CCA_METKA
ID CCA_METKA Reviewed; 485 AA.
AC Q8TGY5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01264};
DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01264};
GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01264}; OrderedLocusNames=MK1366;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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:0000255|HAMAP-Rule:MF_01264}.
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:0000255|HAMAP-Rule:MF_01264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01264};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01264}.
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition. {ECO:0000255|HAMAP-
CC Rule:MF_01264}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Archaeal CCA-adding enzyme subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01264}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009439; AAM02579.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TGY5; -.
DR SMR; Q8TGY5; -.
DR STRING; 190192.MK1366; -.
DR PRIDE; Q8TGY5; -.
DR EnsemblBacteria; AAM02579; AAM02579; MK1366.
DR KEGG; mka:MK1366; -.
DR PATRIC; fig|190192.8.peg.1518; -.
DR HOGENOM; CLU_044679_1_0_2; -.
DR OMA; DVDLVPC; -.
DR Proteomes; UP000001826; 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 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
KW Transferase; tRNA processing.
FT CHAIN 1..485
FT /note="CCA-adding enzyme"
FT /id="PRO_0000139070"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 53
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 56
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 146
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 164
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
SQ SEQUENCE 485 AA; 55774 MW; 0D5F13590F3E14BB CRC64;
MSLEEVLDEI RREVTPDPEE RELVEGFARR ILSEVRDRLK ERDPDAEVEL IGSVARDTWL
PGASDVDVFC VFPKDRDLDE IVEVTLEVGR EAIEALGGEA REEYAHHPYI GGEVEHRGRT
FEVDVVPCYD TEPGEVITPV DRTPHHNRYV EEHLEDTVEA RLLKAFVKAI DAYGAEVRVK
GFSGYLCELL AIHYGSFEEV LREAVRTWRP GFVIDLEGFV GEVYEDYDEV RETFEDQDPA
LIVLDPVDPE RNVAAALSRR QLTRFILAAR AFLGDPSPEF FRGRKPEPVS GEKVRDWFER
NPTHVVAIEV RLPDEVEDIY WPQLEKTARS LSRVLENEGF EVRRWHVMRD SEEEHGYVLL
EFEHGKLPEL EWRVGPSGWV REDRVRGFVR AHGRFWVEED GKLATRAERK FVRPEDLLGR
LEGADRQTLL SHGFGKDLAR SSEGEVRLLS AEELAELADR DPELGKALAE FMRGDPLSEL
VRDRL
