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rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase) (U3 small nucleolar RNA-associated protein NOP1) (Nucleolar protein 1) (U3 snoRNA-associated protein NOP1)

 FBRL_YEAST              Reviewed;         327 AA.
P15646; D6VRX5; P89890;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 169.
RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
EC=2.1.1.-;
AltName: Full=Histone-glutamine methyltransferase;
AltName: Full=U3 small nucleolar RNA-associated protein NOP1;
Short=Nucleolar protein 1;
Short=U3 snoRNA-associated protein NOP1;
Name=NOP1; Synonyms=LOT3; OrderedLocusNames=YDL014W; ORFNames=D2870;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 264-270 AND
298-310, FUNCTION, INTERACTION WITH SNORNAS, AND SUBCELLULAR LOCATION.
PubMed=2686980;
Schimmang T., Tollervey D., Kern H., Frank R., Hurt E.C.;
"A yeast nucleolar protein related to mammalian fibrillarin is
associated with small nucleolar RNA and is essential for viability.";
EMBO J. 8:4015-4024(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 112-142;
157-181 AND 211-231, AND SUBCELLULAR LOCATION.
PubMed=2298745;
Henriquez R., Blobel G., Aris J.P.;
"Isolation and sequencing of NOP1. A yeast gene encoding a nucleolar
protein homologous to a human autoimmune antigen.";
J. Biol. Chem. 265:2209-2215(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=1825809;
Tollervey D., Lehtonen H., Carmo-Fonseca M., Hurt E.C.;
"The small nucleolar RNP protein NOP1 (fibrillarin) is required for
pre-rRNA processing in yeast.";
EMBO J. 10:573-583(1991).
[6]
INTERACTION WITH SOF1.
PubMed=8508778;
Jansen R., Tollervey D., Hurt E.C.;
"A U3 snoRNP protein with homology to splicing factor PRP4 and G beta
domains is required for ribosomal RNA processing.";
EMBO J. 12:2549-2558(1993).
[7]
INTERACTION WITH SIK1 AND NOP58.
PubMed=9372940; DOI=10.1128/MCB.17.12.7088;
Gautier T., Berges T., Tollervey D., Hurt E.;
"Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p
and are required for ribosome biogenesis.";
Mol. Cell. Biol. 17:7088-7098(1997).
[8]
INTERACTION WITH MPP10 AND SNORNA U3, AND IDENTIFICATION IN SSU
PROCESSOME BY MASS SPECTROMETRY.
PubMed=12068309; DOI=10.1038/nature00769;
Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E.,
Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
"A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
biogenesis.";
Nature 417:967-970(2002).
[9]
SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
PubMed=12756332; DOI=10.1261/rna.5020803;
Xu C., Henry P.A., Setya A., Henry M.F.;
"In vivo analysis of nucleolar proteins modified by the yeast arginine
methyltransferase Hmt1/Rmt1p.";
RNA 9:746-759(2003).
[10]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[11]
METHYLATION AT ARG-16; ARG-22; ARG-30; ARG-34; ARG-40; ARG-48; ARG-52;
ARG-58; ARG-70; ARG-73 AND ARG-81.
PubMed=23865587; DOI=10.1021/pr400556c;
Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
"Analysis of the proteome of Saccharomyces cerevisiae for
methylarginine.";
J. Proteome Res. 12:3884-3899(2013).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-87; GLU-103;
ALA-175 AND PRO-219.
PubMed=24352239; DOI=10.1038/nature12819;
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B.,
Nelson C.J., Nielsen M.L., Kouzarides T.;
"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
modification.";
Nature 505:564-568(2014).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:1825809, ECO:0000269|PubMed:24352239,
ECO:0000269|PubMed:2686980}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-glutamine-
[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-
[histone]. {ECO:0000269|PubMed:24352239}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:12068309,
ECO:0000269|PubMed:2686980, ECO:0000269|PubMed:8508778,
ECO:0000269|PubMed:9372940}.
-!- INTERACTION:
P38333:ENP1; NbExp=4; IntAct=EBI-6838, EBI-6482;
Q12460:NOP56; NbExp=3; IntAct=EBI-6838, EBI-17148;
Q12499:NOP58; NbExp=4; IntAct=EBI-6838, EBI-12126;
P39990:SNU13; NbExp=4; IntAct=EBI-6838, EBI-12032;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12756332, ECO:0000269|PubMed:2298745,
ECO:0000269|PubMed:2686980}. Note=Fibrillar region of the
nucleolus.
-!- PTM: 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. {ECO:0000269|PubMed:12756332}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily.
Fibrillarin family. {ECO:0000305}.
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EMBL; J05230; AAA34816.1; -; Genomic_DNA.
EMBL; Z48432; CAA88345.1; -; Genomic_DNA.
EMBL; Z74061; CAA98571.1; -; Genomic_DNA.
EMBL; Z74062; CAA98572.1; -; Genomic_DNA.
EMBL; BK006938; DAA11835.1; -; Genomic_DNA.
PIR; S25421; S25421.
RefSeq; NP_010270.1; NM_001180073.1.
PDB; 5WYJ; EM; 8.70 A; 3B/3C=1-327.
