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Database: UniProt
Entry: A0A2K1X0G4_POPTR
LinkDB: A0A2K1X0G4_POPTR
Original site: A0A2K1X0G4_POPTR 
ID   A0A2K1X0G4_POPTR        Unreviewed;      1575 AA.
AC   A0A2K1X0G4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE            EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN   ORFNames=POPTR_018G138000 {ECO:0000313|EMBL:PNS94276.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNS94276.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNS94276.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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         ECO:0000256|RuleBase:RU000417};
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,
CC       ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; CM009307; PNS94276.1; -; Genomic_DNA.
DR   SMR; A0A2K1X0G4; -.
DR   STRING; 3694.A0A2K1X0G4; -.
DR   EnsemblPlants; Potri.018G138000.1.v4.1; Potri.018G138000.1.v4.1; Potri.018G138000.v4.1.
DR   Gramene; Potri.018G138000.1.v4.1; Potri.018G138000.1.v4.1; Potri.018G138000.v4.1.
DR   InParanoid; A0A2K1X0G4; -.
DR   OrthoDB; 317994at2759; -.
DR   Proteomes; UP000006729; Chromosome 18.
DR   ExpressionAtlas; A0A2K1X0G4; differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central.
DR   CDD; cd04712; BAH_DCM_I; 1.
DR   CDD; cd04708; BAH_plantDCM_II; 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; IPR017198; DNMT1-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF00145; DNA_methylase; 2.
DR   Pfam; PF12047; DNMT1-RFD; 2.
DR   PIRSF; PIRSF037404; DNMT1; 5.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
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; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
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:UP000006729};
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}.
FT   DOMAIN          779..913
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          953..1092
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..728
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1243
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   1575 AA;  177522 MW;  92AFFF4651260450 CRC64;
     MGSSSILDTT TNDPVDNTIS SSSSVGMRKN KKGKQKSSVS NVKKEVPEKN TKGKKRNSPD
     TNKEEPTGGD GSLKRPKRAA ACKDFKEKSV RLHEEKSYVV ESKKEQVVDE EILAVRLTQG
     QEEGRPNRRL IDFVVHDANG NPQPLEMVEV DDMFISGIIM PHEESLDKEK EVHVRCDGFG
     RIEAWDISGY EDGSPVIWLS TEVADYDCIK PAGGYKKFFD HFFQKALACV EVYKKLSRFS
     GGNPEFTLDE LLAGVVRAMS GNKCFSGAVS IKNFLISQGE FIYHQIIGLD ETSTKNDKKF
     ADLPVLVALR DESRNHGNVL IAKAANSGGN LVIGPESVDG AVVNQSNQSS TTVEEDEDAK
     LARLLQDEEY WQSNMRQKKS RGSVSASNTI YIKINEDEIA NDYPLPAFYK HSNEETDEYI
     AVASDDVIDH PDDLPRRMLH NWSLYNSDSR LISLELLPMK PCEDIDVTIF GSGSMTEDDG
     SGFCLDDGPD QSSSRGLEAQ DDMGLPIFLS AIKEWMIEFG SSMIFISLRT DMAWYRLGKP
     SKQYASWYKP VLKTVKLART IITLLKEQSR VSRLSFADVI RKVSEFKKDH HAYISSDLAA
     VERYVVVHGQ IILQLFAEFP DQKIKKCAFV VGLTRMMEER HHTKWVVNKK AIVQKCHSNL
     NPRAAMDTVA SGASKRKLMQ ATTTRLINRI WGEYYSNYSP EDLKEGNDCD VKEEDELEEQ
     DENEDDDKEV VVEKTLKPYS VFEHCKSHTS QKEVRWDGNP VRKISSGEDI YKQAIVCGQV
     IVVGAAVLVE VDEPDELPAI YFVEYMFETR NGSKMFHGRM MKWGSETVLG NTANDREVFL
     TNECMNYKLQ DVKQTIILEV RKRPWGHHHR KDNANADRID REKAEERKKK GLPLEYYCKS
     LYWPERGAFF TLPFDTMGLG SGVCHSCNLK ISEEDKNISK VNSSQTGFSY KGTEYSVHDF
     VYVSPHQFAV ESGETETFKG GRNVGLKPYA VCQLLEVVPM ETKQSETRST EVKVQRFFRP
     DDISPEKAYC SDIREIYYSE ETHLLSVEVI EGKCEVRKKI DIPTCSAPAI FDHTFFCEHM
     YDPSNGSLKQ LPAHIKSKFS AVSKDGDVAS RKRKGKSKEG ENDTEDDKQL EASPEYRLAT
     LDIFAGCGGL SEGLQQAGVS TTKWAIEYEE PAGEAFKLNH AESLMFINNC NVILRAVMER
     CGDADDCIST SEAAKMASSL DAKVIDGLPL PGQVDFINGG PPCQGFSGMN RFNQSTWSKV
     QCEMILAFLS FADYFRPKYF LLENVRNFVS FNKGQTFRLT IASLLQMGYQ VRFGILEAGA
     YGVSQSRKRA FIWAASPEEI LPEWPEPMHV FAAPELKITL SEKSQYAAVR STAYGAPFRA
     ITVRDTIGDL PDVANGASKT NLEYGNDPIS WFQKKIRGDM VVLTDHISKE MNELNLIRCK
     NIPKRPGADW RDLPDEKVKL STGQMVDLIP WCLPNTAKRH NQWKGLFGRL DWEGNFPTSI
     TDPQPMGKVG MCFHPEQDRI LTVRECARSQ GFPDNYQFFG NIQHKHRQIG NAVPPPLAYA
     LGRKLKEALD SKRQK
//
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