RMT2_NEUCR
ID RMT2_NEUCR Reviewed; 429 AA.
AC Q7SCW9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein arginine N-methyltransferase 2 {ECO:0000250|UniProtKB:Q03305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q03305};
DE AltName: Full=Arginine N-methyltransferase 1 {ECO:0000305};
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=ant-1 {ECO:0000305}; Synonyms=rmt2 {ECO:0000250|UniProtKB:Q03305};
GN ORFNames=NCU08111;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:0000250|UniProtKB:Q03305}. Nucleus
CC {ECO:0000250|UniProtKB:Q03305}.
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; CM002236; EAA34605.1; -; Genomic_DNA.
DR RefSeq; XP_963841.1; XM_958748.1.
DR AlphaFoldDB; Q7SCW9; -.
DR SMR; Q7SCW9; -.
DR STRING; 5141.EFNCRP00000009630; -.
DR EnsemblFungi; EAA34605; EAA34605; NCU08111.
DR GeneID; 3879990; -.
DR KEGG; ncr:NCU08111; -.
DR VEuPathDB; FungiDB:NCU08111; -.
DR HOGENOM; CLU_033831_0_1_1; -.
DR InParanoid; Q7SCW9; -.
DR OMA; YWVVDNY; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 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; PS51559; SAM_RMT2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..429
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000228978"
FT DOMAIN 190..429
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 41..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 250..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 271..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 308..309
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 328
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ SEQUENCE 429 AA; 47726 MW; 85EF13DAF4EA1C29 CRC64;
MADNDSISVR ISEDCPPEIQ RMLTAAWAHD VDTVKKLIDT PEVARGQDPK TGESPLHAAI
RSCGAPSEDD TPEDHEKAKA TVSELLMWGA IWNDVDNNNE TPGCVAARLN RPELYELCVN
AGVRAEMLFG LMDGYEALDS DDEDDEEMAE GEEAQAEDGE EAPELVAAEE ATQTAEEETP
AVFQPPAVNL EEQVTSDKYL RSTVAYSDGK LVDDAGNGVM MAWETDIMRR SVDALLPNKE
PGKRILNIGF GMGIIDGMFA ETKPAVHHII EAHPEVLEYI STPESKFDST WEESGPAPGA
YRVWEGKWQQ IGLQLLEEGH VYDAIYFDTF GEDYGQLRMF FTEYIPGLLD SNGIFGFFNG
LGADRQICYD VYTKVAEMHL ADAGLDVEWK EIPVDMKELA EADKDGWEGV KRRYWTLDTY
RLPVCTFLG
