ID A0A063B202_9BURK Unreviewed; 414 AA. AC A0A063B202; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-NOV-2018, entry version 38. DE RecName: Full=Multifunctional CCA protein {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=Phosphatase {ECO:0000256|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000256|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2'-nucleotidase {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=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=CCA 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',3'-cyclic phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01261}; DE EC=3.1.4.- {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; Proteobacteria; 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 CC template. Adds these three nucleotides in the order of C, C, and A CC to the tRNA nucleotide-73, using CTP and ATP as substrates and CC producing inorganic pyrophosphate. Also shows phosphatase, 2'- CC nucleotidase and 2',3'-cyclic phosphodiesterase activities. These CC phosphohydrolase activities are probably involved in the repair of CC the tRNA 3'-CCA terminus degraded by intracellular RNases. CC {ECO:0000256|SAAS:SAAS00958768}. CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a CC 3' CCA end + 3 diphosphate. {ECO:0000256|HAMAP-Rule:MF_01261, CC ECO:0000256|SAAS:SAAS00415332}. CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers. CC {ECO:0000256|HAMAP-Rule:MF_01261, ECO:0000256|SAAS:SAAS00958764}. CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the CC nucleotidyltransferase activity and a C-terminal HD domain CC associated with both phosphodiesterase and phosphatase activities. CC {ECO:0000256|HAMAP-Rule:MF_01261}. CC -!- MISCELLANEOUS: A single active site specifically recognizes both CC ATP and CTP and is responsible for their addition. CC {ECO:0000256|HAMAP-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|SAAS:SAAS00958770}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KDB06285; KDB06285; LIG30_4347. DR PATRIC; fig|1192124.4.peg.4586; -. DR Proteomes; UP000027020; Unassembled WGS sequence. 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: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: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; cd05398; NT_ClassII-CCAase; 1. DR HAMAP; MF_01261; CCA_bact_type1; 1. DR HAMAP; MF_01262; CCA_bact_type2; 1. DR InterPro; IPR012006; CCA_bact. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR032828; PolyA_RNA-bd. 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 PROSITE; PS51831; HD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00415369}; KW Complete proteome {ECO:0000313|Proteomes:UP000027020}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00958760, ECO:0000313|EMBL:KDB06285.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00820053}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00820061}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00958772}; KW Nickel {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00958750}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00415411}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00415426, ECO:0000313|EMBL:KDB06285.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000027020}; KW RNA repair {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00820060}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00415356}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00415377, ECO:0000313|EMBL:KDB06285.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01261, KW ECO:0000256|SAAS:SAAS00820063}. FT DOMAIN 232 333 HD. {ECO:0000259|PROSITE:PS51831}. FT METAL 21 21 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01261}. FT METAL 23 23 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01261}. FT BINDING 8 8 ATP or CTP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01261}. FT BINDING 11 11 ATP or CTP. {ECO:0000256|HAMAP-Rule: FT MF_01261}. FT BINDING 91 91 ATP or CTP. {ECO:0000256|HAMAP-Rule: FT MF_01261}. FT BINDING 143 143 ATP or CTP. {ECO:0000256|HAMAP-Rule: FT MF_01261}. FT BINDING 146 146 ATP or CTP. {ECO:0000256|HAMAP-Rule: FT 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 //