Multifunctional CCA protein - Escherichia coli O6:K15:H31 (strain 536 / UPEC)

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Reviewed, UniProtKB/Swiss-Prot Q0TD50 (CCA_ECOL5)

Last modified June 16, 2009. Version 18. 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:	ECP_3146

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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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_1000054263

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

137

ATP or CTP By similarity

Binding site

140

ATP or CTP By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q0TD50-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A30BADF112522AC9
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FASTA

412

46,382

        10         20         30         40         50         60 
MKIYLVGGAV RDALLGLPVK DRDWVVVGST PQEMLDAGYQ QVGRDFPVFL HPQTHEEYAL 

        70         80         90        100        110        120 
ARTERKSGSG YTGFTCYAAP DVTLEDDLKR RDLTINALAQ DDNGEIIDPY NGLGDLQNRL 

       130        140        150        160        170        180 
LRHVSPAFGE DPLRVLRVAR FAARYAHLGF RIADETLALM REMTHAGELE HLTPERVWKE 

       190        200        210        220        230        240 
TESALTTRNP QVFFQVLRDC GALRVLFPEI DALFGVPAPA RWHPEIDTGI HTLMTLSMAA 

       250        260        270        280        290        300 
MLSPQVDVRF ATLCHDLGKG LTPPELWPRH HGHGPAGVKL VEQLCQRLRV PSEIRDLARL 

       310        320        330        340        350        360 
VAEFHDLIHT FPMLNPKTIV KLFDSIDAWR KPQRVEQLAL TSEADVRGRT GFESADYPQG 

       370        380        390        400        410 
RWLREAWEVA QSVPTKAVVE AGFKGVGIRE ELTRRRIAAV ASWKEQRCPK PD

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References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	CP000247 Genomic DNA. Translation: ABG71129.1.
RefSeq	YP_671030.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4188563.
GenomeReviews	Gene locus ECP_3146 in contig CP000247_GR.
KEGG	ecp:ECP_3146.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TD50.
OMA	Q0TD50. KHHGHGQ.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_3146-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...

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Entry information

Entry name

CCA_ECOL5

Accession

Primary (citable) accession number: Q0TD50

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 18 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents