ID G3PKP2_GASAC Unreviewed; 1506 AA.
AC G3PKP2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018172.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000018172.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000018172.1}
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}.
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DR STRING; 69293.ENSGACP00000018172; -.
DR Ensembl; ENSGACT00000018207.1; ENSGACP00000018172.1; ENSGACG00000013741.1.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR GeneTree; ENSGT00390000005100; -.
DR InParanoid; G3PKP2; -.
DR OMA; EKHRQVG; -.
DR TreeFam; TF328926; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000013741; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051718; F:DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0035622; P:intrahepatic bile duct development; IEA:Ensembl.
DR GO; GO:0070121; P:Kupffer's vesicle development; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; 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; 2.
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 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:UP000007635};
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};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 8..105
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 529..575
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 638..762
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 857..984
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 85..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1115
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1506 AA; 169560 MW; 447C61430F105420 CRC64;
PFVMPSKTSL SLPEDVRKRL QVLDEDGSSG EDHVKEKLKL VQNFLHVDAQ DQLNSLEEKM
KSSEMSMDVY LSKVKALLGK ELNHENGSHV DSVEHNGKTV LSNGSHKDEH SEDVTMEEEE
EAVKSPTASK GKGGRKSKTN SDNTKSPAST RVTRNAGKQP TIMSMFSKVS QKRKSEDLNG
DAANGENEGK KEEDDAEATR EEKRLKVESD ETAAPEKSES EITKPVSAAK TPPPKCTDCR
QYLDDSDLKF FQGDPDTALD EPEMLTDERL SLFDSNEDGF ESYDDLPQHK ITNFSVYDKR
GHLCPFDSGL IEKNVELYFS CVVKPIYDDN PCLDGGVPAK KLGPINAWWI TGFDGGEKAL
IGFTTAFADY ILMQSSEEYA PIFAVMQEKI YMSKIVVEFL QKNPDASYED LLNKIETTVP
PAGLNFNCFT EDTLLRHAQF VVEQVESYDE AGDSDEQPII VTPCMRDLIK LAGVTLGKRR
AARRQAIRHP TKIEKDNKGP TKATTTTLVY QIFDTFFSEQ IEQNDKDSAG AKRQRCGVCE
VCQAPDCGKC PACKDMIKFG GGGKSKQACK QRRCPNLAVK EAEDDEIVEE EDVPVEKPKK
VSHPKRKKQT QCKLSWIGET VQTEGKKRYY QKVCVNDEVL EVGDCVSVSS EDPSLPLYLA
RIASMWEDTN EKMFHAHWFH RGTQTVLGES SDPLELVMVD ECEDMLLNYV QSKVNVMYKA
PSDNWFMEGG MDLEIKVIDD DGKSFFYQFW YDTDCARFET PPKTSPTEDS KFTFCLSCVR
AAEREERERP RAFEPIVDKD HDSKVLYALA CFQGEQFKVG DSVYMHPDAF NFSVKPASPV
KRSHRKEDVD EDLYPEYYRK SSDYIKGSNL DAPEPFRVGR IKEIFCQRRN GKCDTSEVKL
RLYKFYRPEN THKGVKASYH ADINQLYWSD EEVTVNMAEL LGRCQVEYAE DLNESVQDYS
SGGTDRFYFL EAYNAKSKSF EDPPNHARSA VHKGKGKGKG KGKGKGKAAA QEQQDSQNEP
QAVKVPKYRA LDVFSGCGGL SEGFHQAGMT ETLWAIEMWE PAAQAFRLNN PGTTVFTEDC
NVLLKLVMSG EKTNSLGQKL PQKGDVEMLC GGPPCQGFSG MNRFNSRTYS KFKNSLVVSY
LSYCDYYRPK FFLLENVRNF VSFKSSMVLK LTLRCLVRMG YQCTFGVLQA GQYGVAQTRR
RAIILAAAPG EKLPRYPEPL HVFAPRACSL SVVVDEKRHV SNVTRGNGGI YRTITVRDTM
SDLPEIRNGA AGLEISYNGE PQSWFQRQIR GTQYQPILRD HICKDMSALV EGRMRHIPLA
PGSDWRDLPN LEVRLKDGTM TKKLRYSHSD KKNGRSSTGA LRGVCTCSGG TPCDPADRQF
GTLIPWCLPH TGNRHNHWAG LYGRLEWDGF FSTTVTNPEP MGKQGRVLHP EQHRVVSVRE
CARSQGFPDT YRFFGNILDK HRQVGNAVPP PLSRAIGLEL KKCVLERMKE EQATDAVKQE
KIEASD
//
