ID A0A1S3GML1_DIPOR Unreviewed; 1610 AA.
AC A0A1S3GML1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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|RefSeq:XP_012889489.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012889489.1};
RN [1] {ECO:0000313|RefSeq:XP_012889489.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012889489.1};
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|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 RefSeq; XP_012889489.1; XM_013034035.1.
DR STRING; 10020.ENSDORP00000013274; -.
DR GeneID; 105999111; -.
DR KEGG; dord:105999111; -.
DR CTD; 1786; -.
DR InParanoid; A0A1S3GML1; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 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; 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:UP000081671};
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 636..682
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 745..871
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 963..1091
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 96..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1217
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 343
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 1610 AA; 181680 MW; 725603E669599D55 CRC64;
MPARTAPARV PALATPAISL PEDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHTFS RQTNGYLENR NREGRRRGMT
EPNTPPTPTS KARTPRRSKT DLETKPETPS SSVVTRRTTR QTSITSHFSK APTKRKPLEE
SESLKSEPES MEEEEHDQEE KRRRVTSMES GAESAAAEAE TAPEAAGDPE MSIKEESLES
PVQQLTPKLE EPDREASPGT DAQMEEDDPD VKDEKKPKSQ LRDVTPKRKT RPEKRPTPHT
SASRATRESD EKRSKTKEIA EKKETGTKAM LNLKPQEPRC SECGQYLDDL DLKYEQHPHD
ALEEPQMLTN EKLSIFDDTN ESGFESYEAL PQHKLTGFSV YCKRGHLCPI DTGLIEKNVE
LFFSGSAKAI YEDNPSLEGG VNGKHLGPIN EWWITGFDGG EKVLMGFSTA FAEYILMDPS
PEYAPIFGQM QEKVYISKIV VEFLLGNPDA TYEDLINKIE TTVPPSGLNL NHFTEDSLLR
HAQFVVGQVE SYDRAKDTDE EPIYLSPCMR ALIKLCGVTL GQRRAVSSRS MKPPAKDKDK
GPTKATTTKL VYQIFDTFFA EQIEKDERAD REDKENNSKR RRCGVCEVCQ QPECGVCRAC
MDMVKFGGSG RSKQACVQRR CPNLAMKEAE EDEEVDDNIP EMPSPKKMHQ AKKKKQNKAR
ISWVGPAIKV EGKKTFYQKV CIDEETLEVG DCVSVIPDDS SKPLYLARAT ALWEDGSGKM
FHAHWFCAGS DTVLGATSDP RELFLVDECE DMQLSYVHSK VTVIHKPPSP NWAMEGGLEP
EDMLLGEVND GKTYFYQLWY DQDYARFESP PKMQPTEDNK HKFCVSCARL AEMRQKEIPR
VLEQVDELDN RFFYSSATKN GVVYRVGDGV YLPPEAFAFN IKLSSPVKRP KKEPVNEHLY
PEHYRKYSDY IKGSNLDAPE PYRIGRIKEI FCTKKSNGKP NEADIKIRVY KFYRPENTHK
STPASYHADI NMLYWSDEEA VVDFKAAQGR CTVEYGEDLP ECVQEYSARG PDRFYFIEAY
NAKSKSFEDP PNHARSPGNK GKGKGKGKSK AKPAPAPEPS EPEAGKLPKL RTLDVFSGCG
GLSEGFHQAG ISETLWAIEM WEPAAQAFRL NNPASTVFTE DCNVLLKLVM AGEVANALGQ
RLPQKGDVEM LCGGPPCQGF SGMNRFNSRT YSKFKNSLVV SFLSYCDYYR PRFFLLENVR
NFVSFKRSMV LKLTLRCLVR MGYQCTFGVL QAGQYGVAQT RRRAIILAAA PGEQLPLFPE
PLHVFAPRAC QLSVVVDDKK FVSNITRLSS GPYRTITVRD TMSDLPEIQN GASASEISYN
GEPQSWFQRQ LRGSHYQPIL RDHICKDMSP LVAARMRHIP LAPGSDWRDL PNIEVRLSDN
TVTKKLRYNY HDRKHGRSRS GALRGVCSCV QAGTPCDPLA RQFNTLIPWC LPHTGNRHNH
WAGLYGRLEW DGFFSTTVTN PEPMGKQGRV LHPEQHRVVS VRECARSQGF PDTYRLFGNI
LDRHRQVGNA VPPPLAKAIG LEIKQCLLAK ARESASAQVK EEEEEKATQG
//
