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D5H3A8

- D5H3A8_LACCS

UniProt

D5H3A8 - D5H3A8_LACCS

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Protein
CCA-adding enzyme
Gene
cca, LCRIS_01046
Organism
Lactobacillus crispatus (strain ST1)
Status
Unreviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotationSAAS annotations

Catalytic activityi

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.UniRule annotationSAAS annotations

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP or CTP; via amide nitrogen By similarityUniRule annotation
Binding sitei36 – 361ATP or CTP By similarityUniRule annotation
Metal bindingi46 – 461Magnesium By similarityUniRule annotation
Metal bindingi48 – 481Magnesium By similarityUniRule annotation
Binding sitei117 – 1171ATP or CTP By similarityUniRule annotation
Binding sitei160 – 1601ATP or CTP By similarityUniRule annotation
Binding sitei163 – 1631ATP or CTP By similarityUniRule annotation
Binding sitei166 – 1661ATP or CTP By similarityUniRule annotation
Binding sitei169 – 1691ATP or CTP By similarityUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity Source: UniProtKB-EC
  3. CTP:3'-cytidine-tRNA cytidylyltransferase activity Source: UniProtKB-EC
  4. CTP:tRNA cytidylyltransferase activity Source: UniProtKB-EC
  5. magnesium ion binding Source: UniProtKB-HAMAP
  6. tRNA adenylyltransferase activity Source: UniProtKB-HAMAP
  7. tRNA binding Source: UniProtKB-HAMAP
  8. tRNA cytidylyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. RNA repair Source: UniProtKB-KW
  2. tRNA 3'-terminal CCA addition Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

NucleotidyltransferaseUniRule annotationSAAS annotations, Transferase

Keywords - Biological processi

RNA repairUniRule annotationSAAS annotations, tRNA processingUniRule annotationSAAS annotations

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotations, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding, RNA-bindingUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciLCRI748671:GIX1-1110-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CCA-adding enzymeUniRule annotation (EC:2.7.7.72UniRule annotation)
Alternative name(s):
CCA tRNA nucleotidyltransferase
tRNA CCA-pyrophosphorylase
tRNA adenylyl-/cytidylyl- transferase
tRNA nucleotidyltransferase
tRNA-NT
Gene namesi
Name:ccaUniRule annotationImported
Ordered Locus Names:LCRIS_01046Imported
OrganismiLactobacillus crispatus (strain ST1)Imported
Taxonomic identifieri748671 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
ProteomesiUP000002371: Chromosome

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotationSAAS annotations

Structurei

3D structure databases

ProteinModelPortaliD5H3A8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000253346.
KOiK00974.
OMAiDITTSAY.

Family and domain databases

HAMAPiMF_01263. CCA_bact_type3.
InterProiIPR023068. CCA-adding_enz_firmicutes.
IPR002646. PolA_pol_head_dom.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D5H3A8-1 [UniParc]FASTAAdd to Basket

« Hide

MIKIDNLPEI FTKAMPVLQI LENAGFEAYF VGGSVRDVLL HRHVHDVDIT    50
TSAYPEEVKE LFDKSIDTGI KHGTVTVLYG GESYEITTFR TESGYQDFRR 100
PDHVTFVQNL DEDLKRRDFT INALAMDTRG QIVDLFNGLD DLKNHVIRAV 150
GDPEKRFHED ALRMMRAVRF MSQLEFKLES KTQQAIKDNH KLLKKISVER 200
IREEFVKLGL GPHARQAFQV FLDTNLSEDV PDFGGKKDQL AIFPQLKFSP 250
TMENSLWSLI ILLLKLPNEQ IHRFMRDWKN SNAMTEQVER IINLFDLLSS 300
HAPSDYELFL AGEETLINTI DVAHIVGQPI SSEALVDRYM ALPIKKASEL 350
AVDGRFLIDR GMRPGAKLGQ TLNKIRELVV SGEVENNQEA IESYLTTIE 399
Length:399
Mass (Da):45,574
Last modified:June 15, 2010 - v1
Checksum:i90CE4AF4AF161D75
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FN692037 Genomic DNA. Translation: CBL50493.1.
RefSeqiYP_003601518.1. NC_014106.1.

Genome annotation databases

EnsemblBacteriaiCBL50493; CBL50493; LCRIS_01046.
GeneIDi9106371.
KEGGilcr:LCRIS_01046.
PATRICi37240911. VBILacCri149433_1022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FN692037 Genomic DNA. Translation: CBL50493.1 .
RefSeqi YP_003601518.1. NC_014106.1.

3D structure databases

ProteinModelPortali D5H3A8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBL50493 ; CBL50493 ; LCRIS_01046 .
GeneIDi 9106371.
KEGGi lcr:LCRIS_01046.
PATRICi 37240911. VBILacCri149433_1022.

Phylogenomic databases

HOGENOMi HOG000253346.
KOi K00974.
OMAi DITTSAY.

Enzyme and pathway databases

BioCyci LCRI748671:GIX1-1110-MONOMER.

Family and domain databases

HAMAPi MF_01263. CCA_bact_type3.
InterProi IPR023068. CCA-adding_enz_firmicutes.
IPR002646. PolA_pol_head_dom.
[Graphical view ]
Pfami PF01743. PolyA_pol. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiD5H3A8_LACCS
AccessioniPrimary (citable) accession number: D5H3A8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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