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Entry version 168 (13 Nov 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Multifunctional CCA protein

Gene

cca

Organism
Escherichia coli (strain K12)
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 addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni2+ and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP. Without metal or in the presence of Mg2+, this protein hydrolyzes 2',3'-cyclic substrates with the formation of 2'-nucleotides, whereas in the presence of Ni2+, it also produces some 3'-nucleotides. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.1 Publication

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Both phosphatase and phosphodiesterase activities are competitively inhibited by low concentrations of the E.coli tRNA (10 nM). Cu2+ stimulates the hydrolysis of pyrophosphate and ATP and completely inhibits the hydrolysis of 2'-AMP. The phosphodiesterase activity is inhibited by Zn2+, Cu2+ and Co2+.

<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=0.33 mM for ATP (in the tRNA-NT activity assay)2 Publications
  2. KM=0.03 mM for CTP (in the tRNA-NT activity assay)2 Publications
  3. KM=0.015 mM for tRNA-CC2 Publications
  4. KM=0.02 mM for tRNA-C2 Publications
  5. KM=6.2 mM for pNPP2 Publications
  6. KM=0.10 mM for PPi2 Publications
  7. KM=0.15 mM for NADP2 Publications
  8. KM=0.19 mM for ADP2 Publications
  9. KM=0.18 mM for ATP (in the phosphatase activity assay)2 Publications
  10. KM=0.53 mM for CDP2 Publications
  11. KM=0.13 mM for CTP (in the phosphatase activity assay)2 Publications
  12. KM=0.76 mM for 2'-AMP2 Publications
  13. KM=0.49 mM for 2',3'-cAMP2 Publications
  14. KM=1.60 mM for 2',3'-cGMP2 Publications
  1. Vmax=12.4 µmol/min/mg enzyme with pNPP as substrate2 Publications
  2. Vmax=3.01 µmol/min/mg enzyme with PPi as substrate2 Publications
  3. Vmax=17.9 µmol/min/mg enzyme with NADP as substrate2 Publications
  4. Vmax=1.49 µmol/min/mg enzyme with ADP as substrate2 Publications
  5. Vmax=4.53 µmol/min/mg enzyme with ATP as substrate (in the phosphatase activity assay)2 Publications
  6. Vmax=5.80 µmol/min/mg enzyme with CDP as substrate2 Publications
  7. Vmax=4.03 µmol/min/mg enzyme with CTP as substrate (in the phosphatase activity assay)2 Publications
  8. Vmax=3.71 µmol/min/mg enzyme with 2'-AMP as substrate2 Publications
  9. Vmax=3.21 µmol/min/mg enzyme with 2',3'-cAMP as substrate2 Publications
  10. Vmax=2.36 µmol/min/mg enzyme with 2',3'-cGMP as substrate2 Publications

pH dependencei

Optimum pH is 9.4 for AMP incorporation, 10.0 for CMP incorporation, and 7.0 for the phosphatase and phosphodiesterase activities.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei8ATP or CTP; via amide nitrogenBy similarity1
Binding sitei11ATP or CTPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi21MagnesiumBy similarity1
Metal bindingi23MagnesiumBy similarity1
Binding sitei91ATP or CTPBy similarity1
Binding sitei137ATP or CTPBy similarity1
Binding sitei140ATP or CTPBy similarity1

<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

  • RNA repair Source: EcoCyc
  • tRNA 3'-terminal CCA addition Source: EcoCyc

<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, Multifunctional enzyme, Nucleotidyltransferase, RNA-binding, Transferase
Biological processRNA repair, tRNA processing
LigandATP-binding, Magnesium, Metal-binding, Nickel, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10136-MONOMER
ECOL316407:JW3028-MONOMER
MetaCyc:EG10136-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.72 2026
3.1.4.16 2026
3.1.4.37 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P06961

<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_and_taxonomy_section">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:
Multifunctional CCA protein
Including the following 4 domains:
CCA-adding enzyme (EC:2.7.7.72)
Alternative name(s):
CCA tRNA nucleotidyltransferase
tRNA CCA-pyrophosphorylase
tRNA adenylyl-/cytidylyl-transferase
tRNA nucleotidyltransferase
tRNA-NT
2'-nucleotidase (EC:3.1.3.-)
2',3'-cyclic phosphodiesterase (EC:3.1.4.-)
Phosphatase (EC:3.1.3.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:cca
Ordered Locus Names:b3056, JW3028
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000000625 Componenti: Chromosome

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi21D → A: No effect on phosphodiesterase and phosphatase activities. 1 Publication1
Mutagenesisi23D → A: No effect on phosphodiesterase and phosphatase activities. 1 Publication1
Mutagenesisi70G → D: Lowered AMP incorporation. 1 Publication1
Mutagenesisi255H → A: Loss of phosphodiesterase and phosphatase activities. 1 Publication1
Mutagenesisi256D → A: Loss of phosphodiesterase and phosphatase activities. 1 Publication1
Mutagenesisi305H → A: Loss of phosphodiesterase and phosphatase activities. 1 Publication1
Mutagenesisi306D → A: Still possesses phosphodiesterase and phosphatase activities. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3309020

<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_00001389751 – 412Multifunctional CCA proteinAdd BLAST412

