Q058D0 (CCA_BUCCC) 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:	BCc_038

Organism

Buchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]

Taxonomic identifier

372461 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	414 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 – 414	414	CCA-adding enzyme HAMAP MF_01262		PRO_1000054315
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	92	1	ATP or CTP By similarity
	Binding site	138	1	ATP or CTP By similarity
	Binding site	141	1	ATP or CTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q058D0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 9627D5C5071E5858	FASTA	414	49,356
	10 20 30 40 50 60 MKIYLVGGAI RDRLLNIPVR DRDWVVVGIR DPKEMLKKNY QQVGKGFPVF IHPKTHEEYS 70 80 90 100 110 120 LARTEKKNGV GHTGFLFDFS SRITLKEDLK RRDLTINAIA QDSSGKIIDF FNGKKDIQKK 130 140 150 160 170 180 ILRHVSYSFQ EDPLRVLRIA RFAALLSHLG FYIAKKTLSL MKLICSRKEL LYLTPERIWK 190 200 210 220 230 240 ETQKGLSTQN PHVYFQVLYS CNALFFLFPE INYFYKKTYF LNSFIKHINL VQYSLIELSK 250 260 270 280 290 300 ISKVTKDINI RFSYFLQFFY YVYPIPNIGT KDYFFYKKPA FLLKKMLIRL KIPKETSEII 310 320 330 340 350 360 FFLCGFHNFL QNINIQSSKL IIKFFNIIDV WRKPNRLNQL IYLDFYNFNS LKNKKNDFFL 370 380 390 400 410 GKLLKYMFSL IKDISVCSFI KEKKFKGIEI KNDLNRLRIQ SFKEMKEKII LNIF

References

[1]

"A small microbial genome: the end of a long symbiotic relationship?" Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A. Science 314:312-313(2006) [PubMed: 17038625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Cc.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000263 Genomic DNA. Translation: ABJ90519.1.
RefSeq	YP_802612.1. NC_008513.1.
3D structure databases
ProteinModelPortal	Q058D0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q058D0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000001432; EBBUCP00000001342; EBBUCG00000001432.
GeneID	4440713.
GenomeReviews	Gene locus BCc_038 in contig CP000263_GR.
KEGG	bcc:BCc_038.
PATRIC	21246011. VBIBucAph7855_0033.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0617.
GeneTree	EBGT00050000008009.
HOGENOM	HBG635063.
OMA	QVGKGFP.
ProtClustDB	PRK13298.
Enzyme and pathway databases
BioCyc	BAPH372461:BCC_038-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_BUCCC

Accession

Primary (citable) accession number: Q058D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program