SFM1_YEAST
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 03-AUG-2022, entry version 138.
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}; 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; 57.
DR IntAct; Q12314; 4.
DR MINT; Q12314; -.
DR STRING; 4932.YOR021C; -.
DR iPTMnet; Q12314; -.
DR MaxQB; Q12314; -.
DR PaxDb; Q12314; -.
DR PRIDE; Q12314; -.
DR EnsemblFungi; YOR021C_mRNA; YOR021C; YOR021C.
DR GeneID; 854186; -.
DR KEGG; sce:YOR021C; -.
DR SGD; S000005547; SFM1.
DR VEuPathDB; FungiDB:YOR021C; -.
DR eggNOG; ENOG502RXXJ; Eukaryota.
DR HOGENOM; CLU_080487_0_0_1; -.
DR InParanoid; Q12314; -.
DR OMA; KTFVVEH; -.
DR BioCyc; YEAST:G3O-33569-MON; -.
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 InterPro; IPR007364; RNA_MeTrfase_TK0422/Sfm1.
DR PANTHER; PTHR35517; PTHR35517; 1.
DR Pfam; PF04252; RNA_Me_trans; 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
