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Q8U4M2

- FLPA_PYRFU

UniProt

Q8U4M2 - FLPA_PYRFU

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Protein

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase

Gene

flpA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.2 PublicationsUniRule annotation

GO - Molecular functioni

  1. methyltransferase activity Source: UniProtKB-HAMAP
  2. RNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. rRNA processing Source: UniProtKB-HAMAP
  2. tRNA processing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing, tRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferaseUniRule annotation (EC:2.1.1.-UniRule annotation)
Gene namesi
Name:flpAUniRule annotation
Ordered Locus Names:PF0059
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Fibrillarin-like rRNA/tRNA 2'-O-methyltransferasePRO_0000148545Add
BLAST

Proteomic databases

PRIDEiQ8U4M2.

Interactioni

Subunit structurei

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.4 PublicationsUniRule annotation

Protein-protein interaction databases

DIPiDIP-60606N.
STRINGi186497.PF0059.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Beta strandi12 – 165
Beta strandi18 – 203
Beta strandi22 – 276
Beta strandi29 – 324
Beta strandi35 – 373
Beta strandi40 – 434
Beta strandi46 – 505
Turni53 – 553
Helixi57 – 637
Beta strandi76 – 816
Helixi87 – 959
Turni96 – 983
Beta strandi99 – 1068
Helixi108 – 11811
Beta strandi124 – 1285
Beta strandi131 – 1333
Helixi134 – 1407
Beta strandi144 – 1496
Helixi156 – 16712
Beta strandi168 – 17912
Helixi180 – 1834
Beta strandi185 – 1873
Helixi189 – 20113
Beta strandi204 – 2118
Turni213 – 2153
Beta strandi216 – 22510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PRYX-ray1.97A1-227[»]
2NNWX-ray2.70B/D1-227[»]
3NMUX-ray2.73F/J1-227[»]
3NVKX-ray3.21I/J1-227[»]
3NVMX-ray3.41B1-227[»]
4BY9NMR-E/H/K/N1-227[»]
ProteinModelPortaliQ8U4M2.
SMRiQ8U4M2. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U4M2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 872S-adenosyl-L-methionine bindingUniRule annotation
Regioni105 – 1062S-adenosyl-L-methionine binding
Regioni130 – 1312S-adenosyl-L-methionine binding
Regioni150 – 1534S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the methyltransferase superfamily. Fibrillarin family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1889.
HOGENOMiHOG000106741.
KOiK04795.
OMAiWNPNKSK.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8U4M2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVEVKKHKFP GVYVVIDDDG SEKIATKNLV PGQRVYGERV IKWEGEEYRI
60 70 80 90 100
WNPHRSKLGA AIVNGLKNFP IKPGKSVLYL GIASGTTASH VSDIVGWEGK
110 120 130 140 150
IYGIEFSPRV LRELVPIVEE RRNIIPILGD ATKPEEYRAL VTKVDVIFED
160 170 180 190 200
VAQPTQAKIL IDNAKAYLKR GGYGMIAVKS RSIDVTKEPE QVFKEVEREL
210 220
SEYFEVIERL NLEPYEKDHA LFVVRKP
Length:227
Mass (Da):25,762
Last modified:June 1, 2002 - v1
Checksum:iA2190B2983FD6EF3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL80183.1.
RefSeqiNP_577788.1. NC_003413.1.
WP_011011171.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80183; AAL80183; PF0059.
GeneIDi1467888.
KEGGipfu:PF0059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL80183.1 .
RefSeqi NP_577788.1. NC_003413.1.
WP_011011171.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PRY X-ray 1.97 A 1-227 [» ]
2NNW X-ray 2.70 B/D 1-227 [» ]
3NMU X-ray 2.73 F/J 1-227 [» ]
3NVK X-ray 3.21 I/J 1-227 [» ]
3NVM X-ray 3.41 B 1-227 [» ]
4BY9 NMR - E/H/K/N 1-227 [» ]
ProteinModelPortali Q8U4M2.
SMRi Q8U4M2. Positions 1-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60606N.
STRINGi 186497.PF0059.

Proteomic databases

PRIDEi Q8U4M2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL80183 ; AAL80183 ; PF0059 .
GeneIDi 1467888.
KEGGi pfu:PF0059.

Phylogenomic databases

eggNOGi COG1889.
HOGENOMi HOG000106741.
KOi K04795.
OMAi WNPNKSK.

Miscellaneous databases

EvolutionaryTracei Q8U4M2.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_00351. RNA_methyltransf_FlpA.
InterProi IPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01269. Fibrillarin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006540. Nop17p. 1 hit.
PRINTSi PR00052. FIBRILLARIN.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00566. FIBRILLARIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Structure determination of fibrillarin from the hyperthermophilic archaeon Pyrococcus furiosus."
    Deng L., Starostina N.G., Liu Z.J., Rose J.P., Terns R.M., Terns M.P., Wang B.C.
    Biochem. Biophys. Res. Commun. 315:726-732(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS), SUBUNIT.
  3. "Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs."
    Oruganti S., Zhang Y., Li H., Robinson H., Terns M.P., Terns R.M., Yang W., Li H.
    J. Mol. Biol. 371:1141-1150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NOP5, SUBUNIT.
  4. "Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle."
    Xue S., Wang R., Yang F., Terns R.M., Terns M.P., Zhang X., Maxwell E.S., Li H.
    Mol. Cell 39:939-949(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE; RPL7AE; NOP5 AND RNA SUBSTRATE, SUBUNIT, FUNCTION.
  5. "The structure of the box C/D enzyme reveals regulation of RNA methylation."
    Lapinaite A., Simon B., Skjaerven L., Rakwalska-Bange M., Gabel F., Carlomagno T.
    Nature 502:519-523(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH RPL7AE; NOP5 AND RNA SUBSTRATE, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiFLPA_PYRFU
AccessioniPrimary (citable) accession number: Q8U4M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: June 1, 2002
Last modified: October 1, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3