Multifunctional CCA protein - Baumannia cicadellinicola subsp. Homalodisca coagulata

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Reviewed, UniProtKB/Swiss-Prot Q1LSL7 (CCA_BAUCH)

Last modified June 16, 2009. Version 19. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	BCI_0622

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

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Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

Multifunctional CCA protein HAMAP MF_01261

PRO_1000054249

Sites

Metal binding

Magnesium By similarity

Metal binding

Magnesium By similarity

Binding site

ATP or CTP; via amide nitrogen By similarity

Binding site

ATP or CTP By similarity

Binding site

ATP or CTP By similarity

Binding site

138

ATP or CTP By similarity

Binding site

141

ATP or CTP By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q1LSL7-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 3CEDBB6DB9D14326
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FASTA

412

47,235

        10         20         30         40         50         60 
MKKYLVGGAV RDRLLQIPVK ERDWVVIGTT LQDMLKAGYQ QVGKDFPVFL HPKSHEEYAL 

        70         80         90        100        110        120 
ARIEKKSATG GYTGFTYKAS SEITLEEDLK RRDLTINAIA CDENGSLIDP YNGQRDLNQR 

       130        140        150        160        170        180 
WLRHVSEAFC EDPLRVLRVA RFAAQLAYLN FRIVPETRLM MQHMISELPL LSPERIWKET 

       190        200        210        220        230        240 
EKALATRDPQ IYFQVLRDCG ALKTLFPEID ALFGVPAPAK WHPEIDTGIH TMMTVAMAAR 

       250        260        270        280        290        300 
LSDSIAVRFA SLCHDIGKGL TPRDHWPSHH GHGPAGIPLV QSLCQRLRVP NSIRNLAIIV 

       310        320        330        340        350        360 
TEYHDLLHYA VKLKPKTLIK LFYAIDVWRR PERLEQIIII SEADARGRAG YENHFYKPGQ 

       370        380        390        400        410 
FIREAYRIAS SIMPCQVISH NLTGNKIGEK LRQYRQQAIA TWKQQNYESK QQ

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References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	CP000238 Genomic DNA. Translation: ABF14019.1.
RefSeq	YP_589047.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4056331.
GenomeReviews	Gene locus BCI_0622 in contig CP000238_GR.
KEGG	bci:BCI_0622.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LSL7.
OMA	Q1LSL7. KHHGHGQ.
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...

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Entry information

Entry name

CCA_BAUCH

Accession

Primary (citable) accession number: Q1LSL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 19 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents