CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007622
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CCA-adding enzyme 
Protein Synonyms/Alias
 CCA tRNA nucleotidyltransferase; tRNA CCA-pyrophosphorylase; tRNA adenylyl-/cytidylyl- transferase; tRNA nucleotidyltransferase; tRNA-NT 
Gene Name
 cca 
Gene Synonyms/Alias
 papS; ypjI; BSU22450 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
64QRTVDVGKEHGTIIVacetylation[1]
182ETEEAIAKEKSLLSHacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Has no poly(A) polymerase activity. 
Sequence Annotation
 METAL 40 40 Magnesium (By similarity).
 METAL 42 42 Magnesium (By similarity).
 BINDING 27 27 ATP or CTP; via amide nitrogen (By
 BINDING 30 30 ATP or CTP (By similarity).
 BINDING 111 111 ATP or CTP (By similarity).
 BINDING 154 154 ATP or CTP (By similarity).
 BINDING 157 157 ATP or CTP (By similarity).
 BINDING 160 160 ATP or CTP (By similarity).
 BINDING 163 163 ATP or CTP (By similarity).  
Keyword
 ATP-binding; Complete proteome; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding; Transferase; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 397 AA 
Protein Sequence
MEKVFIKALP VLRILIEAGH QAYFVGGAVR DSYMKRTIGD VDIATDAAPD QVERLFQRTV 60
DVGKEHGTII VLWEDETYEV TTFRTESDYV DFRRPSEVQF ISSLEEDLKR RDLTINAMAM 120
TADGKVLDYF GGKKDIDQKV IRTVGKPEDR FQEDALRMLR AVRFMSQLGF TLSPETEEAI 180
AKEKSLLSHV SVERKTIEFE KLLQGRASRQ ALQTLIQTRL YEELPGFYHK RENLISTSEF 240
PFFSLTSREE LWAALLINLG IVLKDAPLFL KAWKLPGKVI KEAIHIADTF GQSLDAMTMY 300
RAGKKALLSA AKISQLRQNE KLDEKKLKDI QYAYQNLPIK SLKDLDITGK DLLALRNRPA 360
GKWVSEELQW IEQAVVTGKL SNQKKHIEEW LKTCGQH 397 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:EC.
 GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:EC.
 GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:EC.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0004810; F:tRNA adenylyltransferase activity; IEA:HAMAP.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0016437; F:tRNA cytidylyltransferase activity; IEA:HAMAP.
 GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
 GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:HAMAP. 
Interpro
 IPR023068; CCA-adding_enz_firmicutes.
 IPR026007; PcnB/CCA-adding.
 IPR002646; PolA_pol_head_dom. 
Pfam
 PF01743; PolyA_pol 
SMART
  
PROSITE
  
PRINTS