CMT1_MAIZE
ID CMT1_MAIZE Reviewed; 912 AA.
AC Q9AXT8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE EC=2.1.1.37;
DE AltName: Full=Chromomethylase 1;
DE AltName: Full=DNA cytosine methyltransferase MET2a;
DE AltName: Full=Zea methyltransferase2;
DE Short=Zmet2;
GN Name=MET2A;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF 834-ASP--GLN-912.
RX PubMed=11487702; DOI=10.2307/3871328;
RA Papa C.M., Springer N.M., Muszynski M.G., Meeley R., Kaeppler S.M.;
RT "Maize chromomethylase Zea methyltransferase2 is required for CpNpG
RT methylation.";
RL Plant Cell 13:1919-1928(2001).
CC -!- FUNCTION: Involved in the CpXpG methylation and in gene silencing.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AF243043; AAK11516.1; -; mRNA.
DR RefSeq; NP_001104978.1; NM_001111508.1.
DR PDB; 4FSX; X-ray; 3.20 A; A/B=130-912.
DR PDB; 4FT2; X-ray; 3.20 A; A/B=130-912.
DR PDB; 4FT4; X-ray; 2.70 A; A/B=130-912.
DR PDBsum; 4FSX; -.
DR PDBsum; 4FT2; -.
DR PDBsum; 4FT4; -.
DR AlphaFoldDB; Q9AXT8; -.
DR SMR; Q9AXT8; -.
DR STRING; 4577.GRMZM2G025592_P01; -.
DR REBASE; 4907; M.ZmaIIA.
DR iPTMnet; Q9AXT8; -.
DR PaxDb; Q9AXT8; -.
DR PRIDE; Q9AXT8; -.
DR GeneID; 541827; -.
DR eggNOG; ENOG502QW29; Eukaryota.
DR OrthoDB; 898916at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9AXT8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..912
FT /note="DNA (cytosine-5)-methyltransferase 1"
FT /id="PRO_0000246694"
FT DOMAIN 184..309
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 341..872
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT DOMAIN 441..504
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT MUTAGEN 834..912
FT /note="Missing: In zmet2-m1::Mu; loss of activity."
FT /evidence="ECO:0000269|PubMed:11487702"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 366..376
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 398..414
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4FSX"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 486..499
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 522..526
FT /evidence="ECO:0007829|PDB:4FT4"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 571..582
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 586..593
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 658..662
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 686..691
FT /evidence="ECO:0007829|PDB:4FT4"
FT TURN 695..699
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:4FSX"
FT HELIX 724..732
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 741..743
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:4FT2"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 775..779
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 780..783
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:4FSX"
FT STRAND 807..813
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 815..820
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 823..829
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 842..851
FT /evidence="ECO:0007829|PDB:4FT4"
FT HELIX 855..870
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:4FT4"
FT STRAND 884..887
FT /evidence="ECO:0007829|PDB:4FT4"
SQ SEQUENCE 912 AA; 101046 MW; C697C45AE152FB4D CRC64;
MAPSSPSPAA PTRVSGRKRA AKAEEIHQNK EEEEEVAAAS SAKRSRKAAS SGKKPKSPPK
QAKPGRKKKG DAEMKEPVED DVCAEEPDEE ELAMGEEEAE EQAMQEEVVA VAAGSPGKKR
VGRRNAAAAA GDHEPEFIGS PVAADEARSN WPKRYGRSTA AKKPDEEEEL KARCHYRSAK
VDNVVYCLGD DVYVKAGENE ADYIGRITEF FEGTDQCHYF TCRWFFRAED TVINSLVSIS
VDGHKHDPRR VFLSEEKNDN VLDCIISKVK IVHVDPNMDP KAKAQLIESC DLYYDMSYSV
AYSTFANISS ENGQSGSDTA SGISSDDVDL ETSSSMPTRT ATLLDLYSGC GGMSTGLCLG
AALSGLKLET RWAVDFNSFA CQSLKYNHPQ TEVRNEKADE FLALLKEWAV LCKKYVQDVD
SNLASSEDQA DEDSPLDKDE FVVEKLVGIC YGGSDRENGI YFKVQWEGYG PEEDTWEPID
NLSDCPQKIR EFVQEGHKRK ILPLPGDVDV ICGGPPCQGI SGFNRYRNRD EPLKDEKNKQ
MVTFMDIVAY LKPKYVLMEN VVDILKFADG YLGKYALSCL VAMKYQARLG MMVAGCYGLP
QFRMRVFLWG ALSSMVLPKY PLPTYDVVVR GGAPNAFSQC MVAYDETQKP SLKKALLLGD
AISDLPKVQN HQPNDVMEYG GSPKTEFQRY IRLSRKDMLD WSFGEGAGPD EGKLLDHQPL
RLNNDDYERV QQIPVKKGAN FRDLKGVRVG ANNIVEWDPE IERVKLSSGK PLVPDYAMSF
IKGKSLKPFG RLWWDETVPT VVTRAEPHNQ VIIHPTQARV LTIRENARLQ GFPDYYRLFG
PIKEKYIQVG NAVAVPVARA LGYCLGQAYL GESEGSDPLY QLPPSFTSVG GRTAGQARAS
PVGTPAGEVV EQ
