Multifunctional CCA protein - Hahella chejuensis (strain KCTC 2396)

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Reviewed, UniProtKB/Swiss-Prot Q2SM94 (CCA_HAHCH)

Last modified June 16, 2009. Version 24. History...

Clusters with 100%, 90%, 50% identity |

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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:	HCH_01366

Organism

Hahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]

Taxonomic identifier

349521 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella

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Protein attributes

Sequence length	422 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 – 422

422

Multifunctional CCA protein HAMAP MF_01261

PRO_1000054268

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

Q2SM94-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 6099690A60677542
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FASTA

422

47,649

        10         20         30         40         50         60 
MQRYLVGGAV RDALLGLPVK DRDWVVVGAT PEQMLDQGYQ QVGADFPVFL HPESKEEHAL 

        70         80         90        100        110        120 
ARTERKSGKG YTGFICDFSP DISLEDDLLR RDLTINAMAM DDDGNLVDPF NGRQDLEARI 

       130        140        150        160        170        180 
LRHVSPAFTE DPLRVLRVAR FASRYADLGF TVAPETLQLM QDIQASGELK ALTAERVWQE 

       190        200        210        220        230        240 
TVRALGQKQP RVYFQVLKDA HALQDIFPEL NALFGVPQTP QYHPEVDTGL HSLMALEQAC 

       250        260        270        280        290        300 
LLSEREEVRF AALIHDLGKG VTPQEEWPKH HNHEAVGVDL VKALTERVKA PKLFKELALM 

       310        320        330        340        350        360 
ACQYHTHCHR ALELRANTLV KLLQSCDAWR RPDRFELFLL ACEADARGRT GWEQKPYPQA 

       370        380        390        400        410        420 
DFLRGVLETC QQIQPQELVA QGYTGARLGE EIQRRRISAV KRFKQDNAPE AQEKGGEDVG 


LT

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References

[1]

"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	CP000155 Genomic DNA. Translation: ABC28230.1.
RefSeq	YP_432655.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3838951.
GenomeReviews	Gene locus HCH_01366 in contig CP000155_GR.
KEGG	hch:HCH_01366.
NMPDR	fig\|349521.5.peg.1235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2SM94.
OMA	Q2SM94. KHHGHGQ.
Enzyme and pathway databases
BioCyc	HCHE349521:HCH_01366-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_HAHCH

Accession

Primary (citable) accession number: Q2SM94

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 24 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