DNMT1_CHICK
ID DNMT1_CHICK Reviewed; 1537 AA.
AC Q92072;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE Short=Dnmt1;
DE EC=2.1.1.37;
DE AltName: Full=DNA methyltransferase GgaI;
DE Short=DNA MTase GgaI;
DE Short=M.GgaI;
DE AltName: Full=MCMT;
GN Name=DNMT1; Synonyms=AIM, DNMT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8586618; DOI=10.1093/oxfordjournals.jbchem.a124805;
RA Tajima S., Tsuda H., Wakabayashi N., Asaso A., Mizuno S., Nishimori K.;
RT "Isolation and expression of a chicken DNA methyltransferase cDNA.";
RL J. Biochem. 117:1050-1057(1995).
RN [2]
RP INTERACTION WITH PCNA, AND MUTAGENESIS OF VAL-190.
RX PubMed=9302295; DOI=10.1126/science.277.5334.1996;
RA Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
RT "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
RT p21WAF1.";
RL Science 277:1996-2000(1997).
CC -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC hemimethylated DNA. It is responsible for maintaining methylation
CC patterns established in development. Mediates transcriptional
CC repression by direct binding to HDAC2. Plays a role in promoter
CC hypermethylation and transcriptional silencing of tumor suppressor
CC genes (TSGs) or other tumor-related genes. Also required to maintain a
CC transcriptionally repressive state of genes in undifferentiated
CC embryonic stem cells (ESCs). Associates at promoter regions of tumor
CC suppressor genes (TSGs) leading to their gene silencing.
CC {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}.
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 -!- SUBUNIT: Homodimer (By similarity). Interacts with PCNA
CC (PubMed:9302295). {ECO:0000250|UniProtKB:P26358,
CC ECO:0000269|PubMed:9302295}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis and lung.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; D43920; BAA07867.1; -; mRNA.
DR PIR; JC4172; JC4172.
DR RefSeq; NP_996835.1; NM_206952.1.
DR AlphaFoldDB; Q92072; -.
DR SMR; Q92072; -.
DR STRING; 9031.ENSGALP00000043396; -.
DR REBASE; 3020; M.GgaDnmt1.
DR GeneID; 396011; -.
DR KEGG; gga:396011; -.
DR CTD; 1786; -.
DR VEuPathDB; HostDB:geneid_396011; -.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR InParanoid; Q92072; -.
DR OrthoDB; 898916at2759; -.
DR PhylomeDB; Q92072; -.
DR PRO; PR:Q92072; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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 SUPFAM; SSF53335; SSF53335; 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 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1537
FT /note="DNA (cytosine-5)-methyltransferase 1"
FT /id="PRO_0000088037"
FT DOMAIN 8..105
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT DOMAIN 667..791
FT /note="BAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 883..1011
FT /note="BAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REPEAT 1020..1021
FT /note="1"
FT REPEAT 1022..1023
FT /note="2"
FT REPEAT 1024..1025
FT /note="3"
FT REPEAT 1026..1027
FT /note="4"
FT REPEAT 1028..1029
FT /note="5"
FT REPEAT 1030..1031
FT /note="6"
FT REPEAT 1032..1033
FT /note="7"
FT REPEAT 1034..1035
FT /note="8; approximate"
FT DOMAIN 1054..1513
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ZN_FING 558..604
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..194
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000269|PubMed:9302295"
FT REGION 614..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1035
FT /note="8 X 2 AA tandem repeats of K-G"
FT REGION 1518..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1061
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1065..1066
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1083..1084
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1105..1106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1494
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT SITE 420
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MUTAGEN 190
FT /note="V->H: No loss of interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:9302295"
SQ SEQUENCE 1537 AA; 172907 MW; FB7E0B2CD10EA17E CRC64;
MPARSAPPPP ALPPALRRRL RDLERDEDSL SEKETLQEKL RLTRGFLRAE VQRRLSALDA
DVRCRELSEE RYLAKVKALL RRELAAENGD AAKLFSRASN GCAGNGEEEW ERGGRGEDGA
MEVEEAAASS SSSSSSSSSS SSSSSSSSSL LPAPRARKAR RSRSNGESKK SPASSRVTRS
SGRQPTILSV FSKGSTKRKS EEVNGAVKPE VSAEKDEEEE EELEEKEQDE KRIKIETKEG
SEIKDEITQV KTSTPAKTTP PKCVDCRQYL DDPDLKFFQG DPDDALEEPE MLTDERLSIF
DANEDGFESY EDLPQHKVTS FSVYDKRGHL CPFDTGLIER NIELYFSGAV KPIYDDNPCL
DGGVRAKKLG PINAWWITGF DGGEKALIGF TTAFADYILM EPSEEYAPIF ALMQEKIYMS
KIVVEFLQNN RDVSYEDLLN KIETTVPPVG LNFNRFTEDS LLRHAQFVVE QVESYDEAGD
SDEPPVLITP CMRDLIKLAG VTLGKRRAVR RQAIRHPTRI DKDKGPTKAT TTKLVYLIFD
TFFSEQIEKD EREDDKENAM KRRRCGVCEV CQQPECGKCK ACQNMVKFGG SGRSKQACLQ
RRCPNLAVRE ADEDEEVDDN IPEMPSPKKM LQGRKKKQNK SRISWVGEPI KSDGKKDFYQ
RVCIDSETLE VGDCVSVSPD DPTKPLYLAR VTAMWEDSSG QMFHAHWFCP GSDTVLGATS
DPLELFLVDE CEDMQLSYIH GKVNVIYKPP SENWAMEGGL DMEIKMVEDD GRTYFYQMWY
DQEYARFETP PRAQPMEDNK YKFCLSCARL DEVRHKEIPK VAEPLDEGDG KMFYAMATKN
GVQYRVGDSV YLLPEAFSFS MKPASPAKRP KKEAVDEDLY PEHYRKYSEY IKGSNLDAPD
PYRVGRIKEI FCHIRTNGKP NEADIKLRIW KFYRPENTHK SMKATYHADI NLLYWSDEET
TVDFCAVQGR CTVVYGEDLT ESIQDYSAGG LDRFYFLEAY NAKTKSFEDP PNHARSSGNK
GKGKGKGKGK GKGKSSTTCE QSEPEPTELK LPKLRTLDVF SGCGGLSEGF HQAGVSETLW
AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL KLVMSGEKTN SLGQKLPQKG DVEMLCGGPP
CQGFSGMNRF NSRTYSKFKN SLVVSFLSYC DYYRPRFFLL ENVRNFVSFK RSMVLKLTLR
CLVRMGYQCT FGVLQAGQYG VAQTRRRAIV LAAAPGEKLP MFPEPLHVFA PRACQLSVVV
DDKKFVSNIT RTYSGPFRTI TVRDTMSDLP EIRNGASALE ISYNGEPQSW FQRQIRGSQY
QPILRDHICK DMSALVAARM RHIPLAPGSD WRDLPNIEVR LSDGTSTRKL RYTHHEKKNG
RSSSGALRGV CSCAEGKPCD PADRQFNTLI PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT
VTNPEPMGKQ GRVLHPEQHR VVSVRECARS QGFPDTYRLF GNILDKHRQV GNAVPPPLAK
AIGLEIRACV GARMREESGA AVAPPAPEKM EMTAAAD
