Q89B06 (CCA_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CCA-adding enzyme
EC=2.7.7.72

Alternative name(s):
CCA tRNA nucleotidyltransferase
tRNA CCA-pyrophosphorylase
tRNA adenylyl-/cytidylyl- transferase
tRNA nucleotidyltransferase
tRNA-NT

Gene names

Name:	cca
Ordered Locus Names:	bbp_057

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
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. HAMAP MF_01262
Catalytic activity	A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP MF_01262
Cofactor	Magnesium By similarity. HAMAP MF_01262
Miscellaneous	A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP MF_01262
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: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA adenylyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	CCA-adding enzyme HAMAP MF_01262		PRO_0000139019
Sites
	Metal binding	21	1	Magnesium By similarity
	Metal binding	23	1	Magnesium By similarity
	Binding site	8	1	ATP or CTP; via amide nitrogen By similarity
	Binding site	11	1	ATP or CTP By similarity
	Binding site	91	1	ATP or CTP By similarity
	Binding site	137	1	ATP or CTP By similarity
	Binding site	140	1	ATP or CTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89B06 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A8C5D8926575D90A	FASTA	419	49,614
	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

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26796.1.
RefSeq	NP_777691.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89B06.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002518; EBBUCP00000002342; EBBUCG00000002518.
GeneID	1058541.
GenomeReviews	Gene locus bbp_057 in contig AE016826_GR.
KEGG	bab:bbp057.
PATRIC	21244887. VBIBucAph80364_0054.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008009.
HOGENOM	HBG635063.
OMA	QVGKGFP.
ProtClustDB	PRK13298.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_057-MONOMER.
Family and domain databases
HAMAP	MF_01262. CCA_bact_type2. [Tree]
InterPro	IPR012006. CCA_bact. IPR002646. PolA_pol_head_dom. [Graphical view]
KO	K00974.
Pfam	PF01743. PolyA_pol. 1 hit. [Graphical view]
PIRSF	PIRSF000813. CCA_bact. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CCA_BUCBP

Accession

Primary (citable) accession number: Q89B06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program