ID DNMT1_PARLI Reviewed; 1612 AA. AC Q27746; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-SEP-2023, entry version 105. DE RecName: Full=DNA (cytosine-5)-methyltransferase PliMCI; DE EC=2.1.1.37; DE AltName: Full=DNA methyltransferase PliMCI; DE Short=DNA MTase PliMCI; DE Short=M.PliMCI; DE AltName: Full=Dnmt1; DE AltName: Full=MCMT; GN Name=DNMT; Synonyms=PLIMCIM; OS Paracentrotus lividus (Common sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea; OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Paracentrotus. OX NCBI_TaxID=7656; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryo; RX PubMed=8921892; DOI=10.1016/0378-1119(96)00334-4; RA Aniello F., Locascio A., Fucci L., Geraci G., Branno M.; RT "Isolation of cDNA clones encoding DNA methyltransferase of sea urchin P. RT lividus: expression during embryonic development."; RL Gene 178:57-61(1996). CC -!- FUNCTION: Methylates CpG residues. 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:0000255|PROSITE-ProRule:PRU10018}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC 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 EMBL; Z50183; CAA90563.1; -; mRNA. DR PIR; JC5210; JC5210. DR AlphaFoldDB; Q27746; -. DR SMR; Q27746; -. DR REBASE; 2961; M.PliMCDnmt1. 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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd04760; BAH_Dnmt1_I; 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 2: Evidence at transcript level; KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Repeat; KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1612 FT /note="DNA (cytosine-5)-methyltransferase PliMCI" FT /id="PRO_0000088038" FT DOMAIN 7..101 FT /note="DMAP1-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260" FT DOMAIN 743..871 FT /note="BAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 967..1089 FT /note="BAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 1131..1590 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT ZN_FING 626..672 FT /note="CXXC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT REGION 87..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 677..708 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1084..1121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..160 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 177..216 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 256..338 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 686..705 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1218 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018" FT BINDING 633 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 636 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 639 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 644 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 647 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 650 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 666 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 671 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 1142..1143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT BINDING 1160..1161 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1182..1183 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT BINDING 1183 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1569 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1571 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" SQ SEQUENCE 1612 AA; 181219 MW; 0CB3853FB565CF50 CRC64; MPSKTICDQV IPPNVRDRVQ ELDGDLNDGL ITEKGYVKKK SKILFEHLSP DIQTKLKGLE DELKDEELTE KGYLNKVQSI LAKFIETCSP VNGDTKEEAS SNGKDDEKAE STVANGTTSN GSTTNGSSGS SKANGHTNGG YVQSSSQEET GTSQSEEEMD MDTPTSGKGG SKKKKKSKGS GGGDAGKGRK RKVLGDDERD GVEKKEGEKK DVEGEEGEEA KEESATPDEK TLRTSKRKRS PKADAKQPSI MSMFTKKPAK KEEEKMEESS SMEVDKKEME NGDNGKKEEE EPSGPGGKRI KKEEEEEEKA KVEPMSPSRD LRHKANHETA ESKQPPLRCK ECRQLLDDPD LKIFPGDPED AREEYITLTD PRLSLLTGDE GDAMSYDERL QHKITNFCVY DKSTHICAFD RGMIEKNKEL YFSGYVKPIY DDNPSTEGGI PTKRIGPINE WYTTGFDGGH KALIGFSTAF AEYIVMSPSE EYKPFWTAVQ EKIYMSKILI EFLQNNVDPV YEDLLTQIET TVPPEGCNRF TEDSLLRHAQ FVVEQVESYD DAADRDEVLL ITMPCMRDLI KLAGVTLGKR RAARKAAAVK KDKKPVFTMA TVTPLVSHIF DAIFKDQIAD EMKAAASERK KRCGVCEICQ APDCGKCTAC KDMIKFGGSG KAKQACKDRR CPNMAVQEAD ENDIDEMDNS SNKENKDEKK AKKGRKLETP LKKKKRAKVT WLDEPTEVTE ERAYYKAAML DDEKIEIGDC VLIHPDDPTK PLFMARVIYM WQESQGEMMF HAQWFVYGSE TVLGETSDPL EVFPIDECQD TYLGSVNAKC TVIYKAPPND WSMIGGIDDP ETDHVIKEDD GKTFFYQKWY DPELARFEDY EVLMAPDDIP AHRFCSCCLK NERAQEKETA RPGAKLEDQD DSSKVLYSSW HYKGNEFQIG DGVYLLPEVF SFNIKQKVVT KKPVSKKDVD EDLYPENYRK SSEYVKGSNL ECPEPFRIGK IISIYTTKSN STVRLRVNKM YRPEDTHKGR TAAYQADLNV LYWSEEEAVT ELEVVQGKCS VVCAEDLNVS TDEYSAGGPH KFYFREAYDS ERKCFEDPPS KSRSTRMKGK GKGKGKGKAK GKIAVEKEEE KESTETPFNK LKCLDVFAGC GGLSEGFHQA GICESSWAIE KEEPAAQAYR LNNPGSTVFS DDCNELLRLV MQGEKTSRTG QKLPQKGDVE LLCGGPPCQG FSGMNRFNSR EYSKFKNSLI SSYLSYCDYY RPRFFLLENV RNFVSYKKNM VLKLALRCLI RMGYQCTFGI LQAGQYGVPQ TRRRAIILAA APGEKLPFYP EPLHVFSSRA CSLSVMIGEK KIESNNQWCL SAPYRTITVR DTMSDLPTIN NGAQKLEISY DGEPQSDFQK KIRGNQYQPI LRDHICKDMS SLVAARMKHI PLAPGSDWRD LPNIPVTLKD GTTCRKLRYT HKDKKNGKSS TGALRGVCSC AEGDACDPSD RQFSTLIPWC LPHTGNRHNN WAGLYGRLEW DGFFSTTVTN PEPMGKQGRV LHPEQHRVVS VRECARSQGF PDTYRFFGSI LDKHRQIGNA VPPPMAAAIG MEIKVCLQTK TKRDQERAAL EPVKEETEES MD //