CCA_ARCFU
ID CCA_ARCFU Reviewed; 437 AA.
AC O28126;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=CCA-adding enzyme {ECO:0000303|PubMed:14592988};
DE EC=2.7.7.72 {ECO:0000269|PubMed:14592988};
DE AltName: Full=CCA tRNA nucleotidyltransferase;
DE AltName: Full=tRNA CCA-pyrophosphorylase;
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase;
DE AltName: Full=tRNA nucleotidyltransferase;
DE AltName: Full=tRNA-NT;
GN Name=cca; OrderedLocusNames=AF_2156;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2] {ECO:0007744|PDB:1UET, ECO:0007744|PDB:1UEU, ECO:0007744|PDB:1UEV}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP ATP; CTP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF ARG-50; ASP-110 AND HIS-133.
RX PubMed=14592988; DOI=10.1093/emboj/cdg563;
RA Okabe M., Tomita K., Ishitani R., Ishii R., Takeuchi N., Arisaka F.,
RA Nureki O., Yokoyama S.;
RT "Divergent evolutions of trinucleotide polymerization revealed by an
RT archaeal CCA-adding enzyme structure.";
RL EMBO J. 22:5918-5927(2003).
RN [3] {ECO:0007744|PDB:1R89, ECO:0007744|PDB:1R8A, ECO:0007744|PDB:1R8B, ECO:0007744|PDB:1R8C}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP ATP; CTP; UTP AND MAGNESIUM, AND SUBUNIT.
RX PubMed=14636575; DOI=10.1016/s1097-2765(03)00440-4;
RA Xiong Y., Li F., Wang J., Weiner A.M., Steitz T.A.;
RT "Crystal structures of an archaeal class I CCA-adding enzyme and its
RT nucleotide complexes.";
RL Mol. Cell 12:1165-1172(2003).
RN [4] {ECO:0007744|PDB:1SZ1, ECO:0007744|PDB:1TFW, ECO:0007744|PDB:1TFY}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH TRNA AND OF COMPLEXES
RP WITH SYNTHETIC RNA DUPLEXES ENDING WITH THE OLIGONUCLEOTIDES C74 AND C75.
RX PubMed=15295590; DOI=10.1038/nature02711;
RA Xiong Y., Steitz T.A.;
RT "Mechanism of transfer RNA maturation by CCA-adding enzyme without using an
RT oligonucleotide template.";
RL Nature 430:640-645(2004).
CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC terminal CCA sequence in tRNAs without using a nucleic acid template.
CC Adds these three nucleotides in the order of C, C, and A to the tRNA
CC nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC pyrophosphate. {ECO:0000269|PubMed:14592988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC Evidence={ECO:0000269|PubMed:14592988};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14434;
CC Evidence={ECO:0000269|PubMed:14592988};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:14592988};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14592988,
CC ECO:0000269|PubMed:14636575}.
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition. In contrast to the
CC eubacterial homologs, the specificity of the nucleotide-binding pocket
CC is determined by both the enzyme and the tRNA.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Archaeal CCA-adding enzyme subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB89084.1; -; Genomic_DNA.
DR PIR; D69519; D69519.
DR RefSeq; WP_010879645.1; NC_000917.1.
DR PDB; 1R89; X-ray; 1.80 A; A=1-437.
DR PDB; 1R8A; X-ray; 2.10 A; A=1-437.
DR PDB; 1R8B; X-ray; 2.00 A; A=1-437.
DR PDB; 1R8C; X-ray; 1.90 A; A=1-437.
DR PDB; 1SZ1; X-ray; 6.21 A; A/B=1-437.
DR PDB; 1TFW; X-ray; 2.20 A; A/B/C/D=1-437.
DR PDB; 1TFY; X-ray; 3.20 A; A/B/C/D=1-437.
DR PDB; 1UET; X-ray; 2.00 A; A=1-437.
DR PDB; 1UEU; X-ray; 2.00 A; A=1-437.
DR PDB; 1UEV; X-ray; 2.70 A; A=1-437.
DR PDB; 2DR5; X-ray; 2.80 A; A=1-437.
DR PDB; 2DR7; X-ray; 2.80 A; A=1-437.
