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Q756P0 (FBRL_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
rRNA 2'-O-methyltransferase fibrillarin

EC=2.1.1.-
Alternative name(s):
Histone-glutamine methyltransferase
Gene names
Name:NOP1
Ordered Locus Names:AER214C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00351

Catalytic activity

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone]. HAMAP-Rule MF_00351

Subunit structure

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus a guide RNA By similarity.

Subcellular location

Nucleusnucleolus By similarity. Note: Fibrillar region of the nucleolus By similarity. HAMAP-Rule MF_00351

Post-translational modification

By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA) By similarity. HAMAP-Rule MF_00351

Sequence similarities

Belongs to the methyltransferase superfamily. Fibrillarin family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Ribonucleoprotein
Transferase
   PTMMethylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326rRNA 2'-O-methyltransferase fibrillarin HAMAP-Rule MF_00351
PRO_0000148521

Regions

Region180 – 1812S-adenosyl-L-methionine binding By similarity
Region199 – 2002S-adenosyl-L-methionine binding By similarity
Region224 – 2252S-adenosyl-L-methionine binding By similarity
Region244 – 2474S-adenosyl-L-methionine binding By similarity
Compositional bias6 – 8479DMA/Gly-rich HAMAP-Rule MF_00351

Amino acid modifications

Modified residue81Asymmetric dimethylarginine By similarity
Modified residue111Asymmetric dimethylarginine By similarity
Modified residue151Asymmetric dimethylarginine By similarity
Modified residue191Asymmetric dimethylarginine By similarity
Modified residue231Asymmetric dimethylarginine By similarity
Modified residue261Asymmetric dimethylarginine By similarity
Modified residue321Asymmetric dimethylarginine By similarity
Modified residue361Asymmetric dimethylarginine By similarity
Modified residue391Asymmetric dimethylarginine By similarity
Modified residue451Asymmetric dimethylarginine By similarity
Modified residue491Asymmetric dimethylarginine By similarity
Modified residue551Asymmetric dimethylarginine By similarity
Modified residue591Asymmetric dimethylarginine By similarity
Modified residue631Asymmetric dimethylarginine By similarity
Modified residue671Asymmetric dimethylarginine By similarity
Modified residue711Asymmetric dimethylarginine By similarity
Modified residue741Asymmetric dimethylarginine By similarity
Modified residue781Asymmetric dimethylarginine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q756P0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 57B6385C6257ED00

FASTA32634,213
        10         20         30         40         50         60 
MAFQPGSRGG RGGARGGARG GARGGRGGFG GRGGSRGGRG GFDSRGGARG GFGGRGGSRG 

        70         80         90        100        110        120 
GPRGGPRGGA RGGRGGARGG AKGGAKVVIE PHKHAGVFIA RGKEDLLVTK NVAPGESVYG 

       130        140        150        160        170        180 
EKRISVEEPA SEEGVPPTKV EYRVWNPFRS KLAAGIMGGL DELFIAPGKK VLYLGAASGT 

       190        200        210        220        230        240 
SVSHVADVVG PEGLVYAVEF SHRPGRELIS MAKKRPNVIP IIEDARHPQK YRMLIGMVDA 

       250        260        270        280        290        300 
VFADVAQPDQ ARIIALNSHM FLKDQGGVVI SIKANCIDST VDAETVFARE VQKLREEKIK 

       310        320 
PLEQLTLEPY ERDHCIVIGR YMRSGL 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016818 Genomic DNA. Translation: AAS52895.1.
RefSeqNP_985071.1. NM_210425.1.

3D structure databases

ProteinModelPortalQ756P0.
SMRQ756P0. Positions 88-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AER214C.

Proteomic databases

PRIDEQ756P0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS52895; AAS52895; AGOS_AER214C.
GeneID4621281.
KEGGago:AGOS_AER214C.

Phylogenomic databases

eggNOGCOG1889.
HOGENOMHOG000106741.
KOK14563.
OMAGEAKIEY.
OrthoDBEOG7FNCK0.
PhylomeDBQ756P0.

Family and domain databases

HAMAPMF_00351. RNA_methyltransf_FlpA.
InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
[Graphical view]
PANTHERPTHR10335. PTHR10335. 1 hit.
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFBRL_ASHGO
AccessionPrimary (citable) accession number: Q756P0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families