DNMT1_PARLI
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 03-AUG-2022, entry version 102.
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 Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.40.50.150; -; 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 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; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 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
