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C6A4N4 (RTCA_THESM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:TSIB_1528
OrganismThermococcus sibiricus (strain MM 739 / DSM 12597) [Complete proteome] [HAMAP]
Taxonomic identifier604354 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length350 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 – 350350RNA 3'-terminal phosphate cyclase HAMAP-Rule MF_00200
PRO_1000204099

Regions

Nucleotide binding290 – 2945ATP By similarity

Sites

Active site3141Tele-AMP-histidine intermediate By similarity
Binding site1001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C6A4N4 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 53A3AE817C034A5A

FASTA35038,601
        10         20         30         40         50         60 
MRVIDGSYGE GGGQILRTAV ALSVITGEPI KIINIRAKRS NPGLRPQHLH GILALKELSD 

        70         80         90        100        110        120 
AKVKGAKEGS TELEFYPKST RVRHVKVLIK TAGSISLVLQ ALLPAMVFAE EEVTFEITGG 

       130        140        150        160        170        180 
TDVAWSPPVD YLKHITLYAL EKLGIKVEIE IRRRGHYPRG GGFVIGKVYP WGTKRPLVAR 

       190        200        210        220        230        240 
TFDKIYSFEG ISHAVRLPSH VAIRQAKAAK EALERVYPSI PIKIHEEYYE QGKDPHFGPG 

       250        260        270        280        290        300 
SGIVIWANTD VLRLGGDALG ERGKPAEIVG REAAKALIEQ LGPRHAVDKF LGDQLIPFLT 

       310        320        330        340        350 
FAGGDIWVSE VTKHLITNVW VVEQFFGRVF EMEGEIGKPG KVRVVKKVEL 

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References

[1]"Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MM 739 / DSM 12597.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001463 Genomic DNA. Translation: ACS90579.1.
RefSeqYP_002994928.1. NC_012883.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING604354.TSIB_1528.

Proteomic databases

PRIDEC6A4N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS90579; ACS90579; TSIB_1528.
GeneID8096536.
KEGGtsi:TSIB_1528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0430.
HOGENOMHOG000015264.
KOK01974.
OMARRGHYPK.
ProtClustDBPRK04204.

Enzyme and pathway databases

BioCycTSIB604354:GHMS-1569-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]
SUPFAMSSF55205. SSF55205. 1 hit.
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRTCA_THESM
AccessionPrimary (citable) accession number: C6A4N4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 33 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