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C6UW93 (C6UW93_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 20. 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:
RNA 3'-terminal phosphate cyclase HAMAP MF_00200

Short name=RNA cyclase HAMAP MF_00200
Short name=RNA-3'-phosphate cyclase HAMAP MF_00200
EC=6.5.1.4 HAMAP MF_00200
Gene names
Name:rtcA HAMAP MF_00200 EMBL ACT74098.1
Ordered Locus Names:ECSP_4372
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier544404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length342 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 MF_00200

Catalytic activity

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00200.

Sequence similarities

Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily. HAMAP MF_00200

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP MF_00200
   LigandATP-binding HAMAP MF_00200
Nucleotide-binding
   Molecular functionLigase HAMAP MF_00200
   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding283 – 2875ATP By similarity HAMAP MF_00200

Sites

Active site3081Tele-AMP-histidine intermediate By similarity HAMAP MF_00200
Binding site1031ATP By similarity HAMAP MF_00200

Sequences

Sequence LengthMass (Da)Tools
C6UW93 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 783FE7FAD7160846

FASTA34236,332
        10         20         30         40         50         60 
MKRMIALDGA QGEGGGQIMR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAATE 

        70         80         90        100        110        120 
ICGATVEGAE LGSQRLVFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV 

       130        140        150        160        170        180 
SGGTDNPSAP PADFIRRVLE PLLAKIGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL 

       190        200        210        220        230        240 
QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAASFSLHE QNIHNLPRDQ GPGNTVSLEV 

       250        260        270        280        290        300 
ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASPAAV GEYLADQLVL PMALAGAGQF 

       310        320        330        340 
TVAHPSCHLL TNIAVVERFL PVRFTLAETD GVTRVMITKL TD 

« Hide

References

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed: 19564389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001368 Genomic DNA. Translation: ACT74098.1.
RefSeqYP_003080174.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6UW93.
SMRC6UW93. Positions 4-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6UW93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000170056; EBESCP00000156919; EBESCG00000167012.
GeneID8218938.
GenomeReviewsGene locus ECSP_4372 in contig CP001368_GR.
KEGGetw:ECSP_4372.
PATRIC18392895. VBIEscCol9396_4437.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011893.
OMAGGTDVAW.
ProtClustDBPRK04204.

Family and domain databases

HAMAPMF_00200. RTC.
[Tree]
InterProIPR013791. RNA3'-term_phos_cycl_insert.
IPR023797. RNA3'_phos_cyclase_dom.
IPR000228. RNA3'_term_phos_cyc.
IPR017770. RNA3'_term_phos_cyc_type_1.
IPR020719. RNA3'_term_phos_cycl-like_CS.
IPR013796. RNA3'_term_phos_cycl_insert.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
Gene3DG3DSA:3.30.360.20. G3DSA:3.30.360.20. 1 hit.
G3DSA:3.65.10.20. RNA3'_term_phos_cycl. 2 hits.
KOK01974.
PANTHERPTHR11096. RNA3'_term_phos_cycl. 1 hit.
PfamPF01137. RTC. 1 hit.
PF05189. RTC_insert. 1 hit.
[Graphical view]
SUPFAMSSF52913. RNA3'-term_phos_cycl_insert. 1 hit.
SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 2 hits.
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6UW93_ECO5T
AccessionPrimary (citable) accession number: C6UW93
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: December 14, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)