Reviewed, UniProtKB/Swiss-Prot Q7U391 (CCA_BORBR)

Names and origin

Protein names

Recommended name:
    CCA-adding enzyme
    EC=2.7.7.25
    EC=2.7.7.21
Alternative name(s):
    tRNA nucleotidyltransferase
    tRNA adenylyl-/cytidylyl- transferase
    tRNA CCA-pyrophosphorylase
    tRNA-NT

Gene names

Name:	cca
Ordered Locus Names:	BB0207

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 By similarity.
Catalytic activity	ATP + tRNA(n) = diphosphate + tRNA(n+1). HAMAP MF_01262 CTP + tRNA(n) = diphosphate + tRNA(n+1). HAMAP MF_01262
Cofactor	Magnesium By similarity.
Miscellaneous	A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity.
Sequence similarities	Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.

Ontologies

Keywords
Biological process	RNA repair tRNA processing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA repair Inferred from electronic annotation. Source: UniProtKB-KW tRNA 3'-terminal CCA addition Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP tRNA adenylyltransferase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP tRNA cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	CCA-adding enzyme HAMAP MF_01262		PRO_0000139014
Sites
	Metal binding	32	1	Magnesium By similarity
	Metal binding	34	1	Magnesium By similarity
	Binding site	19	1	ATP or CTP; via amide nitrogen By similarity
	Binding site	22	1	ATP or CTP By similarity
	Binding site	102	1	ATP or CTP By similarity
	Binding site	148	1	ATP or CTP By similarity
	Binding site	151	1	ATP or CTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7U391-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: FEF8DF92C5A9C4F3	FASTA	364	39,281
	10 20 30 40 50 60 MSRADDPGVA GLQVYIVGGA VRDGLLGLPA 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 DDAAVRAEID 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

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640437 Genomic DNA. Translation: CAE30705.1.
RefSeq	NP_886756.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2662352.
GenomeReviews	Gene locus BB0207 in contig BX470250_GR.
KEGG	bbr:BB0207.
NMPDR	fig|257310.1.peg.203.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7U391.
OMA	Q7U391. ARQCAGD.
Enzyme and pathway databases
BioCyc	BBRO257310:BB0207-MON.
BRENDA	2.7.7.21. 413. 2.7.7.25. 413.
Family and domain databases
HAMAP	MF_01262. [Tree]
InterPro	IPR012006. CCA_bact. IPR002646. PolyA_pol_reg. [Graphical view]
Pfam	PF01743. PolyA_pol. 1 hit. [Graphical view]
PIRSF	PIRSF000813. CCA_bact. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CCA_BORBR

Accession

Primary (citable) accession number: Q7U391

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2003
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)