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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

NOP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:1825809). 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. Involved in the biogenesis of the 18S rRNA. 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 (PubMed:24352239).3 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N5-methyl-L-glutamine-[histone].1 Publication

GO - Molecular functioni

  • histone-glutamine methyltransferase activity Source: UniProtKB
  • O-methyltransferase activity Source: Reactome
  • RNA binding Source: GO_Central
  • rRNA methyltransferase activity Source: SGD

GO - Biological processi

  • box C/D snoRNA 3'-end processing Source: SGD
  • histone glutamine methylation Source: SGD
  • regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  • rRNA 2'-O-methylation Source: Reactome
  • rRNA methylation Source: SGD
  • rRNA processing Source: SGD
  • snoRNA processing Source: SGD
  • tRNA processing Source: InterPro

Keywordsi

Molecular functionMethyltransferase, Ribonucleoprotein, RNA-binding, Transferase
Biological processRibosome biogenesis, rRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29444-MONOMER.
ReactomeiR-SCE-6790901. rRNA modification in the nucleus and cytosol.
R-SCE-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
U3 small nucleolar RNA-associated protein NOP1
Short name:
Nucleolar protein 1
Short name:
U3 snoRNA-associated protein NOP1
Gene namesi
Name:NOP1
Synonyms:LOT3
Ordered Locus Names:YDL014W
ORF Names:D2870
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL014W.
SGDiS000002172. NOP1.

Subcellular locationi

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87V → D in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with G-103; V-175 and S-219. 1 Publication1
Mutagenesisi103E → G in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; V-175 and S-219. 1 Publication1
Mutagenesisi175A → V in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; G-103 and S-219. 1 Publication1
Mutagenesisi219P → S in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; G-103 and V-175. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485271 – 327rRNA 2'-O-methyltransferase fibrillarinAdd BLAST327

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei16Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei22Omega-N-methylarginine; by HMT11 Publication1 Publication1
Modified residuei30Asymmetric dimethylarginine; by HMT11 Publication1 Publication1
Modified residuei34Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei34Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei40Omega-N-methylarginine; by HMT11 Publication1 Publication1
Modified residuei48Asymmetric dimethylarginine; by HMT11 Publication1 Publication1
Modified residuei52Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei52Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei58Omega-N-methylarginine; by HMT11 Publication1 Publication1
Modified residuei70Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei70Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei73Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei73Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei81Asymmetric dimethylarginine; by HMT1; alternate1 Publication1 Publication1
Modified residuei81Omega-N-methylarginine; by HMT1; alternate1 Publication1 Publication1
Cross-linki150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

Methylated by HMT1, forming asymmetric dimethylarginines (DMA) within a domain referred to as an RGG box, made up of repeated Gly-Gly dipeptides interspersed with Arg and aromatic residues.1 Publication

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

MaxQBiP15646.
PRIDEiP15646.

PTM databases

iPTMnetiP15646.

Interactioni

Subunit structurei

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus a guide RNA. Interacts with snoRNA U3. Interacts with MPP10, NOP58, SIK1 and SOF1. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi32040. 356 interactors.
DIPiDIP-698N.
IntActiP15646. 128 interactors.
MINTiMINT-382637.
STRINGi4932.YDL014W.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WYJelectron microscopy8.703B/3C1-327[»]
5WYKelectron microscopy4.503B/3C1-327[»]
ProteinModelPortaliP15646.
SMRiP15646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 83RGG-boxAdd BLAST76
Regioni22 – 42RNA-binding RGG-boxBy similarityAdd BLAST21
Regioni58 – 75RNA-binding RGG-boxBy similarityAdd BLAST18
Regioni179 – 180S-adenosyl-L-methionine bindingBy similarity2
Regioni198 – 199S-adenosyl-L-methionine bindingBy similarity2
Regioni223 – 224S-adenosyl-L-methionine bindingBy similarity2
Regioni243 – 246S-adenosyl-L-methionine bindingBy similarity4
Regioni281 – 313HelicalSequence analysisAdd BLAST33

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi6 – 83DMA/Gly-richAdd BLAST78

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
KOiK14563.
OMAiQPNQAEI.
OrthoDBiEOG092C4CCH.

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.

P15646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRPGSRGG SRGGSRGGFG GRGGSRGGAR GGSRGGFGGR GGSRGGARGG
60 70 80 90 100
SRGGFGGRGG SRGGARGGSR GGRGGAAGGA RGGAKVVIEP HRHAGVYIAR
110 120 130 140 150
GKEDLLVTKN MAPGESVYGE KRISVEEPSK EDGVPPTKVE YRVWNPFRSK
160 170 180 190 200
LAAGIMGGLD ELFIAPGKKV LYLGAASGTS VSHVSDVVGP EGVVYAVEFS
210 220 230 240 250
HRPGRELISM AKKRPNIIPI IEDARHPQKY RMLIGMVDCV FADVAQPDQA
260 270 280 290 300
RIIALNSHMF LKDQGGVVIS IKANCIDSTV DAETVFAREV QKLREERIKP
310 320
LEQLTLEPYE RDHCIVVGRY MRSGLKK
Length:327
Mass (Da):34,465
Last modified:April 1, 1990 - v1
Checksum:i56A8B958A7B6066E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05230 Genomic DNA. Translation: AAA34816.1.
Z48432 Genomic DNA. Translation: CAA88345.1.
Z74061 Genomic DNA. Translation: CAA98571.1.
Z74062 Genomic DNA. Translation: CAA98572.1.
BK006938 Genomic DNA. Translation: DAA11835.1.
PIRiS25421.
RefSeqiNP_010270.1. NM_001180073.1.

Genome annotation databases

EnsemblFungiiYDL014W; YDL014W; YDL014W.
GeneIDi851548.
KEGGisce:YDL014W.

Similar proteinsi

Entry informationi

Entry nameiFBRL_YEAST
AccessioniPrimary (citable) accession number: P15646
Secondary accession number(s): D6VRX5, P89890
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 27, 2017
This is version 168 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names