Reviewed, UniProtKB/Swiss-Prot Q0VMU8 (CCA_ALCBS)

Names and origin

Protein names

Recommended name:
    Multifunctional CCA protein
Including the following 4 domains:
    1- 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
    2- Recommended name:
            2'-nucleotidase
              EC=3.1.3.-
    3- Recommended name:
            2',3'-cyclic phosphodiesterase
              EC=3.1.4.-
    4- Recommended name:
            Phosphatase
              EC=3.1.3.-

Gene names

Name:	cca
Ordered Locus Names:	ABO_2052

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	410 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. 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). HAMAP MF_01261 CTP + tRNA(n) = diphosphate + tRNA(n+1). HAMAP MF_01261
Cofactor	Magnesium for nucleotidyltransferase activity By similarity. Nickel for phosphatase activity By similarity.
Subunit structure	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.
Sequence similarities	Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.

Ontologies

Keywords
Biological process	RNA repair tRNA processing
Ligand	ATP-binding Magnesium Metal-binding Nickel Nucleotide-binding RNA-binding
Molecular function	Hydrolase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
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 cyclic-nucleotide phosphodiesterase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatase activity 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 – 410	410	Multifunctional CCA protein HAMAP MF_01261		PRO_1000054246
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)
	Q0VMU8-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 6C154B4C7E43D51A	FASTA	410	45,874
	10 20 30 40 50 60 MNVYLVGGAV RDSLLGLPVT EKDWVVVGAT PKEMEANGFR PVGKDFPVFL HPKTQEEYAL 70 80 90 100 110 120 ARTERKSGHG YGGFTFHAAS TVSLEEDLIR RDLTINAMAQ ARGGEIIDPF NGRVDLKARL 130 140 150 160 170 180 LRHVSPAFAE DPLRVLRVAR FAARYHWLGF QVADDTLMLM KQLSDSGELG YLVAERVWKE 190 200 210 220 230 240 TSRALMERDP QVFFQVLHRC GALHALFPEL AALDGVPQPE QHHPEVDTLL HQFLCLKQAA 250 260 270 280 290 300 RLGLSLNARY ALLCHDLGKG KTPKEEWPRH IAHEIRSARL SKKVSKRLKV PKEAATLATL 310 320 330 340 350 360 VAEFHTHSHR ALELKPATVW KLFKSLDILR RPERLTDFLG ACEADARGRT SFENREYPQA 370 380 390 400 410 SYLQGAADAA RQVDIQALQA QGHEGPALGE AIEQARIDAI ATFKQQELNP

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL17500.1.
RefSeq	YP_693772.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4212963.
GenomeReviews	Gene locus ABO_2052 in contig AM286690_GR.
KEGG	abo:ABO_2052.
NMPDR	fig|393595.12.peg.2054.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VMU8.
OMA	Q0VMU8. KHHGHGQ.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_2052-MON.
Family and domain databases
HAMAP	MF_01261. [Tree]
InterPro	IPR012006. CCA_bact. IPR003607. Met-dep_phosphohydro_HD. IPR006674. Met-dep_phosphohydro_HD_sub. IPR002646. PolyA_pol_reg. [Graphical view]
Pfam	PF01966. HD. 1 hit. PF01743. PolyA_pol. 1 hit. [Graphical view]
PIRSF	PIRSF000813. CCA_bact. 1 hit.
SMART	SM00471. HDc. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCA_ALCBS

Accession

Primary (citable) accession number: Q0VMU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 20 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)