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P58032 (FLPA_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase

Short name=FIB
EC=2.1.1.-
Gene names
Name:flpA
Ordered Locus Names:SSO0940
ORF Names:C33_014
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Ref.2 Ref.3 Ref.5

Subunit structure

Interacts with nop5. Component of box C/D small ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5, plus a guide RNA. These sRNP particles form homodimers, giving rise to an asymmetric holoenzyme. Ref.2 Ref.4 Ref.5

Sequence similarities

Belongs to the methyltransferase superfamily. Fibrillarin family.

Ontologies

Keywords
   Biological processrRNA processing
tRNA processing
   LigandRNA-binding
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSO0939Q97ZH32EBI-2944159,EBI-2944135

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase HAMAP-Rule MF_00351
PRO_0000148549

Regions

Region89 – 902S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region108 – 1092S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region133 – 1342S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region153 – 1564S-adenosyl-L-methionine binding HAMAP-Rule MF_00351

Experimental info

Mutagenesis851A → V: Loss of methyltransferase activity. Ref.2
Mutagenesis1291P → A: Decreased methyltransferase activity. Ref.2

Secondary structure

................................................... 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58032 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: CFFB34D2D4FA9CF2

FASTA23226,422
        10         20         30         40         50         60 
MSEVITVKQT NMENIYECEF NDGSFRLCTR NLVPNFNVYG ERLIKYEGVE YREWNAFRSK 

        70         80         90        100        110        120 
LAGAILKGLK TNPIRKGTKV LYLGAASGTT ISHVSDIIEL NGKAYGVEFS PRVVRELLLV 

       130        140        150        160        170        180 
AQRRPNIFPL LADARFPQSY KSVVENVDVL YVDIAQPDQT DIAIYNAKFF LKVNGDMLLV 

       190        200        210        220        230 
IKARSIDVTK DPKEIYKTEV EKLENSNFET IQIINLDPYD KDHAIVLSKY KG 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"In vitro reconstitution and activity of a C/D box methylation guide ribonucleoprotein complex."
Omer A.D., Ziesche S., Ebhardt H., Dennis P.P.
Proc. Natl. Acad. Sci. U.S.A. 99:5289-5294(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-85 AND PRO-129, SUBUNIT.
[3]"RNA-guided nucleotide modification of ribosomal and non-ribosomal RNAs in Archaea."
Ziesche S.M., Omer A.D., Dennis P.P.
Mol. Microbiol. 54:980-993(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Structural organization of box C/D RNA-guided RNA methyltransferase."
Ye K., Jia R., Lin J., Ju M., Peng J., Xu A., Zhang L.
Proc. Natl. Acad. Sci. U.S.A. 106:13808-13813(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH RNA; S-ADENOSYL-L-METHIONINE; NOP5 AND RPL7AE, SUBUNIT.
[5]"Structural basis for site-specific ribose methylation by box C/D RNA protein complexes."
Lin J., Lai S., Jia R., Xu A., Zhang L., Lu J., Ye K.
Nature 469:559-563(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH GUIDE RNA; SUBSTRATE RNA AND RPL7AE, SUBUNIT, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006641 Genomic DNA. Translation: AAK41216.1.
PIRA99245.
RefSeqNP_342426.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ID5X-ray4.01B/F1-232[»]
3ID6X-ray2.60C1-232[»]
3PLAX-ray3.15E/F/M1-232[»]
ProteinModelPortalP58032.
SMRP58032. Positions 4-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48939N.
IntActP58032. 2 interactions.
STRING273057.SSO0940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK41216; AAK41216; SSO0940.
GeneID1455183.
KEGGsso:SSO0940.

Phylogenomic databases

eggNOGCOG1889.
HOGENOMHOG000106741.
KOK04795.
OMAWNPNKSK.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-893-MONOMER.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_00351. RNA_methyltransf_FlpA.
InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP58032.

Entry information

Entry nameFLPA_SULSO
AccessionPrimary (citable) accession number: P58032
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 76 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references