ID M4T8W2_NICBE Unreviewed; 901 AA.
AC M4T8W2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
DE Flags: Fragment;
GN Name=CMT3-2 {ECO:0000313|EMBL:AGH70220.1};
OS Nicotiana benthamiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4100 {ECO:0000313|EMBL:AGH70220.1};
RN [1] {ECO:0000313|EMBL:AGH70220.1}
RP NUCLEOTIDE SEQUENCE.
RA Hou P.-Q., Hsu K.-T., Wu W.-Z., Fu S.-F.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGH70220.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23683172; DOI=10.1111/ppl.12071;
RA Hou P.Q., Lee Y.I., Hsu K.T., Lin Y.T., Wu W.Z., Lin J.Y., Nam T.N.,
RA Fu S.F.;
RT "Functional characterization of Nicotiana benthamiana chromomethylase 3 in
RT developmental programs by virus-induced gene silencing.";
RL Physiol. Plantarum 150:119-132(2014).
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 ECO:0000256|RuleBase:RU000417};
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, ECO:0000256|RuleBase:RU000416}.
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DR EMBL; KC453971; AGH70220.1; -; mRNA.
DR AlphaFoldDB; M4T8W2; -.
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; 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 NCBIfam; TIGR00675; dcm; 1.
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; 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 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..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
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 125..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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGH70220.1"
SQ SEQUENCE 901 AA; 101098 MW; C607467E6421A4FD CRC64;
MPSKRKATSP ASKLESSSAS RKSKRLATKP DPVVAPPADS DFEESEPVLS TKKKSTRRTA
EKEAVDSQSK RRAVENSGPF VAEKTEPDPD PEVEDCAVES DFVEEVDETE HGTLKKSLAV
SPSKRKPQRG EKVKEEECML SGEPVPDVEA RQRWPHRYNR GKANGTKSLN GQDDSDQQLQ
AKCHFTQASV DGQIYCLEDD AHVKAADGEE DYICKIVEFF EAVDGMQYFT AQWFYRAKDT
VIKTHDQFID KKRVFLSEIM DDNPIDCLVI KLKIVPVPSN ATLQFKENAK SNCDFYYDMM
YLLPYSSFLS LPPDSSSPVS SSSTISSEND AGEVKEHNLE KKLLDLYSGC GAMSTGLCLG
ANSNGVKLVT KWAVDLNSFA CDSLRLNHPE TQVRNEYASD FLSLLKEWMQ LCSSCSLVKS
SVPPHPHLKV IDEVEEDENA DESEDSGDDK RGENFEVEEL LEVCYGDPNA VKKPGLYFKV
HWQGYGPEED TWEPIDGLSE CPKKIKEFVT KGFKANLLPL PGDVDVICGG PPCQGISGFN
RFRNKENPLE DPKNQQLDVF MDIVDFLKPR FVLMENVVDL IKFSNGFLGR YALGRLVGMN
YQARMGMMAA GAYGLPQFRM RVFMWGALSS EKLPQYPLPT HKVIVRGVIP TEFESNTVAF
DEGQELELKK ELFLGDALSD LPSVENNEQR DEMIYTNEPK SDFQHFIRLG RDGALGSVLY
DHRPLQLNDD DYQRVCQIPK RKGANFRDLP GVRVRSDNKV EWDPDVERVK LPSGKPLVPD
YAMSFVGGSS TKPFGRLWWD ETVPTVVTRA EPHNQTIIHP HQNRVLTIRE NARLQGFPDY
YKLTGPIKER YIQVGNAVAV PVARALGYSL AMAMKGSSEG KPLMSLPDNF PSHAEQIEVS
Q
//
