ID C3YZQ2_BRAFL Unreviewed; 1275 AA.
AC C3YZQ2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_204680 {ECO:0000313|EMBL:EEN54323.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN54323.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54323.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN54323.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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|RuleBase:RU000417};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
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; GG666566; EEN54323.1; -; Genomic_DNA.
DR RefSeq; XP_002598311.1; XM_002598265.1.
DR AlphaFoldDB; C3YZQ2; -.
DR STRING; 7739.C3YZQ2; -.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR InParanoid; C3YZQ2; -.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central.
DR CDD; cd04760; BAH_Dnmt1_I; 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; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; 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; 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.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 293..339
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 407..535
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 629..757
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 751..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 886
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN54323.1"
SQ SEQUENCE 1275 AA; 143744 MW; 46CC211E4AEC0BB1 CRC64;
PVKCKECRQL LDDPDLRMFP GDPQEAVDEV EMLTDERLSL LEEDQEYGTY DDRPQHKITN
FSVYDKNTHL CAFDTGLIEK NVELYFSGAV KPIYDENPSA DGGVLAKNVG PINEWWTAGF
DGGENALIGF TTAFAEYIVM QPSEAYAPFM DTMWEKIHMS KLVIEFLVNN QEAAYEDLLN
KIQTTVPPQS LRVTSFSEES LLRHAQFVVE QVENFDLAGD ADEAPLLTTP CMRALIKLAG
VTLGKRRAGR SGIKQPRKVK AKPMRQTKAT TTNLVCSIFD TFFKDQIQDD KAGGPRRRRC
GVCEVCQQAD CGTCVACKDM TKFGGTGKSK QACVNRRCPN MAVQDADDDD DIEDDLDKEF
SSTVGHKRTH FSPRKKVNSK VKISWEGKPI KEEGKKTFYS AVMLEEEKIE TGDCVTVTSE
DPTKPLFIAR VMYMWEDSGG DMMCHVGWFC RGSDTVLGET SDPLEVFLVD ECEDILIQFV
KFKCKVILKT FDKDWFSHGG VEDPDSDYPI KEDDGRTFFC QKWYDPDLAR FEDPPVLEEG
SGHKFCPLCL RLDHSRKSEI PIVGEQLDDT MGDDNKVYYS LCQKGGLEYK IGDDVFLLPD
SFSFSVKVKN STKKASKKDN YDEDLYPEYY RKRGDYVKGS NEECPEPFRI GRIISIYCKR
TVSGIINTHD VRLRVTKFYR PENTHKGKAG SHHTDLNMLY WSDEEAVVDF MSVQGKCQVV
YGEDLDVSVE DWSSKGLHRF YFNEAYNTES KQFEEPPNKA RSGGKKAKGK GKGKGKGKGK
SSEAESKEQQ PPSPAFTKLR MLDVFAGCGG LSEGFHQAGI ADSKWAVEVM EPAAQAYRLN
NPDCTVFTDD CNILLKLVME GATTNSTGQR LPQKGDVELL CGGPPCQGFS GMNRFNSRQY
SQFKNSLVVS FLSYCDFYRP KFFLLENVRN FVSFKSSMVL KLTLRCLIRM GYQCTFGVLQ
AGNYGVAQTR RRAIILAAAP GEKLPMYPEP QHVFSPRACQ LSVMVDEKKY NSNTQWRQSA
PYRTITIRDT MSDLPSIRNG HSATEISYDG EPRSYFQKII RGNQYQPILR DHICKDMNAL
VEARMRHVPL APGSDWRDLP NIVVRLSDGS SSKLLQYTHE DKKNGTSSTG ALRGVCSCAE
GTACDQNDRQ FNTLIPWCLP HTGNRHNHWA GLYGRLEWDG FFSTTVTNPE PMGKQGRVLH
PEQHRVVSVR ECARSQGFPD TYRFYGSILD KHRQVGNAVP PPMAAAIGRE IKKCLEDKAK
KETQTGETKP VSMEA
//
