ID Q9C9M1_ARATH Unreviewed; 358 AA.
AC Q9C9M1;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Protein-lysine N-methyltransferase At1g66680 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=AR401 {ECO:0000313|EMBL:AEE34544.1, ECO:0000313|TAIR:AT1G66680};
GN OrderedLocusNames=At1g66680 {ECO:0000313|Araport:AT1G66680,
GN ECO:0000313|EMBL:AEE34544.1};
GN ORFNames=F4N21.18 {ECO:0000313|EMBL:AEE34544.1}, F4N21_18
GN {ECO:0000313|EMBL:AAG60072.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AAG60072.1};
RN [1] {ECO:0000313|EMBL:AAG60072.1}
RP NUCLEOTIDE SEQUENCE.
RA Lin X., Kaul S., Town C.D., Benito M., Creasy T.H., Haas B.J., Wu D.,
RA Maiti R., Ronning C.M., Koo H., Fujii C.Y., Utterback T.R., Barnstead M.E.,
RA Bowman C.L., White O., Nierman W.C., Fraser C.M.;
RT "Arabidopsis thaliana chromosome 1 BAC F4N21 genomic sequence.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEE34544.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3] {ECO:0000313|EMBL:AAG60072.1}
RP NUCLEOTIDE SEQUENCE.
RA Town C.D., Kaul S.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PubMed:18433157}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [5] {ECO:0007829|PubMed:19245862}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6] {ECO:0007829|PubMed:19376835}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7] {ECO:0000313|EMBL:AEE34544.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AEE34544.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates elongation factor 1-alpha.
CC {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000256|HAMAP-Rule:MF_03188}.
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DR EMBL; AC013288; AAG60072.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34544.1; -; Genomic_DNA.
DR RefSeq; NP_176841.1; NM_105339.4.
DR AlphaFoldDB; Q9C9M1; -.
DR SMR; Q9C9M1; -.
DR STRING; 3702.Q9C9M1; -.
DR PaxDb; 3702-AT1G66680-1; -.
DR ProteomicsDB; 189168; -.
DR DNASU; 842986; -.
DR EnsemblPlants; AT1G66680.1; AT1G66680.1; AT1G66680.
DR GeneID; 842986; -.
DR Gramene; AT1G66680.1; AT1G66680.1; AT1G66680.
DR KEGG; ath:AT1G66680; -.
DR Araport; AT1G66680; -.
DR TAIR; AT1G66680; AR401.
DR eggNOG; KOG1271; Eukaryota.
DR HOGENOM; CLU_044783_0_0_1; -.
DR OMA; PEANQHL; -.
DR OrthoDB; 609682at2759; -.
DR PRO; PR:Q9C9M1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M1; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12843:SF5; EEF1A LYSINE METHYLTRANSFERASE 2; 1.
DR PANTHER; PTHR12843; PROTEIN-LYSINE N-METHYLTRANSFERASE METTL10; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03188};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03188};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9C9M1,
KW ECO:0007829|ProteomicsDB:Q9C9M1}; Receptor {ECO:0000313|EMBL:AAG60072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03188}.
FT DOMAIN 172..293
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39229 MW; FE9A99DE7FE7C592 CRC64;
MAGIRLLPEE PETTPQQQAR AAAAVTTTTT DSLASDDDRS IAADSWSIKS EYGSTLDDDQ
RHADAAEALS SANFRVSSDY SSDKEEPDAD GGGQSMLGLQ SYWDAAYSDE LTNFREHGHA
GEVWFGDDVM EIVTSWTKDL CVEISQRNMS VSENDVTTEV NDQADKYLSS WNVLDLGTGN
GLLLHQLAKE GFSDLTGTDY SDGAVELAQH LSQRDGFPNI RFMVDDILDT KLEQQFKLVM
DKGTLDAIGL HPDGPVKRVM YWDSVSKLVA PGGILVITSC NHTKDELVEE VENFNIRKSN
LCRGDGNDAN NVLSSGSEAA SRIDQPPFEY LSHVRTYPTF MFSGSVGSRV ATVAFLRK
//
