein in Pfam
PF01544, CorA, 1 hit
SUPFAMiSSF143865, SSF143865, 1 hit
SSF144083, SSF144083, 1 hit
TIGRFAMsiTIGR00383, corA, 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 nameiCORA_THEMA
<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: Q9WZ31
<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: May 30, 2006
Last sequence update: November 1, 1999
Last modified: February 23, 2022
This is version 133 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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