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DNMT3_ARATH
ID   DNMT3_ARATH             Reviewed;        1404 AA.
AC   Q9T0I1;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 3;
DE            EC=2.1.1.37;
DE   AltName: Full=DNA methyltransferase 3;
DE   AltName: Full=DNA methyltransferase III;
DE   AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 57;
GN   Name=MET3; Synonyms=MEE57, METIII; OrderedLocusNames=At4g13610;
GN   ORFNames=T6G15.160;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10579493; DOI=10.1023/a:1006347010369;
RA   Genger R.K., Kovac K.A., Dennis E.S., Peacock W.J., Finnegan E.J.;
RT   "Multiple DNA methyltransferase genes in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 41:269-278(1999).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA   Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21257907; DOI=10.1073/pnas.1019273108;
RA   Hsieh T.-F., Shin J., Uzawa R., Silva P., Cohen S., Bauer M.J.,
RA   Hashimoto M., Kirkbride R.C., Harada J.J., Zilberman D., Fischer R.L.;
RT   "Regulation of imprinted gene expression in Arabidopsis endosperm.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1755-1762(2011).
CC   -!- FUNCTION: Maintains chromatin CpG methylation that plays a role in
CC       genomic imprinting, regulation of embryogenesis and seed viability.
CC       Required for proper patterns of CG DNA methylation in dividing cells
CC       (By similarity). Required during the endosperm development in seeds.
CC       {ECO:0000250, ECO:0000269|PubMed:15634699}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Endosperm development arrested.
CC       {ECO:0000269|PubMed:15634699}.
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; AL049656; CAB41119.1; -; Genomic_DNA.
DR   EMBL; AL161537; CAB78403.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83302.1; -; Genomic_DNA.
DR   PIR; T06663; T06663.
DR   RefSeq; NP_193097.1; NM_117435.1.
DR   AlphaFoldDB; Q9T0I1; -.
DR   SMR; Q9T0I1; -.
DR   STRING; 3702.AT4G13610.1; -.
DR   REBASE; 2839; M.AthMET2.
DR   PaxDb; Q9T0I1; -.
DR   PRIDE; Q9T0I1; -.
DR   EnsemblPlants; AT4G13610.1; AT4G13610.1; AT4G13610.
DR   GeneID; 826994; -.
DR   Gramene; AT4G13610.1; AT4G13610.1; AT4G13610.
DR   KEGG; ath:AT4G13610; -.
DR   Araport; AT4G13610; -.
DR   TAIR; locus:2140892; AT4G13610.
DR   eggNOG; ENOG502QPKK; Eukaryota.
DR   HOGENOM; CLU_002247_0_0_1; -.
DR   InParanoid; Q9T0I1; -.
DR   OMA; KGKCEVM; -.
DR   OrthoDB; 898916at2759; -.
DR   PhylomeDB; Q9T0I1; -.
DR   PRO; PR:Q9T0I1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T0I1; baseline and differential.
DR   Genevisible; Q9T0I1; AT.
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; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
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; IPR017198; DNMT1-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   Pfam; PF12047; DNMT1-RFD; 2.
DR   PIRSF; PIRSF037404; DNMT1; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 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   Chromatin regulator; DNA-binding; Isopeptide bond; Methyltransferase;
KW   Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..1404
FT                   /note="DNA (cytosine-5)-methyltransferase 3"
FT                   /id="PRO_0000430012"
FT   DOMAIN          614..748
FT                   /note="BAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          788..929
FT                   /note="BAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          969..1402
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1085
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
FT   CROSSLNK        486
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:O23273"
SQ   SEQUENCE   1404 AA;  160212 MW;  2FC7B7AA8E5DCAA8 CRC64;
     MKTKAGKQKK RSVDSDDDVS RERRPKRATS GTNFKEKSLR FSEKYETVEA KKEQIVGDDE
     KEEKGVRFQS FGRVENWTIS GYEDGSPVIW ISTVIADYDC RKPSKKYKKL YDYFFEKACA
     CVEVCKNLST NPDTSLKELL AAVVRSMNGR KIFSSGGVIQ EFVISQGEFI YNQLAGLDET
     SKNHETKFVD NRVLVSLRDE SRKIHKAFSN VALRIDESKV LTSDQLMDGG EDEDLKYAKL
     LQEEEHMKSM DRSRNKRSST TSAPNKFYIK INEDEIAHDY PLPSYYKNTK DETDELVLFN
     AGYAVDARNL PCRTLHNWAL YNSDLMLISL EFLPMKPCAD IDVTYLGQIK EWKIDFGEDM
     IFVLLRTDMA WYRLGKPSEQ YAPWFEPILK TVRIGTSILA LLKNETRMAK LSYTDVIKRL
     CGLEENDQAY ISSTFFDVER YVIVHGQIIL QFLTECPDEY IKRCPFVTGL ASKMQDRHHT
     KWIIKKKRKM LQKGENLNLR RGKAPKVSKM KAMQATTTRL INRIWGEFYS IYSPEDPLEE
     IGAEEEFEEV EDVEEEDENE EEDTIQKAIE VQKADTLKKI RGSCKEMEIR WEGEILGETC
     AGEPLYGQAL VGGRKMDVGG AVILEVDDQG ETPLIYFVEY MFESSDNSKK LHGKLLQRGS
     ETVLGTAANE RELFLTNECL TVQLKDIKGT VSFEIRSRPW GHQYKKEHMA ADKLDRARAE
     ERKAKDLPIE YYCKSLYSPE KGGFFSLPRS DMGLGSGFCS SCKIRENEEE RSKTKLNDSK
     TRFLSNGIKY SVGDFVYQIP NYLSKDRGKR RPVFKYGRNV GLRAFVVCQI LDIVDLKEPK
     KGNTTSFEVK VRRFYRPDDV SAEEAYASDI QEVYYSEDTY ILPPEAIKGK CEVMKKTDMP
     LCREYPILDH VYFCDRFYDS SNGCLKKLPY NMMLKFSTIK DDTLLREKKT ETGSAMLLKP
     DEVPKGKRLA TLDIFAGCGG LSYGLEKAGV SDTKWAIEYE EPAAQAFKQN HPKTTVFVDN
     CNVILRISWL RLLINDRAIM EKCGDVDDCI STTEAAELAT KLDENQKSTL PLPGQVDFIS
     GGPPCQGFSR LNRFSDGSWS KNQCQMILAF LSFADYFRPK YFLLENVKTF VSFNEGHTFH
     LTVASLLEMG YQVRFGLLEA GAYGISQPRK RAFIWAAAPN EVLPEWPEPM HVFNNPGFKI
     PLSQGLHYAA VQSTKFGAPF RSITVRDAIG DLPPIESGES KINKEEMRGS MTVLTDHICK
     KMNELNLIRC KKIPKTPGAD WRDLPDEHVN LSNGIVKNIV PNLLNKAKDH NGYKGLYGRL
     DWHGNLPTCI TNLQPMGLVG MCFHPDQDRI ISVRECARSQ GFPDSYKFSG NIKDKHRQVG
     NAVPPPLAFA LGRKLKEALH LRNI
 
 
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