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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

Fib

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. 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. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N5-methyl-L-glutamine-[histone].

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Ribonucleoprotein, RNA-binding, Transferase
Biological processrRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-DME-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA 2'-O-methyltransferase fibrillarin (EC:2.1.1.-)
Alternative name(s):
Histone-glutamine methyltransferase
Gene namesi
Name:FibImported
ORF Names:CG9888
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003062. Fib.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485131 – 344rRNA 2'-O-methyltransferase fibrillarinAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Asymmetric dimethylarginineBy similarity1
Modified residuei23Asymmetric dimethylarginineBy similarity1
Modified residuei25Asymmetric dimethylarginineBy similarity1
Modified residuei40Asymmetric dimethylarginineBy similarity1
Modified residuei42Asymmetric dimethylarginineBy similarity1
Modified residuei48Asymmetric dimethylarginineBy similarity1
Modified residuei51Asymmetric dimethylarginineBy similarity1
Modified residuei58Asymmetric dimethylarginineBy similarity1
Modified residuei63Asymmetric dimethylarginineBy similarity1
Modified residuei71Asymmetric dimethylarginineBy similarity1
Modified residuei77Asymmetric dimethylarginineBy similarity1
Modified residuei83Asymmetric dimethylarginineBy similarity1
Modified residuei88Asymmetric dimethylarginineBy similarity1
Modified residuei93Asymmetric dimethylarginineBy similarity1
Modified residuei98Asymmetric dimethylarginineBy similarity1

Post-translational modificationi

By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).By similarity

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiQ9W1V3.
PRIDEiQ9W1V3.

Expressioni

Gene expression databases

BgeeiFBgn0003062.
ExpressionAtlasiQ9W1V3. differential.
GenevisibleiQ9W1V3. DM.

Interactioni

Subunit structurei

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. It is associated with the U3, U8 and U13 small nuclear RNAs.By similarity

Protein-protein interaction databases

BioGridi63268. 15 interactors.
IntActiQ9W1V3. 9 interactors.
MINTiMINT-307210.
STRINGi7227.FBpp0071892.

Structurei

3D structure databases

ProteinModelPortaliQ9W1V3.
SMRiQ9W1V3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 198S-adenosyl-L-methionine bindingBy similarity2
Regioni216 – 217S-adenosyl-L-methionine bindingBy similarity2
Regioni241 – 242S-adenosyl-L-methionine bindingBy similarity2
Regioni261 – 264S-adenosyl-L-methionine bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 108DMA/Gly-richAdd BLAST100

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
InParanoidiQ9W1V3.
KOiK14563.
OMAiQPNQAEI.
OrthoDBiEOG091G0GV0.
PhylomeDBiQ9W1V3.

Family and domain databases

HAMAPiMF_00351. RNA_methyltransf_FlpA. 1 hit.
InterProiView protein in InterPro
IPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases.
PfamiView protein in Pfam
PF01269. Fibrillarin. 1 hit.
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SMARTiView protein in SMART
SM01206. Fibrillarin. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiView protein in PROSITE
PS00566. FIBRILLARIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9W1V3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKPGFSPRG GGGGGGGGGG GFRGRGGGGG GGGGGFGGGR GRGGGGDRGG
60 70 80 90 100
RGGFGGGRGG GGRGGGGGGG RGAFGGRGGG GGRGGGGRGG GGRGGGGRGG
110 120 130 140 150
GAGGFKGGKT VTIEPHRHEG VFIARGKEDA LVTRNFVPGS EVYGEKRISV
160 170 180 190 200
ETNGEKIEYR VWNPFRSKLA AAVLGGVEQI HMPPGSKVLY LGAASGTTVS
210 220 230 240 250
HVSDVVGPEG LVYAVEFSHR SGRDLINVAK KRTNIIPIIE DARHPHKYRM
260 270 280 290 300
LVGMVDTIFA DVAQPDQGRI VALNAQHFLK NGGHFVISIK ASCIDSTAQP
310 320 330 340
EAVFAAEVKK MQADKLKPQE QLTLEPYERD HAVVVGVYRP PPKQ
Length:344
Mass (Da):34,637
Last modified:May 1, 2000 - v1
Checksum:i58B536FAACAE01D6
GO

Sequence cautioni

The sequence CAA28903 differs from that shown. Reason: Frameshift at position 8.Curated
The sequence CAA28903 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55 – 67Missing in AAN71493 (PubMed:12537569).CuratedAdd BLAST13
Sequence conflicti134R → G in AAN71493 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46950.1.
BT001738 mRNA. Translation: AAN71493.1.
X05285 Genomic DNA. Translation: CAA28903.1. Sequence problems.
RefSeqiNP_523817.1. NM_079093.4.
UniGeneiDm.2821.

Genome annotation databases

EnsemblMetazoaiFBtr0071982; FBpp0071892; FBgn0003062.
GeneIDi37662.
KEGGidme:Dmel_CG9888.
UCSCiCG9888-RA. d. melanogaster.

Similar proteinsi

Entry informationi

Entry nameiFBRL_DROME
AccessioniPrimary (citable) accession number: Q9W1V3
Secondary accession number(s): Q24348, Q8IGK5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: May 1, 2000
Last modified: November 22, 2017
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families