RMT2_SCHPO
ID RMT2_SCHPO Reviewed; 357 AA.
AC Q10170; Q9Y7I7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein arginine N-methyltransferase 2 {ECO:0000250|UniProtKB:Q03305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q03305};
DE AltName: Full=Protein-arginine N5-methyltransferase {ECO:0000250|UniProtKB:Q03305};
DE AltName: Full=Type IV protein arginine N-methyltransferase {ECO:0000250|UniProtKB:Q03305};
DE Short=Type IV PRMT {ECO:0000250|UniProtKB:Q03305};
GN Name=rmt2 {ECO:0000250|UniProtKB:Q03305};
GN ORFNames=SPAC26A3.17c {ECO:0000312|PomBase:SPAC26A3.17c}, SPAC8E11.11;
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 [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that methylates the delta-nitrogen atom of arginine
CC residues to form N5-methylarginine (type IV) in target proteins.
CC Monomethylates ribosomal protein L12. {ECO:0000250|UniProtKB:Q03305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q03305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00892}.
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DR EMBL; CU329670; CAA93240.1; -; Genomic_DNA.
DR PIR; T38405; T38405.
DR RefSeq; NP_594160.2; NM_001019584.2.
DR AlphaFoldDB; Q10170; -.
DR SMR; Q10170; -.
DR BioGRID; 279139; 1.
DR IntAct; Q10170; 1.
DR STRING; 4896.SPAC26A3.17c.1; -.
DR MaxQB; Q10170; -.
DR PaxDb; Q10170; -.
DR PRIDE; Q10170; -.
DR EnsemblFungi; SPAC26A3.17c.1; SPAC26A3.17c.1:pep; SPAC26A3.17c.
DR GeneID; 2542686; -.
DR KEGG; spo:SPAC26A3.17c; -.
DR PomBase; SPAC26A3.17c; rmt2.
DR VEuPathDB; FungiDB:SPAC26A3.17c; -.
DR eggNOG; KOG1709; Eukaryota.
DR HOGENOM; CLU_033831_0_0_1; -.
DR InParanoid; Q10170; -.
DR OMA; YWVVDNY; -.
DR PhylomeDB; Q10170; -.
DR Reactome; R-SPO-71288; Creatine metabolism.
DR PRO; PR:Q10170; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019702; F:protein-arginine N5-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017408; Arginine_N-MeTrfase_2.
DR InterPro; IPR026480; RMT2_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF038148; Arginine_N-mtfrase-2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..357
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000116476"
FT DOMAIN 130..357
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 194..199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 215..217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 242..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ SEQUENCE 357 AA; 40709 MW; 5529B8D3B88D91A9 CRC64;
MDAPLVNESV EFQESQESLS LLEASKQLDL KKIQNLVDQG AVTSAIDIES GKNALHFIAS
YAEKETEVQA IEVTKWILSN GGVWNGIDRA NETPGCIARR RNLLRLYETI VDAGVRSELL
LSLLERKELT NEQLDTNEKY LQSALSYTQP TEDSSSLLDS DANAVMMSWE RKIMHRSAEI
IAPTKGRRVL NVGFGLGIID TFLQEKEPSL HVIIEPHPDV LKHMRKNGWM DRENVIVYET
TWENAINDIA SKYVFDGIYY DAFAESYEDL RNFFDSVVGL LDPETDSKFS FFNGLGADNQ
TFYDVYKKLV PIDLVSFGLQ CTYESMPVSS KDEEWKGAKR RYWDVSKYFL PIVTFDF
