ID A0A063B202_9BURK Unreviewed; 414 AA. AC A0A063B202; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 24-JUL-2024, entry version 62. DE RecName: Full=Multifunctional CCA protein {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01261}; DE EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01261}; DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000256|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2'-nucleotidase {ECO:0000256|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01261}; DE EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=Phosphatase {ECO:0000256|HAMAP-Rule:MF_01261}; GN Name=cca {ECO:0000256|HAMAP-Rule:MF_01261}; GN ORFNames=LIG30_4347 {ECO:0000313|EMBL:KDB06285.1}; OS Burkholderia sp. lig30. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB06285.1, ECO:0000313|Proteomes:UP000027020}; RN [1] {ECO:0000313|EMBL:KDB06285.1, ECO:0000313|Proteomes:UP000027020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020}; RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M., RA Brown S.D., Hazen T.C.; RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30, RT Isolated from Wet Tropical Forest Soil."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. 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_01261}. 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_01261}; 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_01261}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01261}; CC Note=Magnesium is required for nucleotidyltransferase activity. CC {ECO:0000256|HAMAP-Rule:MF_01261}; CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01261}; CC Note=Nickel for phosphatase activity. {ECO:0000256|HAMAP- CC Rule:MF_01261}; CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers. CC {ECO:0000256|HAMAP-Rule:MF_01261}. CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the CC nucleotidyltransferase activity and a C-terminal HD domain associated CC with both phosphodiesterase and phosphatase activities. CC {ECO:0000256|HAMAP-Rule:MF_01261}. 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_01261}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. Bacterial CCA-adding enzyme type 1 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01261}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KDB06285.1}. 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; JGVW01000114; KDB06285.1; -; Genomic_DNA. DR RefSeq; WP_038715479.1; NZ_JGVW01000114.1. DR AlphaFoldDB; A0A063B202; -. DR STRING; 1192124.LIG30_4347; -. DR PATRIC; fig|1192124.4.peg.4586; -. DR eggNOG; COG0617; Bacteria. DR OrthoDB; 9805698at2; -. DR Proteomes; UP000027020; Unassembled WGS sequence. 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:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016791; F:phosphatase activity; 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; cd05398; NT_ClassII-CCAase; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1. DR HAMAP; MF_01261; CCA_bact_type1; 1. DR HAMAP; MF_01262; CCA_bact_type2; 1. DR InterPro; IPR012006; CCA_bact. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR InterPro; IPR050124; tRNA_CCA-adding_enzyme. DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1. DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1. DR Pfam; PF01966; HD; 1. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR PIRSF; PIRSF000813; CCA_bact; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1. DR PROSITE; PS51831; HD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01261}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01261}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01261}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01261}; Reference proteome {ECO:0000313|Proteomes:UP000027020}; KW RNA repair {ECO:0000256|ARBA:ARBA00022800, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01261}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_01261}. FT DOMAIN 232..333 FT /note="HD" FT /evidence="ECO:0000259|PROSITE:PS51831" FT BINDING 8 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 8 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 11 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 21 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 23 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 91 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 143 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 143 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 146 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" FT BINDING 146 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261" SQ SEQUENCE 414 AA; 45437 MW; 75DDBE7362850F60 CRC64; MNVYAVGGAI RDALLGVPVQ DRDYVVVGAT PEQMAAQGFK PVGKDFPVFL HPETHEEYAL ARTERKTAAG YHGFRFHYAP DVTLEDDLAR RDLTVNAMAR EVSPGGALIG PVIDPFDGQA DLRARRFRHV SDAFVEDPVR ILRVARFAAR FADFTVADET NTLMRRMVDA GEADALVAER VWQEVARGLM EARPSRMFEV LRGCGALARI LPEIDALFGV PQRADYHPEV DTGVHVMMVV DHAAKQGYSL AVRFAALTHD LGKATTPADV LPRHIGHEGR SVDLLKPLCE RLRVPNECRD LALVVAREHG NLHRVMEFGA AALVRLFERT DALRKPARFA EVVQACEADA RGRLGFAVQP YPQAERLREA LVAARSVDAG AIARTLGDDP ARIKDAVHRA RIQAVALAAG VSDE //