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P06961

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

More...
PaxDbi
P06961

PRoteomics IDEntifications database

More...
PRIDEi
P06961

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Can also form homodimers and oligomers, but with low levels.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P0A6M42EBI-545256,EBI-562575

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259255, 71 interactors

Database of interacting proteins

More...
DIPi
DIP-9250N

Protein interaction database and analysis system

More...
IntActi
P06961, 25 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3056

<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
P06961

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_and_domains_section">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>Domaini228 – 329HDPROSITE-ProRule annotationAdd BLAST102

<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

Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D4J Bacteria
COG0617 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007368

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06961

KEGG Orthology (KO)

More...
KOi
K00974

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P06961

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00077 HDc, 1 hit
cd05398 NT_ClassII-CCAase, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01261 CCA_bact_type1, 1 hit
MF_01262 CCA_bact_type2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012006 CCA_bact
IPR003607 HD/PDEase_dom
IPR006674 HD_domain
IPR002646 PolA_pol_head_dom
IPR032828 PolyA_RNA-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01966 HD, 1 hit
PF01743 PolyA_pol, 1 hit
PF12627 PolyA_pol_RNAbd, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000813 CCA_bact, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51831 HD, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P06961-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIYLVGGAV RDALLGLPVK DRDWVVVGST PQEMLDAGYQ QVGRDFPVFL
60 70 80 90 100
HPQTHEEYAL ARTERKSGSG YTGFTCYAAP DVTLEDDLKR RDLTINALAQ
110 120 130 140 150
DDNGEIIDPY NGLGDLQNRL LRHVSPAFGE DPLRVLRVAR FAARYAHLGF
160 170 180 190 200
RIADETLALM REMTHAGELE HLTPERVWKE TESALTTRNP QVFFQVLRDC
210 220 230 240 250
GALRVLFPEI DALFGVPAPA KWHPEIDTGI HTLMTLSMAA MLSPQVDVRF
260 270 280 290 300
ATLCHDLGKG LTPPELWPRH HGHGPAGVKL VEQLCQRLRV PNEIRDLARL
310 320 330 340 350
VAEFHDLIHT FPMLNPKTIV KLFDSIDAWR KPQRVEQLAL TSEADVRGRT
360 370 380 390 400
GFESADYPQG RWLREAWEVA QSVPTKAVVE AGFKGVEIRE ELTRRRIAAV
410
ASWKEQRCPK PE
Length:412
Mass (Da):46,467
Last modified:April 1, 1988 - 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:i947182E6086220F7
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
M12788 Genomic DNA Translation: AAA23541.1
U28379 Genomic DNA Translation: AAA89136.1
U00096 Genomic DNA Translation: AAC76092.1
AP009048 Genomic DNA Translation: BAE77107.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25215 RNECTA

NCBI Reference Sequences

More...
RefSeqi
NP_417528.1, NC_000913.3
WP_000708487.1, NZ_STEB01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76092; AAC76092; b3056
BAE77107; BAE77107; BAE77107

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947553

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3028
eco:b3056

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3675

<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
M12788 Genomic DNA Translation: AAA23541.1
U28379 Genomic DNA Translation: AAA89136.1
U00096 Genomic DNA Translation: AAC76092.1
AP009048 Genomic DNA Translation: BAE77107.1
PIRiA25215 RNECTA
RefSeqiNP_417528.1, NC_000913.3
WP_000708487.1, NZ_STEB01000001.1

3D structure databases

SMRiP06961
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4259255, 71 interactors
DIPiDIP-9250N
IntActiP06961, 25 interactors
STRINGi511145.b3056

Chemistry databases

ChEMBLiCHEMBL3309020

Proteomic databases

jPOSTiP06961
PaxDbiP06961
PRIDEiP06961

Genome annotation databases

EnsemblBacteriaiAAC76092; AAC76092; b3056
BAE77107; BAE77107; BAE77107
GeneIDi947553
KEGGiecj:JW3028
eco:b3056
PATRICifig|1411691.4.peg.3675

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0134

Phylogenomic databases

eggNOGiENOG4105D4J Bacteria
COG0617 LUCA
HOGENOMiHOG000007368
InParanoidiP06961
KOiK00974
PhylomeDBiP06961

Enzyme and pathway databases

BioCyciEcoCyc:EG10136-MONOMER
ECOL316407:JW3028-MONOMER
MetaCyc:EG10136-MONOMER
BRENDAi2.7.7.72 2026
3.1.4.16 2026
3.1.4.37 2026
SABIO-RKiP06961

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P06961

Family and domain databases

CDDicd00077 HDc, 1 hit
cd05398 NT_ClassII-CCAase, 1 hit
HAMAPiMF_01261 CCA_bact_type1, 1 hit
MF_01262 CCA_bact_type2, 1 hit
InterProiView protein in InterPro
IPR012006 CCA_bact
IPR003607 HD/PDEase_dom
IPR006674 HD_domain
IPR002646 PolA_pol_head_dom
IPR032828 PolyA_RNA-bd
PfamiView protein in Pfam
PF01966 HD, 1 hit
PF01743 PolyA_pol, 1 hit
PF12627 PolyA_pol_RNAbd, 1 hit
PIRSFiPIRSF000813 CCA_bact, 1 hit
PROSITEiView protein in PROSITE
PS51831 HD, 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 nameiCCA_ECOLI
<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: P06961
Secondary accession number(s): Q2M9E9
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 13, 2019
This is version 168 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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