CCA-adding enzyme
     (EC 2.7.7.25)
     (EC 2.7.7.21)
     (tRNA nucleotidyltransferase)
     (tRNA adenylyl-/cytidylyl-transferase)
     (tRNA CCA-pyrophosphorylase)
     (tRNA-NT)
2'-nucleotidase
     (EC 3.1.3.-)
2',3'-cyclic phosphodiesterase
     (EC 3.1.4.-)
Phosphatase
     (EC 3.1.3.-)

Gene name

	Name:	cca
	OrderedLocusNames:	HD_1091

From

Haemophilus ducreyi

[TaxID: 730]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Wang J., Hanson E., Munson R.S. Jr.; Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=35000HP / ATCC 700724; Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.; "The complete genome sequence of Haemophilus ducreyi."; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.

Comments

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. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases (By similarity).
CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1).
CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1).
COFACTOR: Magnesium for nucleotidyltransferase activity (By similarity).
COFACTOR: Nickel for phosphatase activity (By similarity).
SUBUNIT: Monomer. Can also form homodimers and oligomers (By similarity).
DOMAIN: Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities (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 1 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

AF224467; AAF28362.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017143; AAP95957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_873568.1; -.

3D structure databases

ModBase

Q9L7A3.

Enzyme and pathway databases

BioCyc

HDUC233412:HD_1091-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004112;	Molecular function: cyclic-nucleotide phosphodiesterase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0016151;	Molecular function: nickel ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016791;	Molecular function: phosphatase activity (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_01261; -; 1.
PBIL [Tree]

InterPro

IPR012006; CCA_bact.
IPR003607; Met-dep_phosphohydro_HD.
IPR006674; Met-dep_phosphohydro_HD_sub.
IPR002646; PolyA_pol_reg.
Graphical view of domain structure.

Pfam

PF01966; HD; 1.
PF01743; PolyA_pol; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000813; CCA_bact; 1.

SMART

SM00471; HDc; 1.
SMART graphical view of domain structure.

ProtoNet

Q9L7A3.

Genome annotation databases

GeneID

1491020; -.

GenomeReviews

AE017143_GR; HD_1091.

KEGG

hdu:HD1091; -.

NMPDR

fig|233412.1.peg.933; -.

Phylogenomic databases

HOGENOM

Q9L7A3; -.

Genome annotation databases

CMR

Q9L7A3; HD_1091.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 412`	`412`	`Multifunctional CCA protein.`	`PRO_0000138979`
`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`	`138 138`		`ATP or CTP (By similarity).`
`BINDING`	`141 141`		`ATP or CTP (By similarity).`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 46685 Da [This is the MW of the unprocessed precursor]

CRC64: 4F5D348218E28066 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQIYLVGGAV RDQLLNLPIK DRDFLVVGAT AKELINQGYQ QVGADFPVFL HPVTQQEYAL 

        70         80         90        100        110        120 
ARQERKSGTG YTGFVCDFSP NVTLEQDLIR RDLTINAMAQ DLTSGQIFDP FGGKTDLANR 

       130        140        150        160        170        180 
LLRHISDAFA EDPLRVLRVA RFAARFHHLG FSIAEQTLEL MQKMTACGEL NHLTAERIWR 

       190        200        210        220        230        240 
ETEKALHTES PHIYFQVLRK VNALAILFPE IDQLFGQIQS VKYHLETDRG QHTLLALQQA 

       250        260        270        280        290        300 
KLLVKQAHNP TALLWAVLCH DLGKDLISAE MLPHHYQPNV TGIQLTHQLA DRLKVPTAVK 

       310        320        330        340        350        360 
ELALLVNKYH TNCHKIAELD SERVLELFNQ LDVWRKPQRL DDFLLACEAD ARARLGAEYC 

       370        380        390        400        410 
SYPQATLAID YFNAANAVNV QAIIADGFKK QAIRDELNNR RINIIKQIKN AI

Q9L7A3 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