Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A8A9W2 (RTCA_IGNH4)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable RNA 3'-terminal phosphate cyclase
      Short name=RNA-3'-phosphate cyclase
      Short name=RNA cyclase
    EC=6.5.1.4
Gene names
Name: rtcA
Ordered Locus Names: Igni_0532
OrganismIgnicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125) [Complete proteome] [HAMAP]
Taxonomic identifier453591 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeIgnicoccus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the 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.

Catalytic activity

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

Subcellular location

Cytoplasm Potential.

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Probable RNA 3'-terminal phosphate cyclase HAMAP MF_00200
PRO_0000325190

Sites

Active site3151 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A9W2-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: F513232B42846DA7

FASTA35338,695
        10         20         30         40         50         60 
MIEIDGSFGE GGGQILRTSV ALSAVTLKPV RIFNIRAKRK NPGLRRQHMV AVKALAEMTD 

        70         80         90        100        110        120 
AEVRGLELGS TEIVFIPKTL KAGTFRFDIG TAGSVSLVLQ AVTPAALFAP GEVRVQLRGG 

       130        140        150        160        170        180 
TDVPMSPPVD YLRFVFYPLL ERFGAKTELV LKRRGHYPKG GGEVEFASRP VDSLTQWGEV 

       190        200        210        220        230        240 
ERGEVLKVRG LSHCVKLPKH VAERQAKAAE EVLKKSGLKN VDIDLEWYPP ERDPHLGPGS 

       250        260        270        280        290        300 
GIVLWAITER SLLGADSLGA RGKRAERVGE EAARKLLEDL STGKALDRHM SDMIVPYVSL 

       310        320        330        340        350 
ACGRTEVGGA ALTMHAWTHV HVVKKFLPEL EVEISGELNK PFVMRVKGVC WQR 

« Hide

References

[1]"Unicellular symbiosis at high temperature: genomic insights into the Ignicoccus hospitalis - Naoarchaeum equitans relationship."
Podar M., Anderson I., Ivanova N., Wall M., Mavrommatis K., Lykidis A., Chen J., Hudson M., Deciu C., Hutchison D., Eads J., Fernandes F., Tamang D., Szeto E., Land M., Lapidus A., Kyrpides N., Chang C. expand/collapse author list , Saier M., Eisen J., Rachel R., Huber H., Keller M., Richardson P., Stetter K.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000816 Genomic DNA. Translation: ABU81714.1.
RefSeqYP_001435121.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8A9W2.

Genome annotation databases

GeneID5562318.
GenomeReviewsGene locus Igni_0532 in contig CP000816_GR.
KEGGiho:Igni_0532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEIDGSYG.

Family and domain databases

HAMAPMF_00200.
[Tree]
InterProIPR000228. RNA3'_term_phos_cycl-like.
IPR013796. RNA3'_term_phos_cycl_insert.
IPR017770. RNA3'_term_phos_cycl_sub.
[Graphical view]
Gene3DG3DSA:3.65.10.20. RNA3'_term_phos_cycl. 1 hit.
PANTHERPTHR11096. RNA3'_term_phos_cycl. 1 hit.
PfamPF01137. RTC. 1 hit.
PF05189. RTC_insert. 1 hit.
[Graphical view]
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRTCA_IGNH4
AccessionPrimary (citable) accession number: A8A9W2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents