ID   Q12WX1_METBU            Unreviewed;       446 AA.
AC   Q12WX1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01264};
DE            EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01264};
GN   Name=cca {ECO:0000256|HAMAP-Rule:MF_01264,
GN   ECO:0000313|EMBL:ABE52055.1};
GN   OrderedLocusNames=Mbur_1130 {ECO:0000313|EMBL:ABE52055.1};
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564 {ECO:0000313|EMBL:ABE52055.1, ECO:0000313|Proteomes:UP000001979};
RN   [1] {ECO:0000313|Proteomes:UP000001979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M
RC   {ECO:0000313|Proteomes:UP000001979};
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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. tRNA 3'-terminal CCA addition is required both for tRNA
CC       processing and repair. Also involved in tRNA surveillance by mediating
CC       tandem CCA addition to generate a CCACCA at the 3' terminus of unstable
CC       tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs
CC       are marked with CCACCA and rapidly degraded. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_01264};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3'
CC         CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-
CC         COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071,
CC         ChEBI:CHEBI:195187; Evidence={ECO:0000256|HAMAP-Rule:MF_01264};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01264};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01264}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC       and CTP and is responsible for their addition. {ECO:0000256|HAMAP-
CC       Rule:MF_01264}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Archaeal CCA-adding enzyme subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01264}.
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DR   EMBL; CP000300; ABE52055.1; -; Genomic_DNA.
DR   RefSeq; WP_011499202.1; NC_007955.1.
DR   AlphaFoldDB; Q12WX1; -.
DR   STRING; 259564.Mbur_1130; -.
DR   GeneID; 3997737; -.
DR   KEGG; mbu:Mbur_1130; -.
DR   HOGENOM; CLU_044679_1_0_2; -.
DR   OrthoDB; 7378at2157; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; 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; 3.30.70.1550; Archaeal tRNA CCA-adding enzyme catalytic domain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.1410.30; CCA tRNA nucleotidyltransferase, domain 2; 1.
DR   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   HAMAP; MF_01264; CCA_arch; 1.
DR   InterPro; IPR048833; CAA_C.
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   NCBIfam; TIGR03671; cca_archaeal; 1.
DR   PANTHER; PTHR39643; CCA-ADDING ENZYME; 1.
DR   PANTHER; PTHR39643:SF1; CCA-ADDING ENZYME; 1.
DR   Pfam; PF21133; CAA_C_arc; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF09249; tRNA_NucTransf2; 1.
DR   PIRSF; PIRSF005335; CCA_arch; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01264};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264,
KW   ECO:0000313|EMBL:ABE52055.1};
KW   RNA repair {ECO:0000256|ARBA:ARBA00022800, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01264}.
FT   DOMAIN          39..141
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          154..264
FT                   /note="tRNA nucleotidyltransferase substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF09249"
FT   DOMAIN          283..427
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21133"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         52
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         55
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         141
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         160
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         169
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
SQ   SEQUENCE   446 AA;  50467 MW;  5B4AD00060D50EEB CRC64;
     MESLKKSILE KIKPTEKERE HLTKVADELM YKIDCLTFKV GLVGVKTQLV GSAARGTWIS
     GTHDLDIFIT FPDDTSREDL ESYGLSVGRQ VAKEAEHWDE HYAEHPYVKM RYKGFDVDLV
     PCYSVSSASS IISAVDRTPF HNEFIKANLN GLEDEVLLLK QFMRGTGVYG SELKTEGFSG
     YLTELLVINY GSFEKVLEAA SNWRPGLLLD ILEHGKLKFE DPLVVIDPTD PKRNVAAALS
     LDKFCTFVDM ARSFLCNPDE SMFFSSLIPP ISDNEIVERL EKKGSSLLAI VFKTPDVVDD
     IFYPQFAKME NSVVPMLDKN EFTVLKAGKW SGEDSVVMLE LMSGTLPNVK MHRGPPVWVR
     DHAEKFRDKY VDNEDAYSFT IKDGFYVAEI PRKHISAVEL LKKELANCSL GKHISKSVKE
     GFEILEGEQV LELKEDGFRS YLKSWL
//