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Q0BB41 (CCA_BURCM) 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:Bamb_3076
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length413 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 – 413413Multifunctional CCA protein HAMAP MF_01261
PRO_1000054252

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 site1431ATP or CTP By similarity
Binding site1461ATP or CTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BB41 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: CE17C8357BF2506E

FASTA41345,516
        10         20         30         40         50         60 
MNIYAVGGAI RDDLLGVPVQ DRDYVVVGAT PEQMVAQGFR PVGKDFPVFL HPDTQEEYAL 

        70         80         90        100        110        120 
ARTERKTAAG YHGFQFYFAP DVTLDEDLAR RDLTINAMAR EVSPEGALVG PVIDPFDGQA 

       130        140        150        160        170        180 
DLHARVFRHV GDAFVEDPVR ILRIARFAAR FADFTVADDT LALMRRMVDA GEADALVAER 

       190        200        210        220        230        240 
VWQEIARGLM EAKPSRMFAV LRECGALARV LPEVDALWGV PQRADYHPEV DTGVHVMMVV 

       250        260        270        280        290        300 
DYAAKQGYSL PVRFAALTHD LGKATTPADV LPRHVGHEGR SVELIKPLCE RLRVPNECRD 

       310        320        330        340        350        360 
LALVVAREHG NLHRVMEMGA AALVRFFERS DALRKPARFA EMLQACESDA RGRLGLDTQP 

       370        380        390        400        410 
YPQAERLRVA LVAARSVDAG AIARGVGDDV MQIKDAVHRA RVEAVKQALA IGE

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000440 Genomic DNA. Translation: ABI88632.1.
RefSeqYP_774966.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BB41.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BB41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4310768.
GenomeReviewsGene locus Bamb_3076 in contig CP000440_GR.
KEGGbam:Bamb_3076.
NMPDRfig|339670.3.peg.88.
PATRIC19021930. VBIBurAmb61564_3226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0617.
HOGENOMHBG635063.
OMARWACLLH.
PhylomeDBQ0BB41.
ProtClustDBPRK10885.

Enzyme and pathway databases

BioCycBAMB339670:BAMB_3076-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_BURCM
AccessionPrimary (citable) accession number: Q0BB41
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 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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