PDB; 5WYK; EM; 4.50 A; 3B/3C=1-327.
PDBsum; 5WYJ; -.
PDBsum; 5WYK; -.
ProteinModelPortal; P15646; -.
SMR; P15646; -.
BioGrid; 32040; 356.
DIP; DIP-698N; -.
IntAct; P15646; 65.
MINT; MINT-382637; -.
STRING; 4932.YDL014W; -.
iPTMnet; P15646; -.
MaxQB; P15646; -.
PRIDE; P15646; -.
EnsemblFungi; YDL014W; YDL014W; YDL014W.
GeneID; 851548; -.
KEGG; sce:YDL014W; -.
EuPathDB; FungiDB:YDL014W; -.
SGD; S000002172; NOP1.
GeneTree; ENSGT00550000074792; -.
HOGENOM; HOG000106741; -.
KO; K14563; -.
OMA; QPNQAEI; -.
OrthoDB; EOG092C4CCH; -.
BioCyc; YEAST:G3O-29444-MONOMER; -.
Reactome; R-SCE-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:P15646; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0031428; C:box C/D snoRNP complex; IDA:SGD.
GO; GO:0015030; C:Cajal body; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0032040; C:small-subunit processome; IDA:SGD.
GO; GO:1990259; F:histone-glutamine methyltransferase activity; IDA:UniProtKB.
GO; GO:0008171; F:O-methyltransferase activity; EXP:Reactome.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0008649; F:rRNA methyltransferase activity; IDA:SGD.
GO; GO:0000494; P:box C/D snoRNA 3'-end processing; IMP:SGD.
GO; GO:1990258; P:histone glutamine methylation; IDA:SGD.
GO; GO:0006356; P:regulation of transcription from RNA polymerase I promoter; IDA:UniProtKB.
GO; GO:0000451; P:rRNA 2'-O-methylation; TAS:Reactome.
GO; GO:0031167; P:rRNA methylation; IDA:SGD.
GO; GO:0006364; P:rRNA processing; IMP:SGD.
GO; GO:0043144; P:snoRNA processing; IMP:SGD.
GO; GO:0008033; P:tRNA processing; IEA:InterPro.
HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
InterPro; IPR000692; Fibrillarin.
InterPro; IPR020813; Fibrillarin_CS.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01269; Fibrillarin; 1.
PIRSF; PIRSF006540; Nop17p; 1.
PRINTS; PR00052; FIBRILLARIN.
SMART; SM01206; Fibrillarin; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS00566; FIBRILLARIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Isopeptide bond; Methylation; Methyltransferase; Nucleus;
Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase;
Ubl conjugation.
CHAIN 1 327 rRNA 2'-O-methyltransferase fibrillarin.
/FTId=PRO_0000148527.
REGION 8 83 RGG-box.
REGION 22 42 RNA-binding RGG-box. {ECO:0000250}.
REGION 58 75 RNA-binding RGG-box. {ECO:0000250}.
REGION 179 180 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 198 199 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 223 224 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 243 246 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 281 313 Helical. {ECO:0000255}.
COMPBIAS 6 83 DMA/Gly-rich.
MOD_RES 16 16 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 16 16 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 22 22 Omega-N-methylarginine; by HMT1.
{ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 30 30 Asymmetric dimethylarginine; by HMT1.
{ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 34 34 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 34 34 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 40 40 Omega-N-methylarginine; by HMT1.
{ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 48 48 Asymmetric dimethylarginine; by HMT1.
{ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 52 52 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 52 52 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 58 58 Omega-N-methylarginine; by HMT1.
{ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 70 70 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 70 70 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 73 73 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 73 73 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 81 81 Asymmetric dimethylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
MOD_RES 81 81 Omega-N-methylarginine; by HMT1;
alternate. {ECO:0000269|PubMed:23865587,
ECO:0000305|PubMed:12756332}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 87 87 V->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.
{ECO:0000269|PubMed:24352239}.
MUTAGEN 103 103 E->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.
{ECO:0000269|PubMed:24352239}.
MUTAGEN 175 175 A->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.
{ECO:0000269|PubMed:24352239}.
MUTAGEN 219 219 P->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.
{ECO:0000269|PubMed:24352239}.
SEQUENCE 327 AA; 34465 MW; 56A8B958A7B6066E CRC64;
MSFRPGSRGG SRGGSRGGFG GRGGSRGGAR GGSRGGFGGR GGSRGGARGG SRGGFGGRGG
SRGGARGGSR GGRGGAAGGA RGGAKVVIEP HRHAGVYIAR GKEDLLVTKN MAPGESVYGE
KRISVEEPSK EDGVPPTKVE YRVWNPFRSK LAAGIMGGLD ELFIAPGKKV LYLGAASGTS
VSHVSDVVGP EGVVYAVEFS HRPGRELISM AKKRPNIIPI IEDARHPQKY RMLIGMVDCV
FADVAQPDQA RIIALNSHMF LKDQGGVVIS IKANCIDSTV DAETVFAREV QKLREERIKP
LEQLTLEPYE RDHCIVVGRY MRSGLKK


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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