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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)DescriptionActionsGraphical viewLength
Binding sitei47ATP or CTP1
Binding sitei50ATP or CTP1
Metal bindingi59Magnesium1
Metal bindingi61Magnesium1
Metal bindingi110Magnesium1
Binding sitei133ATP or CTP1
Binding sitei152ATP or CTP1
Binding sitei161ATP or CTP1

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi50R → A: High decrease in both AMP and CMP incorporation. 1 Publication1
Mutagenesisi110D → A: High decrease in both AMP and CMP incorporation. 1 Publication1
Mutagenesisi133H → A: No decrease in both AMP and CMP incorporation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001390651 – 437CCA-adding enzymeAdd BLAST437

Proteomic databases

PRIDEiO28126.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi224325.AF2156.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Helixi18 – 38Combined sources21
Beta strandi42 – 45Combined sources4
Helixi46 – 49Combined sources4
Beta strandi59 – 66Combined sources8
Beta strandi68 – 70Combined sources3
Helixi72 – 86Combined sources15
Beta strandi87 – 104Combined sources18
Beta strandi107 – 115Combined sources9
Beta strandi118 – 121Combined sources4
Helixi126 – 137Combined sources12
Turni138 – 140Combined sources3
Turni142 – 144Combined sources3
Helixi145 – 157Combined sources13
Turni165 – 167Combined sources3
Helixi172 – 182Combined sources11
Helixi185 – 192Combined sources8
Beta strandi199 – 202Combined sources4
Helixi203 – 205Combined sources3
Beta strandi207 – 210Combined sources4
Beta strandi215 – 218Combined sources4
Beta strandi221 – 225Combined sources5
Turni226 – 229Combined sources4
Helixi232 – 247Combined sources16
Helixi251 – 254Combined sources4
Helixi264 – 274Combined sources11
Beta strandi277 – 284Combined sources8
Helixi290 – 310Combined sources21
Beta strandi315 – 322Combined sources8
Beta strandi324 – 334Combined sources11
Beta strandi340 – 348Combined sources9
Helixi352 – 360Combined sources9
Beta strandi368 – 370Combined sources3
Beta strandi373 – 379Combined sources7
Helixi385 – 395Combined sources11
Helixi397 – 399Combined sources3
Helixi402 – 410Combined sources9
Beta strandi413 – 416Combined sources4
Helixi418 – 422Combined sources5
Helixi426 – 433Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2156.

Proteomic databases

PRIDEiO28126.

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

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: November 2, 2016
This is version 113 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.