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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

fib-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

  • box C/D snoRNA 3'-end processing Source: GO_Central
  • histone glutamine methylation Source: GO_Central
  • positive regulation of translation Source: WormBase
  • rRNA methylation Source: GO_Central

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA 2'-O-methyltransferase fibrillarin (EC:2.1.1.-)
Alternative name(s):
Histone-glutamine methyltransferase
Gene namesi
Name:fib-1
ORF Names:T01C3.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiT01C3.7 ; CE12920 ; WBGene00001423 ; fib-1

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_00001485111 – 352rRNA 2'-O-methyltransferase fibrillarinAdd BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8Asymmetric dimethylarginineBy similarity1
Modified residuei16Asymmetric dimethylarginineBy similarity1
Modified residuei19Asymmetric dimethylarginineBy similarity1
Modified residuei23Asymmetric dimethylarginineBy similarity1
Modified residuei27Asymmetric dimethylarginineBy similarity1
Modified residuei35Asymmetric dimethylarginineBy similarity1
Modified residuei43Asymmetric dimethylarginineBy similarity1
Modified residuei51Asymmetric dimethylarginineBy similarity1
Modified residuei55Asymmetric dimethylarginineBy similarity1
Modified residuei58Asymmetric dimethylarginineBy similarity1
Modified residuei63Asymmetric dimethylarginineBy similarity1
Modified residuei67Asymmetric dimethylarginineBy similarity1
Modified residuei70Asymmetric dimethylarginineBy similarity1
Modified residuei75Asymmetric dimethylarginineBy similarity1
Modified residuei81Asymmetric dimethylarginineBy similarity1
Modified residuei85Asymmetric dimethylarginineBy similarity1
Modified residuei91Asymmetric dimethylarginineBy similarity1
Modified residuei95Asymmetric dimethylarginineBy similarity1
Modified residuei98Asymmetric dimethylarginineBy similarity1
Modified residuei102Asymmetric dimethylarginineBy similarity1
Modified residuei105Asymmetric dimethylarginineBy similarity1
Modified residuei112Asymmetric 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

EPDiQ22053
PaxDbiQ22053
PeptideAtlasiQ22053
PRIDEiQ22053

PTM databases

iPTMnetiQ22053

Expressioni

Gene expression databases

BgeeiWBGene00001423

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

BioGridi44995, 2 interactors
DIPiDIP-26332N
STRINGi6239.T01C3.7.1

Structurei

3D structure databases

ProteinModelPortaliQ22053
SMRiQ22053
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni203 – 204S-adenosyl-L-methionine bindingBy similarity2
Regioni222 – 223S-adenosyl-L-methionine bindingBy similarity2
Regioni247 – 248S-adenosyl-L-methionine bindingBy similarity2
Regioni267 – 270S-adenosyl-L-methionine bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi8 – 114DMA/Gly-richAdd BLAST107

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596 Eukaryota
COG1889 LUCA
GeneTreeiENSGT00550000074792
HOGENOMiHOG000106741
InParanoidiQ22053
KOiK14563
OMAiQPNQAEI
OrthoDBiEOG091G0GV0
PhylomeDBiQ22053

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.

Q22053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRPEFNRGG GGGGFRGGRG GDRGGSRGGF GGGGRGGYGG GDRGSFGGGD
60 70 80 90 100
RGGFRGGRGG GDRGGFRGGR GGGDRGGFGG RGSPRGGFGG RGSPRGGRGS
110 120 130 140 150
PRGGRGGAGG MRGGKTVVVE PHRLGGVFIV KGKEDALATK NMVVGESVYG
160 170 180 190 200
EKRVSVDDGA GSIEYRVWNP FRSKLAASIM GGLENTHIKP GTKLLYLGAA
210 220 230 240 250
SGTTVSHCSD VVGPEGIVYA VEFSHRSGRD LLGVAKKRPN VVPIVEDARH
260 270 280 290 300
PHKYRMLVGM VDVIFSDVAQ PDQARIVALN AQNFLRNGGH AVISIKANCI
310 320 330 340 350
DSTAEPEAVF AGEVNKLKEE KFKPLEQVTL EPYERDHAVV VAVYRPVKGK

KV
Length:352
Mass (Da):36,383
Last modified:November 1, 1996 - v1
Checksum:i52FDE6555DBCB717
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z78413 Genomic DNA Translation: CAB01657.1
PIRiT24279
RefSeqiNP_506691.1, NM_074290.4
UniGeneiCel.23500

Genome annotation databases

EnsemblMetazoaiT01C3.7.1; T01C3.7.1; WBGene00001423
T01C3.7.2; T01C3.7.2; WBGene00001423
GeneIDi179999
KEGGicel:CELE_T01C3.7
UCSCiT01C3.7.1 c. elegans

Similar proteinsi

Entry informationi

Entry nameiFBRL_CAEEL
AccessioniPrimary (citable) accession number: Q22053
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health