ID X5JTY0_NICSY Unreviewed; 901 AA.
AC X5JTY0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN Name=cmt3b {ECO:0000313|EMBL:CDN40870.1};
GN Synonyms=LOC104228752 {ECO:0000313|RefSeq:XP_009779580.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|EMBL:CDN40870.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|EMBL:CDN40870.1}
RP NUCLEOTIDE SEQUENCE.
RA Fulnecek J.;
RT "Paralogous gene for chromomethylase3 is common in Solanaceae.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_009779580.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009779580.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000743};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; HG937772; CDN40870.1; -; mRNA.
DR RefSeq; XP_009779580.1; XM_009781278.1.
DR STRING; 4096.X5JTY0; -.
DR KEGG; nsy:104228752; -.
DR eggNOG; ENOG502QW29; Eukaryota.
DR OrthoDB; 1215065at2759; -.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd04716; BAH_plantDCM_I; 1.
DR CDD; cd18635; CD_CMT3_like; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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; IPR023779; Chromodomain_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF47; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
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; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 2: Evidence at transcript level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT DOMAIN 193..312
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 455..508
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 901 AA; 100970 MW; F045DCD93667E6BC CRC64;
MPSKRKAISP ASKPESSSAS RKSKRLATKP DPVVAAPADS DFEESEPVLS TKKKSTRRTA
EKEVVDSQSK RQAVENSGPF VAEKAEPDPD PEVEDCALES DFVEEVDETE HGTLKKSLAV
SPSKRKPKRS EKVKDEECVL SGEPVPDAEA RQRWPHRYNK GKANGTKSLN GQDDADQQLQ
AKCHFTQASV DGQIYYLEDD AHVKAADGEE DYICKIVEFF EAVDGMQYFT AQWFYRAKDT
VIKSHDQFID KKRVFLSEIK DDNPIDCLVI KLKIVPVPSN ATLQFKENAK SNCDFYYDMM
YLLPYSSFLS LPPDSTSPVS SSSTISSDTD AGEVKEHNLE KKLLDLYSGC GAMSTGLCLG
ANSNGVKLVT KWAVDLNRFA CDSLRLNHPG TQVRNEYASD FLSLLKEWVQ LCSSFSLVKS
NVPPHPHLKV TDEVEEDEND DESEDSGDDK KGEIFEVEEI LEVCYGDPNA VKKPGLYFKV
RWQGYGPEED TWEPIDGLSE CPKKIREFVT KGFKANLLPL PGDVDVICGG PPCQGISGFN
RFRNKENPLG DPKNQQLDVF MDIVDFLKPR FVLMENVVDL IKFSNGFLGR YALGRLVGMN
YQARMGMMAA GAYGLPQFRM RVFMWGALSS EKLPQYPLPT HKVIVRGVIP TEFESNTVAF
DEGRELDLKK ELFLGDALSD LPSVENNEQR DEMPYTNEPT SDFQHFIRLG RDGALGSVLY
DHRPLQLNDD DYQRVCQIPK RKGANFRDLP GVRVRSDNKV EWDPDVERVK LPSGKPLVPD
YAMSFVGGSS TKPFGRLWWD ETVPTVVTRA EPHNQTIIHP QQNRVLTIRE NARLQGFPDY
YKLTGPIKER YIQVGNAVAV PVARALGYSL AMAMKGSSDG KPLMSLPENF PSHAEQIEVS
Q
//
