FUNCTION: 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 (By similarity).
CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1).
CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1).
COFACTOR: Magnesium (By similarity).
MISCELLANEOUS: A single active site specifically recognizes both ATP and CTP and is responsible for their addition (By similarity).
SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE016826; AAO26796.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777691.1; -.

3D structure databases

ModBase

Q89B06.

Enzyme and pathway databases

BioCyc

BAPH224915:BBP_057-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004810;	Molecular function: tRNA adenylyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0000049;	Molecular function: tRNA binding (inferred from electronic annotation from HAMAP).
GO:0016437;	Molecular function: tRNA cytidylyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0042245;	Biological process: RNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0001680;	Biological process: tRNA 3'-terminal CCA addition (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01262; -; 1.
PBIL [Tree]

InterPro

IPR012006; CCA_bact.
IPR002646; PolyA_pol_reg.
Graphical view of domain structure.

Pfam

PF01743; PolyA_pol; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000813; CCA_bact; 1.

Genome annotation databases

GeneID

1058541; -.

GenomeReviews

AE016826_GR; bbp_057.

KEGG

bab:bbp057; -.

Phylogenomic databases

HOGENOM

Q89B06; -.

Genome annotation databases

CMR

Q89B06; bbp_057.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; RNA repair; RNA-binding; Transferase; tRNA processing.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 419`	`419`	`CCA-adding enzyme.`	`PRO_0000139019`
`METAL`	`21 21`		`Magnesium (By similarity).`
`METAL`	`23 23`		`Magnesium (By similarity).`
`BINDING`	`8 8`		`ATP or CTP; via amide nitrogen (By similarity).`
`BINDING`	`11 11`		`ATP or CTP (By similarity).`
`BINDING`	`91 91`		`ATP or CTP (By similarity).`
`BINDING`	`137 137`		`ATP or CTP (By similarity).`
`BINDING`	`140 140`		`ATP or CTP (By similarity).`

Sequence information

Length: 419 AA [This is the length of the unprocessed precursor]

Molecular weight: 49614 Da [This is the MW of the unprocessed precursor]

CRC64: A8C5D8926575D90A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVYLVGGAI RNKFLNLPVQ DRDWVVVGAT PEILLSLKFK QVGKGFPVFL HPYSKEEYSL 

        70         80         90        100        110        120 
ARVDRKIGVG HTGFSFDYSN KVTLKEDLMR RDLTINAIAQ DNNGNYIDPF KGIRDIKNRI 

       130        140        150        160        170        180 
LRHVSPAFSE DPLRVLRIAR FCALFHHLGF RIATETMKIM SIVVKNNELL NLTRDRVWKE 

       190        200        210        220        230        240 
TEKAFNTDNP HVYFQVLKNC NALSVIFPEI NLVYQRQYYC IDNMYHNFYD TFDIFMGLAE 

       250        260        270        280        290        300 
LSKISRDIDI RFSYLFFCIN RMLFIDTSSY ILVINQKELV RYFKALCQRF CIPAYIKNVS 

       310        320        330        340        350        360 
ICFSRFYKFL SVIHYQSSKD IIMFFYIIDA WRKPYMIRKL SVLNNFCVSR NAYFKNITCQ 

       370        380        390        400        410 
QYPRNFLKYA FNVANKISIK PILKMGFSGL QIKYELIRLR INAIENWRQN ITVYKKCCF

Q89B06 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools