ID A0A2I3G7H5_NOMLE Unreviewed; 1646 AA.
AC A0A2I3G7H5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN Name=DNMT1 {ECO:0000313|Ensembl:ENSNLEP00000027390.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000027390.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000027390.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000027390.1}
RP IDENTIFICATION.
RG Ensembl;
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|PIRNR:PIRNR037404};
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}.
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DR EMBL; ADFV01088791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01088792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01088793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01088794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01088795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01088796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000027390; -.
DR Ensembl; ENSNLET00000057320.1; ENSNLEP00000027390.1; ENSNLEG00000012092.3.
DR GeneTree; ENSGT00390000005100; -.
DR InParanoid; A0A2I3G7H5; -.
DR OMA; EKHRQVG; -.
DR Proteomes; UP000001073; Chromosome 10.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:1903926; P:cellular response to bisphenol A; IEA:Ensembl.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1905931; P:negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IEA:Ensembl.
DR CDD; cd04760; BAH_Dnmt1_I; 1.
DR CDD; cd04711; BAH_Dnmt1_II; 1.
DR Gene3D; 1.10.10.2230; -; 1.
DR Gene3D; 2.30.30.490; -; 2.
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; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF037404; DNMT1; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01137; DMAP_binding; 1.
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; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037404-3};
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:UP000001073};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037404-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 16..109
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 634..680
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 743..868
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 960..1088
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 103..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1214
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
SQ SEQUENCE 1646 AA; 185193 MW; 4AECE0327CDEEBC8 CRC64;
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ
LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHACN REVNGRLENG NQARSEDRRV
AMADANSPPK PLSKPRTPRR SKSDGEAKCS RDPPASASRA TGIRAEPPPS PRITRKSTRQ
TTITSHFAKG PAKRKPQEES ERAKSDESMK EEDKDQVGPV LSFPDSTLTW SCACVVFCDR
TPKQKLKEEL DREARAGMHT DEDEDGDEKD EKKHRSQPKD LAAKRRPEEK EPEKVNPQIT
DEKDEDEKEE KRRKTTPKEP TEKKMARAKT VVNSKTHPPK CIQCGQYLDD PDLKYGQHPP
DAVDEPQMLT NEKLSIFDAN ESGFESYEAL PQHKLTCFSV YCKHGHLCPI DTGLIEKNIE
LFFSGSAKPI YDDDPSLEGG VNGKNLGPIN EWWITGFDGG EKALIGFSTS FAEYILMDPS
PEYAPIFGLM QEKIYISKIV VEFLQSNSDS TYEDLINKIE TTVPPSGLNL NRFTEDSLLR
HAQFVVEQVE SYDEAGDSDE QPIFLTPCMR DLIKLAGVTL GQRRAQARRQ TIRHSTREKD
RGPTKATTTK LVYQIFDTFF AEQIEKDDRE DKENAFKRRR CGVCEVCQQP ECGKCKACKD
MVKFGGSGRS KQACQERRCP NMAMKEADDD EEVDDNIPEM PSPKKMHQGK KKKQNKNRIS
WVGEAVKTDG KKSYYKKVCI DAETLEVGDC VSVIPDDSSK PLYLARVTAL WEDSSNGQMF
HAHWFCAGTD TVLGATSDPL ELFLVDECED MQLSYIHSKV KVIYKAPSEN WAMEGGMDPE
SLLEGDDGKT YFYQLWYDQD YARFESPPKT QPTEENKFKF CVSCARLAEM RQKEIPRVLE
QLEDLDSRVL YYSATKNGIL YRVGDGVYLP PEAFTFNIKL SSPVKRPRKE PVDEDLYPEH
YRKYSDYIKG SNLDAPEPYR IGRIKEIFCP KKSNGRPNET DIKIRVNKFY RPENTHKSTP
ASYHADINLL YWSDEEAVVD FKAVQGRCTV EYGEDLPECV QVYSMGGPNR FYFLEAYNAK
SKSFEDPPNH ARSPGNKGKG KGKGKGKPKS QACEPSEPEM EIKLPKLRTL DVFSGCGGLS
EGFHQAGISD TLWAIEMWDP AAQAFRLNNP GSTVFTEDCN ILLKLVMAGE TTNSRGQRLP
QKGDVEMLCG GPPCQGFSGM NRFNSRTYSK FKNSLVVSFL SYCDYYRPRF FLLENVRNFV
SFKRSMVLKL TLRCLVRMGY QCTFGVLQAG QYGVAQTRRR AIILAAAPGE KLPLFPEPLH
VFAPRACQLS VVVDDKKFVS NITRLSSGPF RTITVRDTMS DLPEVRNGAS ALEISYNGEP
QSWFQRQLRG TQYQPILRDH ICKDMSALVA ARMRHIPLAP GSDWRDLPNI EVRLSDGTMA
RKLRYTHHDR KNGRSSSGAL RGVCSCVEGG ASGKACDPAA RQFNTLIPWC LPHTGNRHNH
WAGLYGRLEW DGFFSTTVTN PEPMGKQGRV LHPEQHRVVS VRECARSQGF PDTYRLFGNI
LDKHRQVGNA VPPPLAKAIG LEIKLCMLAK ARESASGMVG WAGLPLGPDC PLGVHAGAVA
GHRSGLWDSG GSPTHLRGPI FLEGLL
//
