ID F6QS51_HORSE Unreviewed; 1667 AA.
AC F6QS51;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 74.
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|VGNC:VGNC:17255};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000022889.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000022889.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000022889.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000022889.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000022889.4};
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}.
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DR Ensembl; ENSECAT00000029086.4; ENSECAP00000022889.4; ENSECAG00000026909.4.
DR VGNC; VGNC:17255; DNMT1.
DR GeneTree; ENSGT00390000005100; -.
DR HOGENOM; CLU_003040_0_0_1; -.
DR TreeFam; TF328926; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000026909; Expressed in bone marrow and 23 other cell types or tissues.
DR ExpressionAtlas; F6QS51; baseline.
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 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:UP000002281};
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 69..162
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 697..743
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 806..931
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1023..1151
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 149..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1277
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
SQ SEQUENCE 1667 AA; 187998 MW; 703A707E765FA442 CRC64;
MVRPLSAWYV PPSPTPRPGW YAPPPLAAPP RRFPRARKAR AARAAAASAA VSKMPARTAP
ARVPALASRA FSLPDDVRRR LKDLERDSLT EKECVKEKLN LLHEFLQTEI KNQLCDLETK
LHKEELSEEG YLAKVTSLLN KDLSSENGAP AFSREVNGCL GNGSQARGED RRVSMAEENK
SPKLVSKLGT PRRSRGDGEP KAEVSSSPRI TRQTTRQTTI TSHFARGPAK RKPEEELERA
KADNSVDEEK DQEEKRRRVT SREPVARPLP AEEPDRVRPG THTEEEEERE DREEKRVRSQ
TKEPTPKQKP KEEPDREARP GAQAEVDEGG EERDEKRHRS QPKDLAAKRR PEEKEPERVK
PQVSDEKDED EKEEKRRKTT SKEPMEKKMA RTKTVLSSKI HPPRCVQCGQ YLDDAELKYE
QHAPDAVDEI QLLTNERLSI FDANESGFES YEALPQHKLT CFSVYCKRGH LCPIDTGLIE
KNVELFFSGS AKPIYDDDPS LEGGVNGKDL GPINEWWITG FDGGEKALIG FSTSFAEYIL
MDPNPEYAPM FSVMQEKIYI SKIVVEFLQS NPDSTYEDLI NKIETTVPPS VLNLNRFTED
SLLRHAQFVV EQVESYDEAG DSDEQPIFLT PCMRDLIKLA GVTLGKRRAE RRQTIGHSAK
EKDKGPTKAT TTKLVYQIFD TFFAEQIEKD DREDKENAFK RRRCGVCEVC QQPECGKCKA
CKDMVKFGGS GRSKQACQER RCPNMAMKEA DDDEEVDDNI PEMPSPKKMH QGKKKKQNKN
RITWVGDAVK TDGKKSFYKQ VCIDSETLEV GDCVSVIPDD SSKPLYLARV TALWEDSSNG
QMFHAHWFCA GTDTVLGATS DPLELFLVDE CEDMQLSYIH SKVKVVYKAP SENWALEGGM
DPEALMAEDD GKTYFYQLWY DQDYARFESP PKTQPTEDNK YKFCASCARL AEMRQKEIPR
VLEQLEDLDG RVLYSSATKD GVQYRVGDGV YLLPEAFTFN IKLSSPVKRP RKEPVDEDLY
PEHYRKYSDY IKGSNLDAPE PYRIGRIKEI FCIKKSNGRP NETDIKIRLN KFYRPENTHK
STPATYHADI NLLYWSDEEA VVDFKAVQGR CTVEYSEDLP ECLQAFSAGG PDRFYFLEAY
NAKSKSFEDP PNHARSPGNK GKGKGKGKGK AKSQVCEPSE PKAEIKLPKL RTLDVFSGCG
GLSEGFHQAG ISETLWAIEM WDPAAQAFRL NNPGSTVFTE DCNVLLKLVM AGEVTNSRGQ
KLPQKGDVEM LCGGPPCQGF SGMNRFNSRT YSKFKNSLVV SFLSYCDYYR PRYFLLENVR
NFVSFKRSMV LKLTLRCLVR MGYQCTFGVL QAGQYGVAQT RRRAIILAAA PGEKLPLFPE
PLHVFAPRAC QLSVVVDDRK FVSNITRLSS GPFRTITVRD TMSDLPEVRN GASALEISYN
GEPQSWFQRQ LRGSQYQPIL RDHICKDMSA LVAARMRHIP LAPGSDWRDL PNIEVRLSDG
TMARKLRYTY HDRKNGRSST GALRGVCSCV EAGKACDSAA RQFNTLIPWC LPHTGNRHNH
WAGLYGRLEW DGFFSTTVTN PEPMGKQGRV LHPEQHRVVS VRECARSQGF PDTYRLFGNI
LDKHRQVGNA VPPPLAKAIG LEIKRCMLAK AQESASGGAA GAAAGLL
//
