ID A0A0S3TCZ1_PHAAN Unreviewed; 911 AA.
AC A0A0S3TCZ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN Name=Vigan.11G252900 {ECO:0000313|EMBL:BAU02932.1};
GN ORFNames=VIGAN_11252900 {ECO:0000313|EMBL:BAU02932.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAU02932.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAU02932.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015044; BAU02932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3TCZ1; -.
DR Proteomes; UP000291084; Chromosome 11.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF50; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT3; 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 3: Inferred from homology;
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:UP000291084};
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 168..287
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 446..499
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 911 AA; 103012 MW; 11B78C34649CA3D1 CRC64;
MSTKRKTRSS SSPSLASSVK RVTRSSVTLT VASSSPSPVS SVKRVTRNVA SNSGKSKVEI
VDVASNSGKS KEANSSAVKK ETSSSVVKEE TSTFMDVTPS TPDGEESTAK FIGESVPIEE
ARRRWPKRYQ EKEKKVSTGS RSNRKQDEDE EILQARHHYT CAEVDRSTIY KLFDDAHVKA
DEGEHNYICK IVELFEAIDG SLYFTAQWYY RAKDTVIKKL AYLIEPKRVF FSEVQDDNPL
DCLVEKLNIG RLPLDIDLNV KKETISSYDY YCDTQYLLPY STFVNLPSEN DETSSETCSI
ISSDTTNGVE KSEVDSQSKD AYLPHQSKDM EMRLLDLYSG CGAMSTGLCL GGQLSGVNLV
TKWAVDLNKH ACESLKLNHP ETEVRNESAE CFLSLLKEWQ KLCSYFDLVE NKVSHEKYVN
LFSEVEEDDD EEIKEDGTDD EHGEIFEVYE IFAVCYGDPN KKKEQGLYFK VHWKGYGSDE
DSWEPIEGLR HCKDKINEFV IQGFKSNILP LPGDVDVICG GPPCQGISGF NRFRNKENPL
DDEKNKQMVV YMDIVQYLKP KFTLMENVVD IVKFADGFLG RYALGRLIQM NYQARLGIMA
AGSYGLPQFR LRMFLWGAAP SQKLPQFPLP THDVIVRGVI PVEFETNTVA YDEGHTVQLQ
RKLLLKEAIS DLPPVQNSEH RDEMKYCKPA ETEFQRFIRS TKSEMLGFQS KTKSSKTLLY
DHRPLELNAD DYQRVCRIPK KKGACFRDLP GVLVGTDNKV EWDPDMERVY LDSGKPLVPD
YAMSFVNGTS SKPFARLWWD ETVPTVVTRA EPHNQAILHP EQDRVLTIRE NARLQGFPDF
YKLCGPVKER YIQVGNAVAV PVARALGYTL GLAFQGSTST SDGPLYTLPD KFPMLREQVS
SVSSEDDEQV L
//
