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Protein

Protein arginine N-methyltransferase 1

Gene

rmt1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in target proteins (By similarity). Asymmetrically dimethylates the polyadenylate-binding protein pab2, modulating pab2 oligomerization (PubMed:17213188).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291S-adenosyl-L-methionineBy similarity
Binding sitei38 – 381S-adenosyl-L-methionineBy similarity
Binding sitei62 – 621S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei84 – 841S-adenosyl-L-methionineBy similarity
Binding sitei113 – 1131S-adenosyl-L-methionineBy similarity
Active sitei128 – 1281By similarity
Active sitei137 – 1371By similarity

GO - Molecular functioni

  • protein-arginine N-methyltransferase activity Source: PomBase

GO - Biological processi

  • mRNA export from nucleus Source: PomBase
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-SPO-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 11 Publication (EC:2.1.1.-By similarity)
Alternative name(s):
Type I protein arginine N-methyltransferaseBy similarity
Short name:
Type I PRMTBy similarity
Gene namesi
Name:rmt11 Publication
ORF Names:SPAC890.07cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC890.07c.
PomBaseiSPAC890.07c. rmt1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Protein arginine N-methyltransferase 1PRO_0000212337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphotyrosine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9URX7.

PTM databases

iPTMnetiQ9URX7.

Interactioni

Subunit structurei

Interacts with pab2.1 Publication

Protein-protein interaction databases

BioGridi279912. 1 interaction.
MINTiMINT-4707185.

Structurei

3D structure databases

ProteinModelPortaliQ9URX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 311296SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000198521.
InParanoidiQ9URX7.
KOiK11434.
OMAiAIMQNPH.
OrthoDBiEOG7WDNBC.
PhylomeDBiQ9URX7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9URX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGNTKKSAD SGLTAKDYYF DSYSHWGIHE EMLKDDVRTL SYRDAIMQNP
60 70 80 90 100
HLFRDKIVLD VGCGTGILSM FCARAGAKHV YGVDMSEIIH KAVQIVEVNK
110 120 130 140 150
LSDRITLIQG KMEEIQLPVE KVDIIVSEWM GYFLLYESML DTVLVARDRY
160 170 180 190 200
LAPDGLLFPD RAQIQLAAIE DADYKSEKIG FWDDVYGFDF SPIKKDVWKE
210 220 230 240 250
PLVDTVDRIA VNTNSCVILD LDLKTVKKED LAFSSPFEIT ATRNDFVHAF
260 270 280 290 300
LAWFDIEFSA CHKPIKFSTG PFSRYTHWKQ TVFYTHKDLT VKAGEYIRGT
310 320 330 340
ITCKPAEGNH RELDIDISYT FNPREPNREP VSEDLSYRMC
Length:340
Mass (Da):39,019
Last modified:September 22, 2009 - v2
Checksum:i7302B4988ED5E176
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB63498.2.
PIRiT50263.
RefSeqiNP_594825.2. NM_001020254.3.

Genome annotation databases

EnsemblFungiiSPAC890.07c.1; SPAC890.07c.1:pep; SPAC890.07c.
GeneIDi2543492.
KEGGispo:SPAC890.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB63498.2.
PIRiT50263.
RefSeqiNP_594825.2. NM_001020254.3.

3D structure databases

ProteinModelPortaliQ9URX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279912. 1 interaction.
MINTiMINT-4707185.

PTM databases

iPTMnetiQ9URX7.

Proteomic databases

MaxQBiQ9URX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC890.07c.1; SPAC890.07c.1:pep; SPAC890.07c.
GeneIDi2543492.
KEGGispo:SPAC890.07c.

Organism-specific databases

EuPathDBiFungiDB:SPAC890.07c.
PomBaseiSPAC890.07c. rmt1.

Phylogenomic databases

HOGENOMiHOG000198521.
InParanoidiQ9URX7.
KOiK11434.
OMAiAIMQNPH.
OrthoDBiEOG7WDNBC.
PhylomeDBiQ9URX7.

Enzyme and pathway databases

ReactomeiR-SPO-3214858. RMTs methylate histone arginines.

Miscellaneous databases

PROiQ9URX7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits."
    Bachand F., Silver P.A.
    EMBO J. 23:2641-2650(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast."
    Perreault A., Lemieux C., Bachand F.
    J. Biol. Chem. 282:7552-7562(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAB2.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiANM1_SCHPO
AccessioniPrimary (citable) accession number: Q9URX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.