Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0ACP8 (CCA_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Mlg_0030
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

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_1000054247

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
Q0ACP8 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: BA6A71BF80052450

FASTA41346,943
        10         20         30         40         50         60 
MKVYLVGGAV RDQLLGREVR ERDWVVVGAR PEDLKQRGYR PVGQDFPVFL HPETHEEYAL 

        70         80         90        100        110        120 
ARTERKTGRG YHGFAFHASP EVTLEQDLAR RDLTINAMAR ADDGTLIDPY DGRRDLEQRL 

       130        140        150        160        170        180 
LRHVSPAFAE DPVRILRLAR FAARFQPLGF RVAPETLALC RKMVADGEVD ALVPERVWQE 

       190        200        210        220        230        240 
LSRALLEDTP VPFFRVLREC GALARVLPEL DRLFGIPEPE AYHPEGDTGE HTLLALAQSA 

       250        260        270        280        290        300 
RLGGDLPVRW AVLLHDLGKA TTPSQVWPRH PAHEHRGVPL VEALCERLRA PRECRDLARL 

       310        320        330        340        350        360 
VCRYHLQAHR AFELRASTLL KLLEGLDLFR RQARLEPFLL ACEADARGRL GLEDQPYPQA 

       370        380        390        400        410 
RFLREAYRVA AAVTARPFVQ AGFKGRQIAE AVTRERIRAL AALQRDYPRP EAH

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000453 Genomic DNA. Translation: ABI55389.1.
RefSeqYP_740879.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0ACP8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0ACP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4268887.
GenomeReviewsGene locus Mlg_0030 in contig CP000453_GR.
KEGGaeh:Mlg_0030.
NMPDRfig|187272.6.peg.29.
PATRIC20859230. VBIAlkEhr114327_0030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0617.
HOGENOMHBG635063.
OMAGHGQKGL.
PhylomeDBQ0ACP8.

Enzyme and pathway databases

BioCycAEHR187272:MLG_0030-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_ALHEH
AccessionPrimary (citable) accession number: Q0ACP8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 40 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents