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C0Q0J3 (RTCA_SALPC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA 3'-terminal phosphate cyclase

Short name=RNA cyclase
Short name=RNA-3'-phosphate cyclase
EC=6.5.1.4
Gene names
Name:rtcA
Ordered Locus Names:SPC_3587
OrganismSalmonella paratyphi C (strain RKS4594) [Complete proteome] [HAMAP]
Taxonomic identifier476213 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing By similarity. HAMAP-Rule MF_00200

Catalytic activity

ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate. HAMAP-Rule MF_00200

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00200.

Sequence similarities

Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-3'-phosphate cyclase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344RNA 3'-terminal phosphate cyclase HAMAP-Rule MF_00200
PRO_1000195103

Regions

Nucleotide binding283 – 2875ATP By similarity

Sites

Active site3081Tele-AMP-histidine intermediate By similarity
Binding site1031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C0Q0J3 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: CB04C03426163CAA

FASTA34436,010
        10         20         30         40         50         60 
MARIIALDGA QGEGGGQILR SALSLSMITG QPFEMSGIRA GRAKPGLLRQ HLTAVRAATE 

        70         80         90        100        110        120 
ICGAQVNGDE LGSQQLRFTP GPIRGGEYRF AIGSAGSCML VLQTVLPALW FADGSSRVEV 

       130        140        150        160        170        180 
HGGTHNQAAP SADFICRVWE PLLARMGISQ RTTLIKHGFY PAGGGAAATV VEPATSLRGL 

       190        200        210        220        230        240 
TLISRGETLR TTAEALLAAV PYHVGEREVA TLEAHFPQAE KNVVALEGGC GPGNALSLMI 

       250        260        270        280        290        300 
QSEQLTELFV AFGVKGTSAE AVANQVAHEA RRYLASPAAV GEHLADQLIL PLALAGEGAF 

       310        320        330        340 
TVARASAHLL TNIAVVERFL PVTFNLEEAR GMVQVMVSKK DSGS 

« Hide

References

[1]"Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis and pathogenic convergence with Salmonella typhi."
Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.
PLoS ONE 4:E4510-E4510(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKS4594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000857 Genomic DNA. Translation: ACN47670.1.
RefSeqYP_002639111.1. NC_012125.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING476213.SPC_3587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN47670; ACN47670; SPC_3587.
PATRIC32366113. VBISalEnt12305_3640.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0430.
HOGENOMHOG000015264.
OMAAEMLLRN.
OrthoDBEOG6RNQDX.

Enzyme and pathway databases

BioCycSENT476213:GH8J-3648-MONOMER.

Family and domain databases

Gene3D3.30.360.20. 1 hit.
3.65.10.20. 2 hits.
HAMAPMF_00200. RTC.
InterProIPR013791. RNA3'-term_phos_cycl_insert.
IPR023797. RNA3'_phos_cyclase_dom.
IPR000228. RNA3'_term_phos_cyc.
IPR017770. RNA3'_term_phos_cyc_type_1.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PANTHERPTHR11096. PTHR11096. 1 hit.
PfamPF01137. RTC. 1 hit.
PF05189. RTC_insert. 1 hit.
[Graphical view]
SUPFAMSSF52913. SSF52913. 1 hit.
SSF55205. SSF55205. 2 hits.
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRTCA_SALPC
AccessionPrimary (citable) accession number: C0Q0J3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families