ID CCA_BUCAP Reviewed; 412 AA. AC Q8KA53; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 05-MAY-2009, entry version 43. DE RecName: Full=CCA-adding enzyme; DE EC=2.7.7.25; DE EC=2.7.7.21; DE AltName: Full=tRNA nucleotidyltransferase; DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase; DE AltName: Full=tRNA CCA-pyrophosphorylase; DE AltName: Full=tRNA-NT; GN Name=cca; OrderedLocusNames=BUsg_058; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1). CC -!- CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1). CC -!- COFACTOR: Magnesium (By similarity). CC -!- MISCELLANEOUS: A single active site specifically recognizes both CC ATP and CTP and is responsible for their addition (By similarity). CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. Bacterial CCA-adding enzyme type 2 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013218; AAM67629.1; -; Genomic_DNA. DR RefSeq; NP_660418.1; -. DR GeneID; 1005874; -. DR GenomeReviews; AE013218_GR; BUsg_058. DR KEGG; bas:BUsg058; -. DR HOGENOM; Q8KA53; -. DR OMA; Q8KA53; NPHVYFQ. DR BioCyc; BAPH198804:BUSG058-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP. DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:HAMAP. DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW. DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:HAMAP. DR HAMAP; MF_01262; -; 1. DR InterPro; IPR012006; CCA_bact. DR InterPro; IPR002646; PolyA_pol_reg. DR Pfam; PF01743; PolyA_pol; 1. DR PIRSF; PIRSF000813; CCA_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleotidyltransferase; RNA repair; RNA-binding; KW Transferase; tRNA processing. FT CHAIN 1 412 CCA-adding enzyme. FT /FTId=PRO_0000139018. FT METAL 21 21 Magnesium (By similarity). FT METAL 23 23 Magnesium (By similarity). FT BINDING 8 8 ATP or CTP; via amide nitrogen (By FT similarity). FT BINDING 11 11 ATP or CTP (By similarity). FT BINDING 91 91 ATP or CTP (By similarity). FT BINDING 137 137 ATP or CTP (By similarity). FT BINDING 140 140 ATP or CTP (By similarity). SQ SEQUENCE 412 AA; 48583 MW; B0A850ECD5D20C22 CRC64; MKVYLVGGAV RDSLLNLPIK DRDWVIVGGT KEILLKKNFQ QVGKDFPVFL HPETHEEYSL ARKERKSGRG YTGFHTEFSS DVTLEEDLIR RDLTINAIAQ DENGNYIDPF QGRKDLNLRL LRHVSESFTE DPLRILRTAR FAANLMHLGF HIDKDTMILM CKMVKKNELL YLTKNRIWNE TEKAFKTLNP HVYFQILHAC KALNFIFPEI FFLYERRTFF SILFTNFYSI SFLSIGLSKI STLTKDVSIR FSYLCQFLSE KIDFSSTKEN YDDDSAKLVK KLCKRCNIPS HIEELAVLNT GFCVFLSSIH YQSSSNIIKM FSKIDAWRKP DRIYKLSFLC DFNLFYHQNK IDNSKLKTGF LKKCFFIIKD ISVKKILNQG FKGYQIKNEL NKLRVNKLKF WRMKKKCFFF KE //