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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 + N(5)-methyl-L-glutamine-[histone].

GO - Molecular functioni

GO - Biological processi

  • box C/D snoRNA 3'-end processing Source: GO_Central
  • cellular response to starvation Source: FlyBase
  • centrosome organization Source: FlyBase
  • histone glutamine methylation Source: GO_Central
  • RNA processing Source: UniProtKB
  • rRNA methylation Source: GO_Central
  • tRNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Ribonucleoprotein, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

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

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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003062. Fib.

Subcellular locationi

  • Nucleusnucleolus By similarity

  • Note: Fibrillar region of the nucleolus.By similarity

GO - Cellular componenti

  • box C/D snoRNP complex Source: GO_Central
  • Cajal body Source: FlyBase
  • dense fibrillar component Source: UniProtKB
  • nucleolus Source: FlyBase
  • small nuclear ribonucleoprotein complex Source: FlyBase
  • small nucleolar ribonucleoprotein complex Source: FlyBase
  • small-subunit processome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344rRNA 2'-O-methyltransferase fibrillarinPRO_0000148513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Asymmetric dimethylarginineBy similarity
Modified residuei23 – 231Asymmetric dimethylarginineBy similarity
Modified residuei25 – 251Asymmetric dimethylarginineBy similarity
Modified residuei40 – 401Asymmetric dimethylarginineBy similarity
Modified residuei42 – 421Asymmetric dimethylarginineBy similarity
Modified residuei48 – 481Asymmetric dimethylarginineBy similarity
Modified residuei51 – 511Asymmetric dimethylarginineCurated
Modified residuei58 – 581Asymmetric dimethylarginineCurated
Modified residuei63 – 631Asymmetric dimethylarginineCurated
Modified residuei71 – 711Asymmetric dimethylarginineCurated
Modified residuei77 – 771Asymmetric dimethylarginineCurated
Modified residuei83 – 831Asymmetric dimethylarginineCurated
Modified residuei88 – 881Asymmetric dimethylarginineCurated
Modified residuei93 – 931Asymmetric dimethylarginineCurated
Modified residuei98 – 981Asymmetric dimethylarginineCurated

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

BgeeiQ9W1V3.
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. 5 interactions.
IntActiQ9W1V3. 9 interactions.
MINTiMINT-307210.
STRINGi7227.FBpp0071892.

Structurei

3D structure databases

ProteinModelPortaliQ9W1V3.
SMRiQ9W1V3. Positions 113-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 1982S-adenosyl-L-methionine bindingBy similarity
Regioni216 – 2172S-adenosyl-L-methionine bindingBy similarity
Regioni241 – 2422S-adenosyl-L-methionine bindingBy similarity
Regioni261 – 2644S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 108100DMA/Gly-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
InParanoidiQ9W1V3.
KOiK14563.
OMAiPGVYIVI.
OrthoDBiEOG7KWSJP.
PhylomeDBiQ9W1V3.

Family and domain databases

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

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 CAA28903.1 differs from that shown. Reason: Frameshift at position 8. Curated
The sequence CAA28903.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 6713Missing in AAN71493 (PubMed:12537569).CuratedAdd
BLAST
Sequence conflicti134 – 1341R → G in AAN71493 (PubMed:12537569).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9W1V3.
SMRiQ9W1V3. Positions 113-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63268. 5 interactions.
IntActiQ9W1V3. 9 interactions.
MINTiMINT-307210.
STRINGi7227.FBpp0071892.

Proteomic databases

PaxDbiQ9W1V3.
PRIDEiQ9W1V3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi37662.
FlyBaseiFBgn0003062. Fib.

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
InParanoidiQ9W1V3.
KOiK14563.
OMAiPGVYIVI.
OrthoDBiEOG7KWSJP.
PhylomeDBiQ9W1V3.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSifbl. fly.
GenomeRNAii37662.
PROiQ9W1V3.

Gene expression databases

BgeeiQ9W1V3.
ExpressionAtlasiQ9W1V3. differential.
GenevisibleiQ9W1V3. DM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. "A novel GC-rich dispersed repeat sequence in Drosophila melanogaster."
    Flavell A.J., Dyson J., Ish-Horowicz D.
    Nucleic Acids Res. 15:4035-4048(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-140.

Entry informationi

Entry nameiFBRL_DROME
AccessioniPrimary (citable) accession number: Q9W1V3
Secondary accession number(s): Q24348, Q8IGK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [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

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.