IME4_YEAST
ID IME4_YEAST Reviewed; 600 AA.
AC P41833; D6VTW2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=N6-adenosine-methyltransferase IME4;
DE EC=2.1.1.348 {ECO:0000269|PubMed:12384598};
GN Name=IME4; Synonyms=SPO8; OrderedLocusNames=YGL192W; ORFNames=G1337;
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 [GENOMIC DNA].
RC STRAIN=GKY5;
RX PubMed=1545790; DOI=10.1128/mcb.12.3.1078-1086.1992;
RA Shah J.C., Clancy M.J.;
RT "IME4, a gene that mediates MAT and nutritional control of meiosis in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:1078-1086(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sakurai M.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND MUTAGENESIS OF ASP-348 AND
RP TRP-351.
RX PubMed=12384598; DOI=10.1093/nar/gkf573;
RA Clancy M.J., Shambaugh M.E., Timpte C.S., Bokar J.A.;
RT "Induction of sporulation in Saccharomyces cerevisiae leads to the
RT formation of N6-methyladenosine in mRNA: a potential mechanism for the
RT activity of the IME4 gene.";
RL Nucleic Acids Res. 30:4509-4518(2002).
RN [7]
RP IDENTIFICATION IN THE MIS COMPLEX, AND FUNCTION.
RX PubMed=22685417; DOI=10.1371/journal.pgen.1002732;
RA Agarwala S.D., Blitzblau H.G., Hochwagen A., Fink G.R.;
RT "RNA methylation by the MIS complex regulates a cell fate decision in
RT yeast.";
RL PLoS Genet. 8:E1002732-E1002732(2012).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE MIS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24269006; DOI=10.1016/j.cell.2013.10.047;
RA Schwartz S., Agarwala S.D., Mumbach M.R., Jovanovic M., Mertins P.,
RA Shishkin A., Tabach Y., Mikkelsen T.S., Satija R., Ruvkun G., Carr S.A.,
RA Lander E.S., Fink G.R., Regev A.;
RT "High-resolution mapping reveals a conserved, widespread, dynamic mRNA
RT methylation program in yeast meiosis.";
RL Cell 155:1409-1421(2013).
CC -!- FUNCTION: Catalytic component of the MIS complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation on some mRNAs during
CC meiosis and is required for sporulation. M6A, which takes place on the
CC adenosine of 5'-[AG]GAC-3' consensus sites of some mRNAs, is probably
CC required to initiate sporulation. Positive regulator for IME2.
CC {ECO:0000269|PubMed:12384598, ECO:0000269|PubMed:22685417,
CC ECO:0000269|PubMed:24269006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348;
CC Evidence={ECO:0000269|PubMed:12384598};
CC -!- SUBUNIT: Component of the MIS complex, composed of SLZ1, MUM2 and IME4.
CC {ECO:0000269|PubMed:22685417, ECO:0000269|PubMed:24269006}.
CC -!- INTERACTION:
CC P41833; P38236: MUM2; NbExp=3; IntAct=EBI-9210, EBI-11619;
CC P41833; P40167: SLZ1; NbExp=2; IntAct=EBI-9210, EBI-29095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24269006}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:24269006}. Note=Localizes in the
CC nucleolus during the period of m6A mRNA accumulation.
CC -!- INDUCTION: In response to starvation conditions.
CC {ECO:0000269|PubMed:12384598}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC ProRule:PRU00489}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U30859; AAA74443.1; -; Genomic_DNA.
DR EMBL; D23721; BAA04938.1; -; Genomic_DNA.
DR EMBL; X91837; CAA62952.1; -; Genomic_DNA.
DR EMBL; Z72714; CAA96904.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07923.1; -; Genomic_DNA.
DR PIR; S48509; S48509.
DR RefSeq; NP_011323.3; NM_001181057.3.
DR AlphaFoldDB; P41833; -.
DR SMR; P41833; -.
DR BioGRID; 33064; 20.
DR ComplexPortal; CPX-3211; MIS complex.
DR DIP; DIP-1382N; -.
DR IntAct; P41833; 4.
DR MINT; P41833; -.
DR STRING; 4932.YGL192W; -.
DR PaxDb; P41833; -.
DR PRIDE; P41833; -.
DR EnsemblFungi; YGL192W_mRNA; YGL192W; YGL192W.
DR GeneID; 852683; -.
DR KEGG; sce:YGL192W; -.
DR SGD; S000003160; IME4.
DR VEuPathDB; FungiDB:YGL192W; -.
DR eggNOG; KOG2098; Eukaryota.
DR GeneTree; ENSGT00550000075058; -.
DR HOGENOM; CLU_018702_4_1_1; -.
DR InParanoid; P41833; -.
DR OMA; YVHYLQY; -.
DR BioCyc; YEAST:G3O-30673-MON; -.
DR PRO; PR:P41833; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P41833; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:1902974; P:meiotic DNA replication initiation; IMP:SGD.
DR GO; GO:0080009; P:mRNA methylation; IMP:SGD.
DR GO; GO:2000221; P:negative regulation of pseudohyphal growth; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Methyltransferase; Nucleus; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Sporulation; Transferase.
FT CHAIN 1..600
FT /note="N6-adenosine-methyltransferase IME4"
FT /id="PRO_0000207634"
FT REGION 525..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 348
FT /note="D->A: Impairs ability to sporulate."
FT /evidence="ECO:0000269|PubMed:12384598"
FT MUTAGEN 351
FT /note="W->A: Impairs ability to sporulate."
FT /evidence="ECO:0000269|PubMed:12384598"
SQ SEQUENCE 600 AA; 69396 MW; A99BE7EBA76790BA CRC64;
MINDKLVHFL IQNYDDILRA PLSGQLKDVY SLYISGGYDD EMQKLRNDKD EVLQFEQFWN
DLQDIIFATP QSIQFDQNLL VADRPEKIVY LDVFSLKILY NKFHAFYYTL KSSSSSCEEK
VSSLTTKPEA DSEKDQLLGR LLGVLNWDVN VSNQGLPREQ LSNRLQNLLR EKPSSFQLAK
ERAKYTTEVI EYIPICSDYS HASLLSTSVY IVNNKIVSLQ WSKISACQEN HPGLIECIQS
KIHFIPNIKP QTDISLGDCS YLDTCHKLNT CRYIHYLQYI PSCLQERADR ETASENKRIR
SNVSIPFYTL GNCSAHCIKK ALPAQWIRCD VRKFDFRVLG KFSVVIADPA WNIHMNLPYG
TCNDIELLGL PLHELQDEGI IFLWVTGRAI ELGKESLNNW GYNVINEVSW IKTNQLGRTI
VTGRTGHWLN HSKEHLLVGL KGNPKWINKH IDVDLIVSMT RETSRKPDEL YGIAERLAGT
HARKLEIFGR DHNTRPGWFT IGNQLTGNCI YEMDVERKYQ EFMKSKTGTS HTGTKKIDKK
QPSKLQQQHQ QQYWNNMDMG SGKYYAEAKQ NPMNQKHTPF ESKQQQKQQF QTLNNLYFAQ
