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).
SUBUNIT: Homodimer (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. Archaeal CCA-adding enzyme 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

BA000002; BAA80794.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E72563; E72563.

RefSeq

NP_148168.2; -.

3D structure databases

HSSP

O28126; 1UET. [HSSP ENTRY / PDB]

ModBase

Q9YB04.

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_01264; -; 1.
PBIL [Tree]

InterPro

IPR008229; CCA-adding_enz.
IPR002934; Nucleotidyltransferase.
IPR015329; tRNA_NucTransf2.
Graphical view of domain structure.

Pfam

PF01909; NTP_transf_2; 1.
PF09249; tRNA_NucTransf2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005335; CCA_arch; 1.

ProtoNet

Q9YB04.

Genome annotation databases

GeneID

1446242; -.

GenomeReviews

BA000002_GR; APE_1791.1.

KEGG

ape:APE_1791.1; -.

NMPDR

fig|272557.1.peg.1276; -.

Phylogenomic databases

HOGENOM

Q9YB04; -.

Genome annotation databases

CMR

Q9YB04; APE_1791.1.

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`	`1 465`	`465`	`CCA-adding enzyme.`	`PRO_0000139064`
`METAL`	`75 75`		`Magnesium (By similarity).`
`METAL`	`77 77`		`Magnesium (By similarity).`
`METAL`	`127 127`		`Magnesium (By similarity).`
`BINDING`	`63 63`		`ATP or CTP (By similarity).`
`BINDING`	`66 66`		`ATP or CTP (By similarity).`
`BINDING`	`149 149`		`ATP or CTP (By similarity).`
`BINDING`	`171 171`		`ATP or CTP (By similarity).`
`BINDING`	`180 180`		`ATP or CTP (By similarity).`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 51778 Da [This is the MW of the unprocessed precursor]

CRC64: DF472F68507B2673 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRGASGESVL PEDLRSRVLE RIRPTRLQFS MLGRLYSLVA RALEECEDLR LSIPSYRVEL 

        70         80         90        100        110        120 
VGSAAKGTLL RDKWEVDVFL LLDAPREEVR RLGESLLRSC LGGRLPYYFK YSEHPYATVS 

       130        140        150        160        170        180 
LMGMQADVVP APLAVDPRDA VGVERTPFHT RYVRSRLEER PWLVDDILLF KSFLKGIGVY 

       190        200        210        220        230        240 
GAETRVGGFS GYLAEVLIIH HGGFEETVKA ASSWRPPVMV DTTSGKADLD MLARRYPDSP 

       250        260        270        280        290        300 
IIVPDPVDPS RNTAASVTPK RLAELVHAAN IFLRKPSPTF FHALQPGEPC RRTLPGVMVL 

       310        320        330        340        350        360 
MSGNYSDHPP DSVWGRLKRL GERLYRATKA RGYPALSYSF YTDEALEAAV YIHMESPSRY 

       370        380        390        400        410        420 
PIEGRLGPPP WERERAARFT EKRLGEGGWV WIGDDGRLSG ARPYTGSAAG DVERALATLP 

       430        440        450        460 
LPPGTRSYKV VTCPSTGPCG FPSYLEALRD PTPPWLRHVL GGCRS

Q9YB04 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