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Q1R6S5 (CCA_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Multifunctional CCA protein

Including the following 4 domains:

  1. 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. 2'-nucleotidase
    EC=3.1.3.-
  3. 2',3'-cyclic phosphodiesterase
    EC=3.1.4.-
  4. Phosphatase
    EC=3.1.3.-
Gene names
Name:cca
Ordered Locus Names:UTI89_C3492
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases By similarity. HAMAP MF_01261

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP MF_01261

Cofactor

Magnesium for nucleotidyltransferase activity By similarity.

Nickel for phosphatase activity By similarity. HAMAP MF_01261

Subunit structure

Monomer. Can also form homodimers and oligomers By similarity.

Domain

Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities By similarity. HAMAP MF_01261

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP MF_01261

Sequence similarities

Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Multifunctional CCA protein HAMAP MF_01261
PRO_1000054264

Sites

Metal binding211Magnesium By similarity
Metal binding231Magnesium By similarity
Binding site81ATP or CTP; via amide nitrogen By similarity
Binding site111ATP or CTP By similarity
Binding site911ATP or CTP By similarity
Binding site1371ATP or CTP By similarity
Binding site1401ATP or CTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1R6S5 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 6AFE8DA5A89A6BB2

FASTA41246,538
        10         20         30         40         50         60 
MKIYLVGGAV RDALLGLPVK DRDWVVVGST PQEMLDAGYQ QVGRDFPVFL HPQTHEEYAL 

        70         80         90        100        110        120 
ARTERKSGSG YTGFTCYAAP DVTLEDDLKR RDLTINALAQ DDNGEIIDPY NGLGDLQNRL 

       130        140        150        160        170        180 
LRHVSPAFGE DPLRVLRVAR FAARYAHLCF RIADETLALM REMTHAGELE HLTPERVWKE 

       190        200        210        220        230        240 
TENALTTRNP QVFFQVLRDC GALRVLFPEI DALFGVPAPA RWHPEIDTGI HTLMTLSMAA 

       250        260        270        280        290        300 
MLSPQVDVRF ATLCHDLGKG LTPPELWPRH HGHGPAGVKL VEQLCQRLRV PNEIRDLARL 

       310        320        330        340        350        360 
VAEFHDLIHT FPMLNPKTIV KLFDSIDAWR KPQRVEQLAL TSEADVRGRT GFESADYPQG 

       370        380        390        400        410 
RWLREAWEVA QSVPTKAVVE AGFKGVEIRE ELTRRRIAAV AGWKEQRCPK PE

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000243 Genomic DNA. Translation: ABE08939.1.
RefSeqYP_542470.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R6S5.
SMRQ1R6S5. Positions 1-403.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R6S5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000065866; EBESCP00000063344; EBESCG00000064913.
GeneID3993898.
GenomeReviewsGene locus UTI89_C3492 in contig CP000243_GR.
KEGGeci:UTI89_C3492.
PATRIC18456484. VBIEscCol42261_3459.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0617.
GeneTreeEBGT00050000009869.
HOGENOMHBG635063.
OMAGHGQKGL.
ProtClustDBPRK10885.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C3492-MONOMER.

Family and domain databases

HAMAPMF_01261. CCA_bact_type1.
[Tree]
InterProIPR012006. CCA_bact.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR006674. Metal-dep_PHydrolase_HD_sub.
IPR002646. PolA_pol_head_dom.
[Graphical view]
KOK00974.
PfamPF01966. HD. 1 hit.
PF01743. PolyA_pol. 1 hit.
[Graphical view]
PIRSFPIRSF000813. CCA_bact. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCCA_ECOUT
AccessionPrimary (citable) accession number: Q1R6S5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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