ID G1LZR6_AILME Unreviewed; 1662 AA.
AC G1LZR6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 71.
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:ENSAMEP00000012576.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000012576.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000012576.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000012576.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 9646.ENSAMEP00000012576; -.
DR Ensembl; ENSAMET00000013111.2; ENSAMEP00000012576.2; ENSAMEG00000011823.2.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR GeneTree; ENSGT00390000005100; -.
DR HOGENOM; CLU_003040_0_0_1; -.
DR InParanoid; G1LZR6; -.
DR TreeFam; TF328926; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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:UP000008912};
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 63..156
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 692..738
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 801..926
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1018..1146
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 153..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1272
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
SQ SEQUENCE 1662 AA; 187721 MW; 369838F0A810C9E3 CRC64;
MVRPAFPHVG AEMVHAASAR RPSPLVSARK ARAASAAGAA VSAAVSKMPA RTAPARVPTL
ASRAISLPDD VRRRLKDLER DSLTEKECVK EKLNLLREFL QTEIKNQLCD LETKLHKEEL
SEEGYLAKVK SLLNKDLSLE NGAHAFSREV NGCLENGSQT SGEDRRVGMT EENKSPKPVS
KLSTPRRSKS DGETKAEASS SSGPRITRQT TRQTTILSHF ARGPAKRKPE EEQEKAKSDD
SPEEEKDQEE KRRRVTSREQ VARPLPAEEP ERVKPGTHME EEEERDEKEE KRLRSQTKEP
TPKPKSKEEP DREGKTGVQA EMAEGDERDE RRPRSQPKDL AAKRRPEEKE PERVKPQVSE
EKDEDEKEEK RRKTTSKEPT EKKMARTKTV MSSKTNLLRC VQCGQYLDDA ELKYEQHPPD
AVDEPQLLTS EKLSIFDANE SGFESYEALP QHKLTCFSVY CKRGHLCPID TGLIEKNVEL
FFSGYAKPIY DDDPSLEGGV NGKNLGPINE WWITGFDGGE KALIGFSTSF AEYILMDPNP
EYAPLFSVMQ EKIYISKIVV EFLQSNPDST YEDLINKIET TVPPSVLNLN RFTEDSLLRH
AQFVVEQVES YDEAGDSDEQ PIFLTPCMRD LIKLAGVTLG KRRAERRRTI GHSAKEKDKG
PTKATTTKLV YQIFDTFFAE QIEKDDREDK ENAFKRRRCG VCEVCQQPEC GQCKACKDMV
KFGGSGRSKQ ACQERRCPNM AMKEADDDEE VDDNIPEMPS PKKMHQGKKK KQNKNRISWV
GDAVKTDGKK NYFKKVCIDS ETLEVGDCVS VIPDDSSKPL YLARVTALWE DSSNGQMFHA
HWFCAGTDTV LGATSDPLEL FLVDECEDMQ LSYIHSKVKV VYKAPSENWA LEGGMDPEAV
MAEDDGKTYF YQLWYDQDYA RFESPPKTQP TEENKYKFCV SCARLAEMRQ KEIPRVLEQI
EDLDTRVLYS SATKNGVQYR VGDGVYLLPE AFTFNIKLSS PVKRPRKEPV DEDLYPEHYR
KYSDYIKGSN LDAPEPYRIG RIKEIFCIKK SNGRPNETDI KIRINKFYRP ENTHKSTPAS
YHADINLLYW SDEEVVVDFK AVQGRCTVEY GEDLPGCLQD FSAGGPDRFY FLEAYNAKNK
SFEDPPNHAR SPGNKGKGKG KGKGRAKSQT CEPSEPEAEI KLPKLRTLDV FSGCGGLSEG
FHQAGISETL WAIEMWDPAA QAFRLNNPGS TVFTEDCNVL LKLVMAGEAT NPRGQKLPQK
GDVEMLCGGP PCQGFSGMNR FNSRTYSKFK NSLVVSFLSY CDYYRPRYFL LENVRNFVSF
KRSMVLKLTL RCLVRMGYQC TFGVLQAGQY GVAQTRRRAI ILAAAPGEKL PLFPEPLHVF
APRACQLSVV VDDKKFVSNI TRLSSGPFRT ITVRDTMSDL PEVRNGASAL EILYNGEPQS
WFQRQLRGSQ YQPILRDHIC KDMSALVAAR MRHIPLAPGS DWRDLPNIEV RLSDGTMARK
LRYTYHDKKN GCSSTGALRG VCSCVEAGKA CDSAARQFNT LIPWCLPHTG NRHNHWAGLY
GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR LFGNILDKHR
QVGNAVPPPL AKAIGLEIKR CMLAKARESA SVKIKEEETT KD
//
