ID W1PFN6_AMBTC Unreviewed; 1566 AA.
AC W1PFN6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN ORFNames=AMTR_s00017p00254260 {ECO:0000313|EMBL:ERN08792.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN08792.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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|PIRNR:PIRNR037404,
CC ECO:0000256|RuleBase:RU000417};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037404}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family.
CC {ECO:0000256|PIRNR:PIRNR037404, ECO:0000256|PROSITE-ProRule:PRU01016,
CC ECO:0000256|RuleBase:RU000416}.
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DR EMBL; KI393256; ERN08792.1; -; Genomic_DNA.
DR STRING; 13333.W1PFN6; -.
DR EnsemblPlants; ERN08792; ERN08792; AMTR_s00017p00254260.
DR Gramene; ERN08792; ERN08792; AMTR_s00017p00254260.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR HOGENOM; CLU_002247_0_0_1; -.
DR OMA; KINDAEC; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central.
DR CDD; cd04712; BAH_DCM_I; 1.
DR CDD; cd04708; BAH_plantDCM_II; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2.
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; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00145; DNA_methylase; 2.
DR Pfam; PF12047; DNMT1-RFD; 2.
DR PIRSF; PIRSF037404; DNMT1; 6.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037404};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037404}.
FT DOMAIN 765..899
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 937..1077
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..698
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1222
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1566 AA; 175482 MW; 9C000A9118387560 CRC64;
MDTAVKRQKP TKATTTTNNY NKKRTADAPP ERNSTSDIEN PSRRRLPKRA ASCSNFKERE
KPLRLNQDDY ILPKVQQTIA DDEQTAIQLT RKGDEEEEQT PQRRLMDFII HDSDGTPQPF
EMSEVQDLYI SALILPAGPT SSTDKNCGAC CEGFGRIESW SISGYDEGKP LIWVSTDLAE
YSLLKPSSQY KKHFDIFSDK ALLSVEVFKK LSKFHGGYPL IGLDELLASL ARALGSRKGG
LTRDFIISQG EFVANQLYGL DSTSSNNDQV FAGLPVLTSW RNECQMREPS CRLTKVKDGS
LKIGNGLASS ASSSPDVMED ESEKMARLLQ EEEVWREMKQ KKGHVFTSSK SKKYYVKINE
DEIVNDYPLP AFYKASEEEM DEYVFFDEDL HTLAPDDLPR RMLHNWALYN SDSRLVSLEL
LPMLPGTETD VTIFGSGSMT EDDGSGFCID VKGPSGSSSN GALDEVSNKG IPVYLSAVKE
WMIEFGASML FISIRTDGAW YRLGKPSKQY APWYEPVLRT ATLAIGIITM LKEQSRVSRL
SFNDVIRKLS ELPKGDPICI SSNQAAVERY VVVHGQIILQ QFAEFPDENI RKSAFVSGLS
MKMEQRHHTK LAMKKKLMLV RKEANMNPRA AMRPEITKKK QMRATTTKLI NRIWSDYYSN
FEVENGVEPT KGGKEEEDEE VENEENEDEE EEEEEEGEAL ASRPISNGGE SAFVKTNSSN
GMSKPSTTSN SQKSNGEITR WVGDCVGKVA SSGNVLYKSA SILGDMVLVG GFVIVEPDSY
DELPAILFVE YMFENSDGVK MIHGRLMQRG SQTVLGNAAN AREVFLTDEC MDVELSEVKQ
SVVVDVRQRP WGQKYRKENE ASDKVDKARA EEMEKKGLPI EYYCKSLYLP DRGGFFKLPC
ETMGLGTGVC VSCSCKEGVN KEFRMLSDKS GFVCKGVQYT LLDFVYVNPQ VFAVSVEQEK
FKAGRNVGLR AYVVCQLLEI EVSGGSKKVD SIKTTKLKVR RFYRPEDIGT EKAYTADIRE
VYYSEEICTV PLDMLEGKCE VRKQHDLPSL HGPVTFDHIF FCLCVYDPVN GSVKQLPSGT
KLRYSKGTLS GNGKNKGKAV EGESPSQKKS HSPNNCLATL DIFAGCGGLS EGLQKSGVGF
TKWAIEYEEP AAEAFKLNHP EAHVFCDNCN VILRAIMEKC GDIDDCICTP EAADHALKLS
EDKKNNLPLP GQVDFINGGP PCQGFSGMNR FNQSTWSKVQ CEMILSFLSY ADYFRPRFFL
LENVRNFVAF NKGQTFRLTL ASLLEMGYQV RFGVLEAGNY GVAQSRKRAF IWAASPNETL
PEWPEPMHVF ASPQLKITLS DDSQFSAVRS TSEGAPFRSM TVRDTIGDLP PVGNGADKVE
IKYGSDPASW FQKQIRLNEE VLIDHVTKEM NGLNFIRCQK IPKRPGADWR DLPDEKVKLS
NGQLVDLIPW CLPNTSERHN QWKGLFGRLD WQGNFPTSIT DPQPMGKVGM CFHPDQDRIL
TVRECARSQG FPDSYRFCGN IHNKYRQIGN AVPPPLAMVL GRKLKEALDA KARTFDEPRN
LNMSTI
//
