CRG1_YEAST
ID CRG1_YEAST Reviewed; 291 AA.
AC P38892; D3DLF8; Q6Q5R3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase CRG1;
DE EC=2.1.1.-;
DE AltName: Full=Cantharidin resistance protein 1;
GN Name=CRG1; OrderedLocusNames=YHR209W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=9873020; DOI=10.1074/jbc.274.2.814;
RA Niewmierzycka A., Clarke S.;
RT "S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae.
RT Identification of a novel protein arginine methyltransferase.";
RL J. Biol. Chem. 274:814-824(1999).
RN [5]
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 [6]
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 [7]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
RN [8]
RP FUNCTION.
RX PubMed=18622389; DOI=10.1038/nchembio.100;
RA Hoon S., Smith A.M., Wallace I.M., Suresh S., Miranda M., Fung E.,
RA Proctor M., Shokat K.M., Zhang C., Davis R.W., Giaever G., St Onge R.P.,
RA Nislow C.;
RT "An integrated platform of genomic assays reveals small-molecule
RT bioactivities.";
RL Nat. Chem. Biol. 4:498-506(2008).
CC -!- FUNCTION: Probable S-adenosylmethionine-dependent methyltransferase
CC which mediates cantharidin resistance. {ECO:0000269|PubMed:18622389,
CC ECO:0000269|PubMed:9873020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By cell wall perturbation. {ECO:0000269|PubMed:15116342}.
CC -!- MISCELLANEOUS: Present with 4380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; U00029; AAB69732.1; -; Genomic_DNA.
DR EMBL; AY557767; AAS56093.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06902.1; -; Genomic_DNA.
DR PIR; S48990; S48990.
DR RefSeq; NP_012079.1; NM_001179340.1.
DR AlphaFoldDB; P38892; -.
DR SMR; P38892; -.
DR BioGRID; 36643; 94.
DR DIP; DIP-828N; -.
DR IntAct; P38892; 1.
DR MINT; P38892; -.
DR STRING; 4932.YHR209W; -.
DR iPTMnet; P38892; -.
DR MaxQB; P38892; -.
DR PaxDb; P38892; -.
DR PRIDE; P38892; -.
DR EnsemblFungi; YHR209W_mRNA; YHR209W; YHR209W.
DR GeneID; 856616; -.
DR KEGG; sce:YHR209W; -.
DR SGD; S000001252; CRG1.
DR VEuPathDB; FungiDB:YHR209W; -.
DR eggNOG; KOG3010; Eukaryota.
DR GeneTree; ENSGT00940000176672; -.
DR HOGENOM; CLU_049344_1_2_1; -.
DR InParanoid; P38892; -.
DR OMA; KEWQECV; -.
DR BioCyc; YEAST:G3O-31234-MON; -.
DR PRO; PR:P38892; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38892; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IMP:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0055088; P:lipid homeostasis; IMP:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..291
FT /note="Probable S-adenosylmethionine-dependent
FT methyltransferase CRG1"
FT /id="PRO_0000202943"
FT CONFLICT 23
FT /note="Y -> C (in Ref. 3; AAS56093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 33785 MW; C1DFE5F73BAAC617 CRC64;
MPKTSYLNKN FESAHYNNVR PSYPLSLVNE IMKFHKGTRK SLVDIGCGTG KATFVVEPYF
KEVIGIDPSS AMLSIAEKET NERRLDKKIR FINAPGEDLS SIRPESVDMV ISAEAIHWCN
LERLFQQVSS ILRSDGTFAF WFYIQPEFVD FPEALNVYYK YGWSKDYMGK YLNDNQREIL
LNYGGEKLRS LLSDRFGDIE VTIYSPSDPN ASTVTAENSQ FLWRAAITLN QFKEFVKSWS
IYTSWARDNP SKPDIADIFI NELKEICHCE DLNVPLKIEW STFYYLCRKR E
