Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1R5L5 (RTCA_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:UTI89_C3920
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length338 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.

Sequence caution

The sequence ABE09349.1 differs from that shown. Reason: Erroneous initiation.

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 – 338338RNA 3'-terminal phosphate cyclase HAMAP-Rule MF_00200
PRO_0000264794

Regions

Nucleotide binding283 – 2875ATP By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q1R5L5 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 89F388CC1BC7FF02

FASTA33835,896
        10         20         30         40         50         60 
MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAAAE 

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

       130        140        150        160        170        180 
SGGTDNPSAP PADFIRRVLE PLLAKIGVHQ QTTLLRHGFY PAGGGVVATE VSPVASFNSL 

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

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

       310        320        330 
TVAHPSCHLL TNIAVVERFL PVRFGLIETD GVTRVSIE 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE09349.1. Different initiation.
RefSeqYP_542880.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R5L5.
SMRQ1R5L5. Positions 4-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING364106.UTI89_C3920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE09349; ABE09349; UTI89_C3920.
GeneID3994280.
KEGGeci:UTI89_C3920.
PATRIC18457278. VBIEscCol42261_3838.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0430.
HOGENOMHOG000015264.
KOK01974.
OMARRGHYPK.
OrthoDBEOG6RNQDX.
ProtClustDBPRK04204.

Enzyme and pathway databases

BioCycECOL364106:GHPQ-3883-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.
IPR020719. RNA3'_term_phos_cycl-like_CS.
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.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRTCA_ECOUT
AccessionPrimary (citable) accession number: Q1R5L5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 57 of the entry and version 2 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