DR PDB; 2DR8; X-ray; 2.50 A; A=1-437.
DR PDB; 2DR9; X-ray; 2.80 A; A=1-437.
DR PDB; 2DRA; X-ray; 2.50 A; A=1-437.
DR PDB; 2DRB; X-ray; 2.80 A; A=1-437.
DR PDB; 2DVI; X-ray; 2.61 A; A=1-437.
DR PDB; 2ZH1; X-ray; 2.80 A; A=1-437.
DR PDB; 2ZH2; X-ray; 2.66 A; A=1-437.
DR PDB; 2ZH3; X-ray; 2.50 A; A=1-437.
DR PDB; 2ZH4; X-ray; 2.65 A; A=1-437.
DR PDB; 2ZH5; X-ray; 2.60 A; A=1-437.
DR PDB; 2ZH6; X-ray; 2.50 A; A=1-437.
DR PDB; 2ZH7; X-ray; 3.00 A; A=2-437.
DR PDB; 2ZH8; X-ray; 2.65 A; A=1-437.
DR PDB; 2ZH9; X-ray; 2.90 A; A=1-437.
DR PDB; 2ZHA; X-ray; 2.95 A; A=1-437.
DR PDB; 2ZHB; X-ray; 3.05 A; A=2-437.
DR PDB; 3OUY; X-ray; 2.69 A; A/B=1-437.
DR PDB; 3OV7; X-ray; 3.00 A; A/B=1-437.
DR PDB; 3OVA; X-ray; 1.98 A; A=3-437.
DR PDB; 3OVB; X-ray; 1.95 A; A/B=1-437.
DR PDB; 3OVS; X-ray; 2.80 A; A/B=1-437.
DR PDB; 4X4N; X-ray; 2.95 A; A/C/E/F=1-437.
DR PDB; 4X4O; X-ray; 3.20 A; A/C=1-437.
DR PDB; 4X4P; X-ray; 3.00 A; A/C/E/G=1-437.
DR PDB; 4X4Q; X-ray; 3.15 A; A/C=1-437.
DR PDB; 4X4R; X-ray; 3.20 A; A/C=1-437.
DR PDB; 4X4S; X-ray; 3.25 A; A/C=1-437.
DR PDB; 4X4T; X-ray; 2.50 A; A/C/E/F=1-437.
DR PDB; 4X4U; X-ray; 2.70 A; A/C/E/F=1-437.
DR PDB; 4X4V; X-ray; 2.60 A; A/C=1-437.
DR PDBsum; 1R89; -.
DR PDBsum; 1R8A; -.
DR PDBsum; 1R8B; -.
DR PDBsum; 1R8C; -.
DR PDBsum; 1SZ1; -.
DR PDBsum; 1TFW; -.
DR PDBsum; 1TFY; -.
DR PDBsum; 1UET; -.
DR PDBsum; 1UEU; -.
DR PDBsum; 1UEV; -.
DR PDBsum; 2DR5; -.
DR PDBsum; 2DR7; -.
DR PDBsum; 2DR8; -.
DR PDBsum; 2DR9; -.
DR PDBsum; 2DRA; -.
DR PDBsum; 2DRB; -.
DR PDBsum; 2DVI; -.
DR PDBsum; 2ZH1; -.
DR PDBsum; 2ZH2; -.
DR PDBsum; 2ZH3; -.
DR PDBsum; 2ZH4; -.
DR PDBsum; 2ZH5; -.
DR PDBsum; 2ZH6; -.
DR PDBsum; 2ZH7; -.
DR PDBsum; 2ZH8; -.
DR PDBsum; 2ZH9; -.
DR PDBsum; 2ZHA; -.
DR PDBsum; 2ZHB; -.
DR PDBsum; 3OUY; -.
DR PDBsum; 3OV7; -.
DR PDBsum; 3OVA; -.
DR PDBsum; 3OVB; -.
DR PDBsum; 3OVS; -.
DR PDBsum; 4X4N; -.
DR PDBsum; 4X4O; -.
DR PDBsum; 4X4P; -.
DR PDBsum; 4X4Q; -.
DR PDBsum; 4X4R; -.
DR PDBsum; 4X4S; -.
DR PDBsum; 4X4T; -.
DR PDBsum; 4X4U; -.
