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Protein

CCA-adding enzyme

Gene

cca

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471ATP or CTP
Binding sitei50 – 501ATP or CTP
Metal bindingi59 – 591Magnesium
Metal bindingi61 – 611Magnesium
Metal bindingi110 – 1101Magnesium
Binding sitei133 – 1331ATP or CTP
Binding sitei152 – 1521ATP or CTP
Binding sitei161 – 1611ATP or CTP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

RNA repair, tRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-2200-MONOMER.
BRENDAi2.7.7.72. 414.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:cca
Ordered Locus Names:AF_2156
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501R → A: High decrease in both AMP and CMP incorporation. 1 Publication
Mutagenesisi110 – 1101D → A: High decrease in both AMP and CMP incorporation. 1 Publication
Mutagenesisi133 – 1331H → A: No decrease in both AMP and CMP incorporation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437CCA-adding enzymePRO_0000139065Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi224325.AF2156.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Helixi18 – 3821Combined sources
Beta strandi42 – 454Combined sources
Helixi46 – 494Combined sources
Beta strandi59 – 668Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 8615Combined sources
Beta strandi87 – 10418Combined sources
Beta strandi107 – 1159Combined sources
Beta strandi118 – 1214Combined sources
Helixi126 – 13712Combined sources
Turni138 – 1403Combined sources
Turni142 – 1443Combined sources
Helixi145 – 15713Combined sources
Turni165 – 1673Combined sources
Helixi172 – 18211Combined sources
Helixi185 – 1928Combined sources
Beta strandi199 – 2024Combined sources
Helixi203 – 2053Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi221 – 2255Combined sources
Turni226 – 2294Combined sources
Helixi232 – 24716Combined sources
Helixi251 – 2544Combined sources
Helixi264 – 27411Combined sources
Beta strandi277 – 2848Combined sources
Helixi290 – 31021Combined sources
Beta strandi315 – 3228Combined sources
Beta strandi324 – 33411Combined sources
Beta strandi340 – 3489Combined sources
Helixi352 – 3609Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi373 – 3797Combined sources
Helixi385 – 39511Combined sources
Helixi397 – 3993Combined sources
Helixi402 – 4109Combined sources
Beta strandi413 – 4164Combined sources
Helixi418 – 4225Combined sources
Helixi426 – 4338Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4X4NX-ray2.95A/C/E/F1-437[»]
4X4OX-ray3.20A/C1-437[»]
4X4PX-ray3.00A/C/E/G1-437[»]
4X4QX-ray3.15A/C1-437[»]
4X4RX-ray3.20A/C1-437[»]
4X4SX-ray3.25A/C1-437[»]
4X4TX-ray2.50A/C/E/F1-437[»]
4X4UX-ray2.70A/C/E/F1-437[»]
4X4VX-ray2.60A/C1-437[»]
ProteinModelPortaliO28126.
SMRiO28126. Positions 1-437.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28126.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG04249. Archaea.
COG1746. LUCA.
KOiK07558.
OMAiFMAFPLD.

Family and domain databases

HAMAPiMF_01264. CCA_arch. 1 hit.
InterProiIPR008229. CCA-adding_arc.
IPR011068. NuclTrfase_I_C.
IPR002934. Polymerase_NTP_transf_dom.
IPR015329. tRNA_NucTransf2.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF09249. tRNA_NucTransf2. 1 hit.
[Graphical view]
PIRSFiPIRSF005335. CCA_arch. 1 hit.
SUPFAMiSSF55003. SSF55003. 1 hit.
TIGRFAMsiTIGR03671. cca_archaeal. 1 hit.

Sequencei

Sequence statusi: Complete.

O28126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVEEILEKA LELVIPDEEE VRKGREAEEE LRRRLDELGV EYVFVGSYAR
60 70 80 90 100
NTWLKGSLEI DVFLLFPEEF SKEELRERGL EIGKAVLDSY EIRYAEHPYV
110 120 130 140 150
HGVVKGVEVD VVPCYKLKEP KNIKSAVDRT PFHHKWLEGR IKGKENEVRL
160 170 180 190 200
LKGFLKANGI YGAEYKVRGF SGYLCELLIV FYGSFLETVK NARRWTRRTV
210 220 230 240 250
IDVAKGEVRK GEEFFVVDPV DEKRNVAANL SLDNLARFVH LCREFMEAPS
260 270 280 290 300
LGFFKPKHPL EIEPERLRKI VEERGTAVFA VKFRKPDIVD DNLYPQLERA
310 320 330 340 350
SRKIFEFLER ENFMPLRSAF KASEEFCYLL FECQIKEISR VFRRMGPQFE
360 370 380 390 400
DERNVKKFLS RNRAFRPFIE NGRWWAFEMR KFTTPEEGVR SYASTHWHTL
410 420 430
GKNVGESIRE YFEIISGEKL FKEPVTAELC EMMGVKD
Length:437
Mass (Da):51,385
Last modified:January 1, 1998 - v1
Checksum:iC5D57122F63CAC97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89084.1.
PIRiD69519.
RefSeqiWP_010879645.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89084; AAB89084; AF_2156.
GeneIDi24795903.
KEGGiafu:AF_2156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89084.1.
PIRiD69519.
RefSeqiWP_010879645.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4X4NX-ray2.95A/C/E/F1-437[»]
4X4OX-ray3.20A/C1-437[»]
4X4PX-ray3.00A/C/E/G1-437[»]
4X4QX-ray3.15A/C1-437[»]
4X4RX-ray3.20A/C1-437[»]
4X4SX-ray3.25A/C1-437[»]
4X4TX-ray2.50A/C/E/F1-437[»]
4X4UX-ray2.70A/C/E/F1-437[»]
4X4VX-ray2.60A/C1-437[»]
ProteinModelPortaliO28126.
SMRiO28126. Positions 1-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89084; AAB89084; AF_2156.
GeneIDi24795903.
KEGGiafu:AF_2156.

Phylogenomic databases

eggNOGiarCOG04249. Archaea.
COG1746. LUCA.
KOiK07558.
OMAiFMAFPLD.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-2200-MONOMER.
BRENDAi2.7.7.72. 414.

Miscellaneous databases

EvolutionaryTraceiO28126.

Family and domain databases

HAMAPiMF_01264. CCA_arch. 1 hit.
InterProiIPR008229. CCA-adding_arc.
IPR011068. NuclTrfase_I_C.
IPR002934. Polymerase_NTP_transf_dom.
IPR015329. tRNA_NucTransf2.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF09249. tRNA_NucTransf2. 1 hit.
[Graphical view]
PIRSFiPIRSF005335. CCA_arch. 1 hit.
SUPFAMiSSF55003. SSF55003. 1 hit.
TIGRFAMsiTIGR03671. cca_archaeal. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCCA_ARCFU
AccessioniPrimary (citable) accession number: O28126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: December 9, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.