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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

fib-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 + N(5)-methyl-L-glutamine-[histone].

GO - Molecular functioni

GO - Biological processi

  • positive regulation of translation Source: WormBase
  • rRNA processing Source: UniProtKB-KW
  • 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

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

  • Nucleusnucleolus By similarity

  • Note: Fibrillar region of the nucleolus.By similarity

GO - Cellular componenti

  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • nucleolus Source: WormBase
  • nucleoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352rRNA 2'-O-methyltransferase fibrillarinPRO_0000148511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Asymmetric dimethylarginineBy similarity
Modified residuei16 – 161Asymmetric dimethylarginineBy similarity
Modified residuei19 – 191Asymmetric dimethylarginineBy similarity
Modified residuei23 – 231Asymmetric dimethylarginineBy similarity
Modified residuei27 – 271Asymmetric dimethylarginineBy similarity
Modified residuei35 – 351Asymmetric dimethylarginineBy similarity
Modified residuei43 – 431Asymmetric dimethylarginineBy similarity
Modified residuei51 – 511Asymmetric dimethylarginineBy similarity
Modified residuei55 – 551Asymmetric dimethylarginineBy similarity
Modified residuei58 – 581Asymmetric dimethylarginineBy similarity
Modified residuei63 – 631Asymmetric dimethylarginineBy similarity
Modified residuei67 – 671Asymmetric dimethylarginineBy similarity
Modified residuei70 – 701Asymmetric dimethylarginineBy similarity
Modified residuei75 – 751Asymmetric dimethylarginineBy similarity
Modified residuei81 – 811Asymmetric dimethylarginineBy similarity
Modified residuei85 – 851Asymmetric dimethylarginineBy similarity
Modified residuei91 – 911Asymmetric dimethylarginineBy similarity
Modified residuei95 – 951Asymmetric dimethylarginineBy similarity
Modified residuei98 – 981Asymmetric dimethylarginineBy similarity
Modified residuei102 – 1021Asymmetric dimethylarginineBy similarity
Modified residuei105 – 1051Asymmetric dimethylarginineBy similarity
Modified residuei112 – 1121Asymmetric dimethylarginineBy similarity

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.

PTM databases

iPTMnetiQ22053.

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 interactions.
DIPiDIP-26332N.
MINTiMINT-1109493.
STRINGi6239.T01C3.7.1.

Structurei

3D structure databases

ProteinModelPortaliQ22053.
SMRiQ22053. Positions 118-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 2042S-adenosyl-L-methionine bindingBy similarity
Regioni222 – 2232S-adenosyl-L-methionine bindingBy similarity
Regioni247 – 2482S-adenosyl-L-methionine bindingBy similarity
Regioni267 – 2704S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 114107DMA/Gly-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
InParanoidiQ22053.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiQ22053.

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ22053.
SMRiQ22053. Positions 118-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44995. 2 interactions.
DIPiDIP-26332N.
MINTiMINT-1109493.
STRINGi6239.T01C3.7.1.

PTM databases

iPTMnetiQ22053.

Proteomic databases

EPDiQ22053.
PaxDbiQ22053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi179999.
WormBaseiT01C3.7; CE12920; WBGene00001423; fib-1.

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
InParanoidiQ22053.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiQ22053.

Miscellaneous databases

NextBioi907698.
PROiQ22053.

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

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiFBRL_CAEEL
AccessioniPrimary (citable) accession number: Q22053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.