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O28126 (CCA_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
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
Gene names
Name:cca
Ordered Locus Names:AF_2156
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP MF_01264

Cofactor

Magnesium Probable.

Subunit structure

Homodimer. Ref.2 Ref.3

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition. In contrast to the eubacterial homologs, the specificity of the nucleotide-binding pocket is determined by both the enzyme and the tRNA. HAMAP MF_01264

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437CCA-adding enzyme HAMAP MF_01264
PRO_0000139065

Sites

Metal binding591Magnesium
Metal binding611Magnesium
Metal binding1101Magnesium
Binding site471ATP or CTP
Binding site501ATP or CTP
Binding site1331ATP or CTP
Binding site1521ATP or CTP
Binding site1611ATP or CTP

Experimental info

Mutagenesis501R → A: High decrease in both AMP and CMP incorporation. Ref.2
Mutagenesis1101D → A: High decrease in both AMP and CMP incorporation. Ref.2
Mutagenesis1331H → A: No decrease in both AMP and CMP incorporation. Ref.2

Secondary structure

1 ........................................................................ 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O28126 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C5D57122F63CAC97

FASTA43751,385
        10         20         30         40         50         60 
MKVEEILEKA LELVIPDEEE VRKGREAEEE LRRRLDELGV EYVFVGSYAR NTWLKGSLEI 

        70         80         90        100        110        120 
DVFLLFPEEF SKEELRERGL EIGKAVLDSY EIRYAEHPYV HGVVKGVEVD VVPCYKLKEP 

       130        140        150        160        170        180 
KNIKSAVDRT PFHHKWLEGR IKGKENEVRL LKGFLKANGI YGAEYKVRGF SGYLCELLIV 

       190        200        210        220        230        240 
FYGSFLETVK NARRWTRRTV IDVAKGEVRK GEEFFVVDPV DEKRNVAANL SLDNLARFVH 

       250        260        270        280        290        300 
LCREFMEAPS LGFFKPKHPL EIEPERLRKI VEERGTAVFA VKFRKPDIVD DNLYPQLERA 

       310        320        330        340        350        360 
SRKIFEFLER ENFMPLRSAF KASEEFCYLL FECQIKEISR VFRRMGPQFE DERNVKKFLS 

       370        380        390        400        410        420 
RNRAFRPFIE NGRWWAFEMR KFTTPEEGVR SYASTHWHTL GKNVGESIRE YFEIISGEKL 

       430 
FKEPVTAELC EMMGVKD

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed: 9389475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure."
Okabe M., Tomita K., Ishitani R., Ishii R., Takeuchi N., Arisaka F., Nureki O., Yokoyama S.
EMBO J. 22:5918-5927(2003) [PubMed: 14592988] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH ATP AND CTP, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-50; ASP-110 AND HIS-133.
[3]"Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes."
Xiong Y., Li F., Wang J., Weiner A.M., Steitz T.A.
Mol. Cell 12:1165-1172(2003) [PubMed: 14636575] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH ATP; CTP AND UTP, SUBUNIT.
[4]"Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template."
Xiong Y., Steitz T.A.
Nature 430:640-645(2004) [PubMed: 15295590] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH TRNA AND OF COMPLEXES WITH SYNTHETIC RNA DUPLEXES ENDING WITH THE OLIGONUCLEOTIDES C74 AND C75.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB89084.1.
PIRD69519.
RefSeqNP_070981.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R89X-ray1.80A1-437[»]
1R8AX-ray2.10A1-437[»]
1R8BX-ray2.00A1-437[»]
1R8CX-ray1.90A1-437[»]
1SZ1X-ray6.21A/B1-437[»]
1TFWX-ray2.20A/B/C/D1-437[»]
1TFYX-ray3.20A/B/C/D1-437[»]
1UETX-ray2.00A1-437[»]
1UEUX-ray2.00A1-437[»]
1UEVX-ray2.70A1-437[»]
2DR5X-ray2.80A1-437[»]
2DR7X-ray2.80A1-437[»]
2DR8X-ray2.50A1-437[»]
2DR9X-ray2.80A1-437[»]
2DRAX-ray2.50A1-437[»]
2DRBX-ray2.80A1-437[»]
2DVIX-ray2.61A1-437[»]
2ZH1X-ray2.80A1-437[»]
2ZH2X-ray2.66A1-437[»]
2ZH3X-ray2.50A1-437[»]
2ZH4X-ray2.65A1-437[»]
2ZH5X-ray2.60A1-437[»]
2ZH6X-ray2.50A1-437[»]
2ZH7X-ray3.00A2-437[»]
2ZH8X-ray2.65A1-437[»]
2ZH9X-ray2.90A1-437[»]
2ZHAX-ray2.95A1-437[»]
2ZHBX-ray3.05A2-437[»]
3OUYX-ray2.69A/B1-437[»]
3OV7X-ray3.00A/B1-437[»]
3OVAX-ray1.98A3-437[»]
3OVBX-ray1.95A/B1-437[»]
3OVSX-ray2.80A/B1-437[»]
ProteinModelPortalO28126.
SMRO28126. Positions 1-437.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1485385.
GenomeReviewsGene locus AF_2156 in contig AE000782_GR.
KEGGafu:AF2156.
NMPDRfig|224325.1.peg.2142.
TIGRAF_2156.

Phylogenomic databases

HOGENOMHBG645243.
OMADRTPFHN.
ProtClustDBPRK13300.

Enzyme and pathway databases

BioCycAFUL224325:AF_2156-MONOMER.

Family and domain databases

HAMAPMF_01264. CCA_arch.
[Tree]
InterProIPR008229. CCA-adding_arc.
IPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR015329. tRNA_NucTransf2.
[Graphical view]
KOK07558.
PfamPF01909. NTP_transf_2. 1 hit.
PF09249. tRNA_NucTransf2. 1 hit.
[Graphical view]
PIRSFPIRSF005335. CCA_arch. 1 hit.
SUPFAMSSF55003. PAP_C. 1 hit.
TIGRFAMsTIGR03671. Cca_archaeal. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCCA_ARCFU
AccessionPrimary (citable) accession number: O28126
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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