ANM1_SCHPO
ID ANM1_SCHPO Reviewed; 340 AA.
AC Q9URX7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000303|PubMed:17213188};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P38074};
DE AltName: Full=Type I protein arginine N-methyltransferase {ECO:0000250|UniProtKB:P38074};
DE Short=Type I PRMT {ECO:0000250|UniProtKB:P38074};
GN Name=rmt1 {ECO:0000303|PubMed:17213188};
GN ORFNames=SPAC890.07c {ECO:0000312|PomBase:SPAC890.07c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=15175657; DOI=10.1038/sj.emboj.7600265;
RA Bachand F., Silver P.A.;
RT "PRMT3 is a ribosomal protein methyltransferase that affects the cellular
RT levels of ribosomal subunits.";
RL EMBO J. 23:2641-2650(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH PAB2.
RX PubMed=17213188; DOI=10.1074/jbc.m610512200;
RA Perreault A., Lemieux C., Bachand F.;
RT "Regulation of the nuclear poly(A)-binding protein by arginine methylation
RT in fission yeast.";
RL J. Biol. Chem. 282:7552-7562(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that catalyzes both the mono- and asymmetric (type I)
CC dimethylation of the guanidino nitrogens of arginine residues in target
CC proteins (By similarity). Asymmetrically dimethylates the
CC polyadenylate-binding protein pab2, modulating pab2 oligomerization
CC (PubMed:17213188). {ECO:0000250|UniProtKB:P38074,
CC ECO:0000269|PubMed:17213188}.
CC -!- SUBUNIT: Interacts with pab2. {ECO:0000269|PubMed:17213188}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15175657}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB63498.2; -; Genomic_DNA.
DR PIR; T50263; T50263.
DR RefSeq; NP_594825.2; NM_001020254.3.
DR AlphaFoldDB; Q9URX7; -.
DR SMR; Q9URX7; -.
DR BioGRID; 279912; 9.
DR STRING; 4896.SPAC890.07c.1; -.
DR iPTMnet; Q9URX7; -.
DR MaxQB; Q9URX7; -.
DR PaxDb; Q9URX7; -.
DR PRIDE; Q9URX7; -.
DR EnsemblFungi; SPAC890.07c.1; SPAC890.07c.1:pep; SPAC890.07c.
DR GeneID; 2543492; -.
DR KEGG; spo:SPAC890.07c; -.
DR PomBase; SPAC890.07c; rmt1.
DR VEuPathDB; FungiDB:SPAC890.07c; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q9URX7; -.
DR OMA; RNDFVHA; -.
DR PhylomeDB; Q9URX7; -.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q9URX7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IMP:PomBase.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..340
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000212337"
FT DOMAIN 16..311
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 128
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 137
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 29
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT MOD_RES 19
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 340 AA; 39019 MW; 7302B4988ED5E176 CRC64;
MPGNTKKSAD SGLTAKDYYF DSYSHWGIHE EMLKDDVRTL SYRDAIMQNP HLFRDKIVLD
VGCGTGILSM FCARAGAKHV YGVDMSEIIH KAVQIVEVNK LSDRITLIQG KMEEIQLPVE
KVDIIVSEWM GYFLLYESML DTVLVARDRY LAPDGLLFPD RAQIQLAAIE DADYKSEKIG
FWDDVYGFDF SPIKKDVWKE PLVDTVDRIA VNTNSCVILD LDLKTVKKED LAFSSPFEIT
ATRNDFVHAF LAWFDIEFSA CHKPIKFSTG PFSRYTHWKQ TVFYTHKDLT VKAGEYIRGT
ITCKPAEGNH RELDIDISYT FNPREPNREP VSEDLSYRMC
