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Q3K5S5 (CCA_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. 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:Pfl01_5142
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length409 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-Rule MF_01261

Catalytic activity

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

Cofactor

Magnesium for nucleotidyltransferase activity By similarity.

Nickel for phosphatase activity By similarity.

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-Rule MF_01261

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP-Rule 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 – 409409Multifunctional CCA protein HAMAP-Rule MF_01261
PRO_1000054285

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
Q3K5S5 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 3E58ADEF6984EC34

FASTA40946,100
        10         20         30         40         50         60 
MQIYKVGGAV RDRLLGKPVT DIDWVVVGAT TEEMLAKGFR PVGADFPVFL HPKSGEEYAL 

        70         80         90        100        110        120 
ARTERKSGRG YGGFTFHASP EVTLEEDLIR RDLTINAMAE DDQQNLTDPY HGQRDLEERI 

       130        140        150        160        170        180 
LRHVSPAFAE DPLRVLRVAR FAARYAELGF KVAPETLELM RQLSESGELE ALTAERSWKE 

       190        200        210        220        230        240 
ISRALMEDQP QVFIQVLRDC GALKVLMPEV DALFGVPQPE AHHPEIDSGL HTLSVLEQSA 

       250        260        270        280        290        300 
LHKQPLTVRW ACLLHDLGKG LTPEEEWPRH IAHEHKGLKL IKAVNERFKA PKDCQELALL 

       310        320        330        340        350        360 
VGQYHTHGHR ALELKASTLL ELLQSFDVYR RPQRFEEFIV ACEMDARGRK GLEQRSYPQA 

       370        380        390        400 
DYLRGAANVA RGVAVQPLLE KGFKGPELGE ALKRERLKAL KVYKESAAS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000094 Genomic DNA. Translation: ABA76879.1.
RefSeqYP_350870.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3K5S5.
ModBaseSearch...

Protein-protein interaction databases

STRING205922.Pfl01_5142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA76879; ABA76879; Pfl01_5142.
GeneID3717273.
KEGGpfo:Pfl01_5142.
PATRIC19892506. VBIPseFlu44242_5159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0617.
HOGENOMHOG000007368.
KOK00974.
OMAPVREVNQ.
ProtClustDBPRK10885.

Enzyme and pathway databases

BioCycPFLU205922:GJBD-5230-MONOMER.

Family and domain databases

HAMAPMF_01261. CCA_bact_type1.
InterProIPR012006. CCA_bact.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002646. PolA_pol_head_dom.
[Graphical view]
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_PSEPF
AccessionPrimary (citable) accession number: Q3K5S5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 61 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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