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Protein

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

Gene

flpA

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: 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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

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:MJ0697
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485331 – 230Fibrillarin-like rRNA/tRNA 2'-O-methyltransferaseAdd BLAST230

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.UniRule annotation

Protein-protein interaction databases

IntActiQ58108. 2 interactors.
STRINGi243232.MJ_0697.

Structurei

Secondary structure

1230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Turni10 – 12Combined sources3
Beta strandi13 – 17Combined sources5
Beta strandi19 – 21Combined sources3
Beta strandi25 – 28Combined sources4
Beta strandi36 – 38Combined sources3
Beta strandi41 – 44Combined sources4
Beta strandi47 – 51Combined sources5
Turni54 – 56Combined sources3
Helixi58 – 64Combined sources7
Beta strandi77 – 82Combined sources6
Helixi87 – 95Combined sources9
Turni96 – 98Combined sources3
Beta strandi99 – 106Combined sources8
Helixi108 – 117Combined sources10
Turni118 – 120Combined sources3
Beta strandi124 – 128Combined sources5
Helixi134 – 137Combined sources4
Turni138 – 140Combined sources3
Beta strandi144 – 149Combined sources6
Helixi156 – 167Combined sources12
Beta strandi168 – 179Combined sources12
Helixi180 – 182Combined sources3
Beta strandi185 – 187Combined sources3
Helixi189 – 203Combined sources15
Beta strandi205 – 212Combined sources8
Turni214 – 216Combined sources3
Beta strandi220 – 227Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBNX-ray1.60A1-230[»]
1G8SX-ray1.60A1-230[»]
ProteinModelPortaliQ58108.
SMRiQ58108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58108.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 88S-adenosyl-L-methionine bindingUniRule annotation2
Regioni105 – 106S-adenosyl-L-methionine bindingUniRule annotation2
Regioni130 – 131S-adenosyl-L-methionine bindingUniRule annotation2
Regioni150 – 153S-adenosyl-L-methionine bindingUniRule annotation4

Sequence similaritiesi

Belongs to the methyltransferase superfamily. Fibrillarin family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00078. Archaea.
COG1889. LUCA.
InParanoidiQ58108.
KOiK04795.
OMAiEYREWNL.
PhylomeDBiQ58108.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA. 1 hit.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SMARTiSM01206. Fibrillarin. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDIKIKEIF ENIYEVDLGD GLKRIATKSI VKGKKVYDEK IIKIGDEEYR
60 70 80 90 100
IWNPNKSKLA AAIIKGLKVM PIKRDSKILY LGASAGTTPS HVADIADKGI
110 120 130 140 150
VYAIEYAPRI MRELLDACAE RENIIPILGD ANKPQEYANI VEKVDVIYED
160 170 180 190 200
VAQPNQAEIL IKNAKWFLKK GGYGMIAIKA RSIDVTKDPK EIFKEQKEIL
210 220 230
EAGGFKIVDE VDIEPFEKDH VMFVGIWEGK
Length:230
Mass (Da):25,966
Last modified:November 1, 1996 - v1
Checksum:i9ECAAD7C4C606756
GO

Mass spectrometryi

Molecular mass is 25971 Da from positions 1 - 230. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98690.1.
PIRiA64387.
RefSeqiWP_010870202.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98690; AAB98690; MJ_0697.
GeneIDi1451564.
KEGGimja:MJ_0697.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98690.1.
PIRiA64387.
RefSeqiWP_010870202.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBNX-ray1.60A1-230[»]
1G8SX-ray1.60A1-230[»]
ProteinModelPortaliQ58108.
SMRiQ58108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ58108. 2 interactors.
STRINGi243232.MJ_0697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98690; AAB98690; MJ_0697.
GeneIDi1451564.
KEGGimja:MJ_0697.

Phylogenomic databases

eggNOGiarCOG00078. Archaea.
COG1889. LUCA.
InParanoidiQ58108.
KOiK04795.
OMAiEYREWNL.
PhylomeDBiQ58108.

Miscellaneous databases

EvolutionaryTraceiQ58108.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA. 1 hit.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SMARTiSM01206. Fibrillarin. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFLPA_METJA
AccessioniPrimary (citable) accession number: Q58108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 108 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.