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CMT3_ORYSJ
ID   CMT3_ORYSJ              Reviewed;         907 AA.
AC   C0SQ89; B9G594; Q0IZC8; Q33BI4; Q9AYI4;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase CMT3 {ECO:0000305};
DE            EC=2.1.1.37 {ECO:0000305};
DE   AltName: Full=Chromomethylase 3 {ECO:0000305};
DE   AltName: Full=OsCMT3a {ECO:0000303|PubMed:26243209};
GN   Name=CMT3 {ECO:0000305};
GN   OrderedLocusNames=Os10g0104900 {ECO:0000312|EMBL:BAT09590.1},
GN   LOC_Os10g01570 {ECO:0000312|EMBL:ABB46585.2};
GN   ORFNames=OsJ_30466 {ECO:0000312|EMBL:EEE50451.1},
GN   OSJNBa0071K19.14 {ECO:0000312|EMBL:AAL75760.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=26243209; DOI=10.1111/tpj.12952;
RA   Cheng C., Tarutani Y., Miyao A., Ito T., Yamazaki M., Sakai H., Fukai E.,
RA   Hirochika H.;
RT   "Loss of function mutations in the rice chromomethylase OsCMT3a cause a
RT   burst of transposition.";
RL   Plant J. 83:1069-1081(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=19788421; DOI=10.1111/j.1742-4658.2009.07338.x;
RA   Sharma R., Mohan Singh R.K., Malik G., Deveshwar P., Tyagi A.K., Kapoor S.,
RA   Kapoor M.;
RT   "Rice cytosine DNA methyltransferases - gene expression profiling during
RT   reproductive development and abiotic stress.";
RL   FEBS J. 276:6301-6311(2009).
CC   -!- FUNCTION: Involved in CpXpG DNA methylation. Plays a critical role in
CC       the maintenance of CpXpG DNA methylation and suppression of a wide
CC       spectrum of transposable element (TE) activities. Required for proper
CC       plant development in reproductive stage. {ECO:0000269|PubMed:26243209}.
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:0000305};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: Down-regulated by salt and dehydration stresses.
CC       {ECO:0000269|PubMed:19788421}.
CC   -!- DISRUPTION PHENOTYPE: Reduced overall plant height, early flowering and
CC       reduced fertility. {ECO:0000269|PubMed:26243209}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL75760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABB46585.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF25937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAT09590.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB360583; BAH37019.1; -; Genomic_DNA.
DR   EMBL; AC069324; AAL75760.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000086; ABB46585.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008216; BAF25937.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014966; BAT09590.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000147; EEE50451.1; -; Genomic_DNA.
DR   RefSeq; XP_015613201.1; XM_015757715.1.
DR   AlphaFoldDB; C0SQ89; -.
DR   SMR; C0SQ89; -.
DR   STRING; 4530.OS10T0104900-01; -.
DR   PRIDE; C0SQ89; -.
DR   EnsemblPlants; Os10t0104900-01; Os10t0104900-01; Os10g0104900.
DR   GeneID; 4347954; -.
DR   Gramene; Os10t0104900-01; Os10t0104900-01; Os10g0104900.
DR   KEGG; osa:4347954; -.
DR   eggNOG; ENOG502QW29; Eukaryota.
DR   OrthoDB; 898916at2759; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000007752; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
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:0032776; P:DNA methylation on cytosine; IMP:UniProtKB.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..907
FT                   /note="DNA (cytosine-5)-methyltransferase CMT3"
FT                   /id="PRO_0000438158"
FT   DOMAIN          172..297
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          335..868
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   DOMAIN          437..500
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   REGION          1..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..89
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   CONFLICT        99
FT                   /note="A -> P (in Ref. 6; EEE50451)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   907 AA;  101415 MW;  90EF5B0E0DD151CF CRC64;
     MAPSSPSSAA APTRTSTRKR AASASASAKA TDEPSTKRTR RPKAETKPRK KKDEVKEEEK
     PPMEDDACGE EPDAEEMALG EEAEAEEAEA EQKQLDAPAP GVARKRVAQP SRVRHGSDGD
     HDPEFVGDPF PAKEARDKWP QRYQRNAATR RPDEEEDIKA RCHYSSAKVD GTLYCLHDDV
     YVKAEEDKAD YIGRITEFFE GTDHCHYFTC RWFFRAEDTV ISSIMMENAD DEKHDLKRVF
     LSEEKNDNVL DCIISKVKIV YIDPNMESEA KARRLADCDL YYDMSYTVAY STFANIPLEN
     GASGSDTASD ISSDDVDSSK GKVVSDSEAS SVGKATLLDL YSGCGGMSTG LCLGAALAGL
     NLETRWAVDF NSFACESLKY NHPRTEVRNE KADEFLALLK GWHSLCDEYV KKDIDFSSAG
     ASENEEDDDE PLEKDEFVVE KLAGICYGGS GREDGLYFKV QWKGYGREED TWEPIENLRD
     CPLKIKEFVQ EGYRRKILPL PGDVDVICGG PPCQGISGFN RFRNRKEPLK DEKNKQMVTF
     MDIVAYLKPK YVLMENVVDI LKFADGYLGR YALSRLVAMK YQARLGMMVA GCYGLPQFRM
     RVFLWGALPT MVLPKYPLPT HNVVVRGGAP NAFSQSIVAY DETQKPTLKN ALLLGDAISD
     LPEVNNHQPN EVMEYGSSPK TEFQRYIRLS RKEMLDSSFE GKDGPDLGKL LDHQPLKLNK
     DDHERVQQIP VKKGANFRDL KGVRVGANNI VEWDPDVPRV YLSSGKPLVP DYAMSFIKGR
     SLKPFGRLWW DETVPTVVTR AEPHNQIILH PNQARVLTVR ENARLQGFPD YYKMFGPIKE
     KYIQVGNAVA VPVARALGYS LGLAYQRESE GSSPLFVLPD SFTEVGRQAA PARASSVGIP
     VGEVVEQ
 
 
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