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Database: UniProt
Entry: A0A072VMY4_MEDTR
LinkDB: A0A072VMY4_MEDTR
Original site: A0A072VMY4_MEDTR 
ID   A0A072VMY4_MEDTR        Unreviewed;       821 AA.
AC   A0A072VMY4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 48.
DE   SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|EMBL:KEH43202.1};
GN   Name=11427647 {ECO:0000313|EnsemblPlants:KEH43202};
GN   OrderedLocusNames=MTR_1g086980 {ECO:0000313|EMBL:KEH43202.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH43202.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH43202.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH43202.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH43202,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:KEH43202.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH43202.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH43202,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:KEH43202}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH43202};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC         COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC         Evidence={ECO:0000256|ARBA:ARBA00000090};
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DR   EMBL; CM001217; KEH43202.1; -; Genomic_DNA.
DR   RefSeq; XP_013469164.1; XM_013613710.1.
DR   AlphaFoldDB; A0A072VMY4; -.
DR   EnsemblPlants; KEH43202; KEH43202; MTR_1g086980.
DR   GeneID; 11427647; -.
DR   Gramene; KEH43202; KEH43202; MTR_1g086980.
DR   KEGG; mtr:11427647; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000002051; Chromosome 1.
DR   ExpressionAtlas; A0A072VMY4; differential.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10519; SET_EZH; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR045318; EZH1/2-like.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_plant.
DR   InterPro; IPR041355; Pre-SET_CXC.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   PANTHER; PTHR45747:SF14; HISTONE-LYSINE N-METHYLTRANSFERASE EZA1; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS51576; SAM_MT43_EZ; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          559..658
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          672..787
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  92521 MW;  D5FA7006575AC252 CRC64;
     MVSDSPHNLH RELVEEPPND DVGTLSNKIN QLKKQIQAER IQSIKEKLQR NQKKLQCHTS
     GIMSAVSTRD SSQTEENTTR SILSSRMDRP LCKFYGFTQG PGDRNQGNQD MSSATSIKIP
     RMERLPPYTS WIFLDRNQRM ADDQSVVGRR RIYYDQRGSE ALICSDSEEE LTEPDGEKHE
     FCDAEDRILC MAFEEHGLNE EVLNVVSKYV GGTSLEIQER YKSIRGSNIG RLDQHPKSSG
     EHEFPMSMYL EKNLSDALDS LDNLFCRRCL IFDCRLHGCS QPLIYPSEKK TVWSEPVGDR
     KPCGDQCYLQ FKVVKSFSKD STPGSFRDKK TTIVEETDGI LSPSSAEEPG SQSTTLPTRT
     DCHGYINLND PDSENLSKRK VTNQSDTAQC DSRSLPDSQD SCKKLKRISD VVTVITDNSQ
     SLHLDGPKAV TNVTELKNSL NSMEEQVDGI LGFSDWKPLE KELYLKGVEM FGRNSCLIAR
     NLLSGSKTCM EISSYMHDGG MSMPHRSIIS AGSIMDDKGK FDTECTDQDM PSRPRLLRKR
     GKTRKFKYSW KSAGHPTIWK RIADGKNQSC MQYTPCGCQS MCGKDCSCLN GGTCCEKYCG
     CSKSCKNRFR GCHCAKSQCR SRQCPCFAAG RECDPDVCRN CWVSCGDGTL GEPHRRGEGQ
     CGNMRLLLRQ QQRIILGKSD VSGWGAFLKN PVNKNDYLGE YTGELISHRE ADKRGKIYDR
     ANSSFLFDLN EQYVLDAYRK GDKLKFANHS SNPNCYAKVM LVAGDHRVGI FAKEHIDAGE
     ELFYDYCYGP DQAPPWARKP EGSKRDESAV PQGRAKKHQS H
//
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