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

BX640420; CAE43328.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_881630.1; -.

3D structure databases

ModBase

Q7U358.

Enzyme and pathway databases

BioCyc

BPER257313:BP3059-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

2666541; -.

BX470248_GR; BP3059.

bpe:BP3059; -.

fig|257313.1.peg.2702; -.

Phylogenomic databases

HOGENOM

Q7U358; -.

Genome annotation databases

CMR

Q7U358; BP3059.

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`	`1 364`	`364`	`CCA-adding enzyme.`	`PRO_0000139016`
`METAL`	`32 32`		`Magnesium (By similarity).`
`METAL`	`34 34`		`Magnesium (By similarity).`
`BINDING`	`19 19`		`ATP or CTP; via amide nitrogen (By similarity).`
`BINDING`	`22 22`		`ATP or CTP (By similarity).`
`BINDING`	`102 102`		`ATP or CTP (By similarity).`
`BINDING`	`148 148`		`ATP or CTP (By similarity).`
`BINDING`	`151 151`		`ATP or CTP (By similarity).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39427 Da [This is the MW of the unprocessed precursor]

CRC64: B607EA021D20698D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRTDDPGVA GLRVYIVGGA VRDDLLGLPA GDRDWVVVGA TPEDMARRGF IPVGGDFPVF 

        70         80         90        100        110        120 
LHPRTKEEYA LARTERKSGR GYKGFTFYTG ADVTLEQDLQ RRDLTVNAIA RTPQGELVDP 

       130        140        150        160        170        180 
LDGVADVRAR VLRHVGEAFA EDPVRILRLG RFAARFGDFS IAPETMQLCR RMVEAGEADA 

       190        200        210        220        230        240 
LVPERVWKEV SRGLMAQAPS RMLDVLARAG ALARVMPELH DDTAVRAEID RAAAAGLPLA 

       250        260        270        280        290        300 
GRYALLCRHT PERDALGRRL RAPVECMDQA RLLPLAVDAL AASATPAAQL DLIERCDALR 

       310        320        330        340        350        360 
KPERFDALLQ AAAIVAPVDL SAWRARVQAV RAIDAGAIAR QCAGDPARIK PALRQARLQA 


LGGA

Q7U358 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