DR PDBsum; 4X4V; -.
DR AlphaFoldDB; O28126; -.
DR SMR; O28126; -.
DR STRING; 224325.AF_2156; -.
DR PRIDE; O28126; -.
DR EnsemblBacteria; AAB89084; AAB89084; AF_2156.
DR GeneID; 24795903; -.
DR KEGG; afu:AF_2156; -.
DR eggNOG; arCOG04249; Archaea.
DR HOGENOM; CLU_044679_1_0_2; -.
DR OMA; DVDLVPC; -.
DR OrthoDB; 82755at2157; -.
DR PhylomeDB; O28126; -.
DR BRENDA; 2.7.7.72; 414.
DR EvolutionaryTrace; O28126; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 1.10.1410.30; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01264; CCA_arch; 1.
DR InterPro; IPR008229; CCA-adding_arc.
DR InterPro; IPR042090; CCA_tRNA_nucleotrans_2.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR015329; tRNA_NucTransf2.
DR PANTHER; PTHR39643; PTHR39643; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF09249; tRNA_NucTransf2; 1.
DR PIRSF; PIRSF005335; CCA_arch; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR03671; cca_archaeal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
KW Transferase; tRNA processing.
FT CHAIN 1..437
FT /note="CCA-adding enzyme"
FT /id="PRO_0000139065"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R8B,
FT ECO:0007744|PDB:1UEV"
FT BINDING 47
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R89,
FT ECO:0007744|PDB:1UEU"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R8B,
FT ECO:0007744|PDB:1UEV"
FT BINDING 50
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R89,
FT ECO:0007744|PDB:1UEU"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0007744|PDB:1UEV"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEV"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0007744|PDB:1R89, ECO:0007744|PDB:1UEV"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R8B,
FT ECO:0007744|PDB:1UEV"
FT BINDING 133
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R89,
FT ECO:0007744|PDB:1UEU"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R8B,
FT ECO:0007744|PDB:1UEV"
FT BINDING 152
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R89,
FT ECO:0007744|PDB:1UEU"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R8B,
FT ECO:0007744|PDB:1UEV"
FT BINDING 161
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:14592988,
FT ECO:0000269|PubMed:14636575, ECO:0007744|PDB:1R89,
FT ECO:0007744|PDB:1UEU"
FT MUTAGEN 50
FT /note="R->A: High decrease in both AMP and CMP
FT incorporation."
FT /evidence="ECO:0000269|PubMed:14592988"
FT MUTAGEN 110
FT /note="D->A: High decrease in both AMP and CMP
FT incorporation."
FT /evidence="ECO:0000269|PubMed:14592988"
FT MUTAGEN 133
FT /note="H->A: No decrease in both AMP and CMP
FT incorporation."
FT /evidence="ECO:0000269|PubMed:14592988"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 18..38
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4X4T"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 87..104
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1R89"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1R89"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3OUY"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:1R89"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1R89"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 324..334
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:1R89"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:1R89"
FT HELIX 426..433
FT /evidence="ECO:0007829|PDB:1R89"
SQ SEQUENCE 437 AA; 51385 MW; C5D57122F63CAC97 CRC64;
MKVEEILEKA LELVIPDEEE VRKGREAEEE LRRRLDELGV EYVFVGSYAR NTWLKGSLEI
DVFLLFPEEF SKEELRERGL EIGKAVLDSY EIRYAEHPYV HGVVKGVEVD VVPCYKLKEP
KNIKSAVDRT PFHHKWLEGR IKGKENEVRL LKGFLKANGI YGAEYKVRGF SGYLCELLIV
FYGSFLETVK NARRWTRRTV IDVAKGEVRK GEEFFVVDPV DEKRNVAANL SLDNLARFVH
LCREFMEAPS LGFFKPKHPL EIEPERLRKI VEERGTAVFA VKFRKPDIVD DNLYPQLERA
SRKIFEFLER ENFMPLRSAF KASEEFCYLL FECQIKEISR VFRRMGPQFE DERNVKKFLS
RNRAFRPFIE NGRWWAFEMR KFTTPEEGVR SYASTHWHTL GKNVGESIRE YFEIISGEKL
FKEPVTAELC EMMGVKD
