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D5H3A8 (D5H3A8_LACCS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CCA-adding enzyme HAMAP-Rule MF_01263
EC=2.7.7.72 HAMAP-Rule MF_01263
Alternative name(s):
CCA tRNA nucleotidyltransferase HAMAP-Rule MF_01263
tRNA CCA-pyrophosphorylase HAMAP-Rule MF_01263
tRNA adenylyl-/cytidylyl- transferase HAMAP-Rule MF_01263
tRNA nucleotidyltransferase HAMAP-Rule MF_01263
tRNA-NT HAMAP-Rule MF_01263
Gene names
Name:cca HAMAP-Rule MF_01263 EMBL CBL50493.1
Ordered Locus Names:LCRIS_01046
OrganismLactobacillus crispatus (strain ST1) [Complete proteome] [HAMAP] EMBL CBL50493.1
Taxonomic identifier748671 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus ›

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred 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-Rule MF_01263 SAAS SAAS002646

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP-Rule MF_01263 SAAS SAAS002646

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01263 SAAS SAAS002646

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01263 SAAS SAAS002646

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP-Rule MF_01263

Sequence similarities

Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily. HAMAP-Rule MF_01263

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding461Magnesium By similarity HAMAP-Rule MF_01263
Metal binding481Magnesium By similarity HAMAP-Rule MF_01263
Binding site331ATP or CTP; via amide nitrogen By similarity HAMAP-Rule MF_01263
Binding site361ATP or CTP By similarity HAMAP-Rule MF_01263
Binding site1171ATP or CTP By similarity HAMAP-Rule MF_01263
Binding site1601ATP or CTP By similarity HAMAP-Rule MF_01263
Binding site1631ATP or CTP By similarity HAMAP-Rule MF_01263
Binding site1661ATP or CTP By similarity HAMAP-Rule MF_01263
Binding site1691ATP or CTP By similarity HAMAP-Rule MF_01263

Sequences

Sequence LengthMass (Da)Tools
D5H3A8 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 90CE4AF4AF161D75

FASTA39945,574
        10         20         30         40         50         60 
MIKIDNLPEI FTKAMPVLQI LENAGFEAYF VGGSVRDVLL HRHVHDVDIT TSAYPEEVKE 

        70         80         90        100        110        120 
LFDKSIDTGI KHGTVTVLYG GESYEITTFR TESGYQDFRR PDHVTFVQNL DEDLKRRDFT 

       130        140        150        160        170        180 
INALAMDTRG QIVDLFNGLD DLKNHVIRAV GDPEKRFHED ALRMMRAVRF MSQLEFKLES 

       190        200        210        220        230        240 
KTQQAIKDNH KLLKKISVER IREEFVKLGL GPHARQAFQV FLDTNLSEDV PDFGGKKDQL 

       250        260        270        280        290        300 
AIFPQLKFSP TMENSLWSLI ILLLKLPNEQ IHRFMRDWKN SNAMTEQVER IINLFDLLSS 

       310        320        330        340        350        360 
HAPSDYELFL AGEETLINTI DVAHIVGQPI SSEALVDRYM ALPIKKASEL AVDGRFLIDR 

       370        380        390 
GMRPGAKLGQ TLNKIRELVV SGEVENNQEA IESYLTTIE

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Lactobacillus crispatus ST1."
Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P., Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.
J. Bacteriol. 192:3547-3548(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ST1.
[2]"Genome Sequence of Lactobacillus crispatus ST1."
Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P., Edelman S., Westerlund-Wikstroem B., Korhonen T.K., Paulin L., Kankainen M.
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ST1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FN692037 Genomic DNA. Translation: CBL50493.1.
RefSeqYP_003601518.1. NC_014106.1.

3D structure databases

ProteinModelPortalD5H3A8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBL50493; CBL50493; LCRIS_01046.
GeneID9106371.
KEGGlcr:LCRIS_01046.
PATRIC37240911. VBILacCri149433_1022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000253346.
KOK00974.
OMADITTSAY.

Enzyme and pathway databases

BioCycLCRI748671:GIX1-1110-MONOMER.

Family and domain databases

HAMAPMF_01263. CCA_bact_type3.
InterProIPR023068. CCA-adding_enz_firmicutes.
IPR026007. PcnB/CCA-adding.
IPR002646. PolA_pol_head_dom.
[Graphical view]
PANTHERPTHR13734:SF5. PTHR13734:SF5. 1 hit.
PfamPF01743. PolyA_pol. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD5H3A8_LACCS
AccessionPrimary (citable) accession number: D5H3A8
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 1, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info