ID   SFM1_YEAST              Reviewed;         213 AA.
AC   Q12314; D6W288;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Protein arginine N-methyltransferase SFM1 {ECO:0000305|PubMed:22650761};
DE            EC=2.1.1.- {ECO:0000269|PubMed:22650761};
DE   AltName: Full=SPOUT family methyltransferase 1 {ECO:0000303|PubMed:22650761};
GN   Name=SFM1 {ECO:0000303|PubMed:22650761};
GN   OrderedLocusNames=YOR021C {ECO:0000312|SGD:S000005547};
GN   ORFNames=OR26.11;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-207, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22650761; DOI=10.1021/bi300186g;
RA   Young B.D., Weiss D.I., Zurita-Lopez C.I., Webb K.J., Clarke S.G.,
RA   McBride A.E.;
RT   "Identification of methylated proteins in the yeast small ribosomal
RT   subunit: a role for SPOUT methyltransferases in protein arginine
RT   methylation.";
RL   Biochemistry 51:5091-5104(2012).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC       methyltransferase that monomethylates ribosomal protein S3 (RPS3) at
CC       'Arg-146'. {ECO:0000269|PubMed:22650761}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2520 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase SFM1 family.
CC       {ECO:0000305}.
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DR   EMBL; X87331; CAA60770.1; -; Genomic_DNA.
DR   EMBL; Z74929; CAA99211.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10804.1; -; Genomic_DNA.
DR   PIR; S54627; S54627.
DR   RefSeq; NP_014664.1; NM_001183440.1.
DR   PDB; 5C74; X-ray; 1.90 A; A/B=1-204.
DR   PDB; 5C77; X-ray; 2.50 A; A/B=1-213.
DR   PDB; 5H5D; X-ray; 2.70 A; A=2-213.
DR   PDB; 5H5E; X-ray; 2.09 A; A=2-213.
DR   PDB; 5H5F; X-ray; 1.70 A; A=2-213.
DR   PDBsum; 5C74; -.
DR   PDBsum; 5C77; -.
DR   PDBsum; 5H5D; -.
DR   PDBsum; 5H5E; -.
DR   PDBsum; 5H5F; -.
DR   AlphaFoldDB; Q12314; -.
DR   SMR; Q12314; -.
DR   BioGRID; 34425; 58.
DR   IntAct; Q12314; 4.
DR   MINT; Q12314; -.
DR   STRING; 4932.YOR021C; -.
DR   iPTMnet; Q12314; -.
DR   MaxQB; Q12314; -.
DR   PaxDb; 4932-YOR021C; -.
DR   PeptideAtlas; Q12314; -.
DR   EnsemblFungi; YOR021C_mRNA; YOR021C; YOR021C.
DR   GeneID; 854186; -.
DR   KEGG; sce:YOR021C; -.
DR   AGR; SGD:S000005547; -.
DR   SGD; S000005547; SFM1.
DR   VEuPathDB; FungiDB:YOR021C; -.
DR   eggNOG; ENOG502RXXJ; Eukaryota.
DR   HOGENOM; CLU_080487_0_0_1; -.
DR   InParanoid; Q12314; -.
DR   OMA; LEYIHIC; -.
DR   OrthoDB; 275799at2759; -.
DR   BioCyc; YEAST:G3O-33569-MONOMER; -.
DR   BioGRID-ORCS; 854186; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q12314; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12314; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:SGD.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IMP:SGD.
DR   CDD; cd18090; Arginine_MT_Sfm1; 1.
DR   InterPro; IPR007364; SFM1-like.
DR   PANTHER; PTHR35517; PROTEIN ARGININE N-METHYLTRANSFERASE SFM1; 1.
DR   PANTHER; PTHR35517:SF1; PROTEIN ARGININE N-METHYLTRANSFERASE SFM1; 1.
DR   Pfam; PF04252; SFM1-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methyltransferase; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..213
FT                   /note="Protein arginine N-methyltransferase SFM1"
FT                   /id="PRO_0000237643"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           14..27
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           48..52
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           93..97
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:5C74"
FT   HELIX           118..123
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   TURN            125..127
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           140..151
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:5H5F"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:5H5F"
SQ   SEQUENCE   213 AA;  24744 MW;  11A1FB089B39E7EA CRC64;
     MKYIIEHMEE GFSEWVILEY SQILREVGAE NLILSSLPES TTEKDIPQRL LKLGLRWTTK
     DLKGINEDFK DLELLKDGRV CLLDPRATID LQPEDATKFD YFVFGGILGD HPPRDRTKEL
     KTAYPNLLIS RRLGDKQMTT DTAIRTTQLI IKDRIAFEDI KFIDYPEFRF NKNEATEMPF
     RYVLDKEGKP ILPEGMLDLI KKDSAQSLDD LLM
//