ID M4BTP2_HYAAE Unreviewed; 1490 AA.
AC M4BTP2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 42.
DE RecName: Full=[Histone H3]-lysine(27) N-trimethyltransferase {ECO:0008006|Google:ProtNLM};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP809827, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP809827}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP809827};
RG EnsemblProtists;
RL Submitted (JUN-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; JH597858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 559515.M4BTP2; -.
DR EnsemblProtists; HpaT809827; HpaP809827; HpaG809827.
DR VEuPathDB; FungiDB:HpaG809827; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_253096_0_0_1; -.
DR InParanoid; M4BTP2; -.
DR OMA; NDITAIC; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
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; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 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; PS50280; SET; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1212..1314
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 1334..1451
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 39..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..676
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1490 AA; 167737 MW; 55C7DB82D5FD3E37 CRC64;
MTIPHSSYRL GHSNDCRSLL RCFCATDTHE VIVLFSSSDE ASSGLHRSSR RKLRKKAQLK
PGHHPPLPSS GDARGDTEVR RTRMSSSKSE TSQEIQESKT KVEQPKQLRR PPQLKQAKVA
PTTATGASTR SSRKVRGETQ QIKEAMSFYE LQAQEQMMAR FQAQNRKKAP DKQKEPSSTS
VAAGQAARKS GRLKWKNGVT ASQAKKRAAQ QSHAKKCQKP VFLERIDDEQ YDSVYDKEEE
REQAERVFFT ETSVRREKRL RKQKWETRSG VTWVSESGRK SKDKVSVSRK SGDDHHKSSR
KQQGVRNMDF VTRPKQQQTT AGRKQKQQAF SITRQSDSSQ ADKQESEQES VQESDELSGK
ESEDDEAEVS TLPRYWRQEK VPSQPKLKSK VIFDLSTAVG PTKRSYKNTA SALPPRGFCA
SEASEHIVLD DTSEAGSVTE ISSWELQEQE KMFSRLHAQK KNVSSDVSST DQKKRHYAYG
PTGADRTSGS SCRARMGGYQ KKTHSIPSSS SSFSPPRPRN GFPASGAKFA ADVESTVPPV
EIPTTPVVHS TAWRRLIIGK APPNVIVGTS ASPYAYGFDR PLWTYDTTGV LEEECKFRAV
GLGTATTEVN TENQVSKQLA TIPPSQSEVN VQVRYLVSQE LLRIQKYHVQ RVRHTLKSMR
QQLAEYFRNL QELRSERCRR LRWLEIASKY SRDKPPFEYV VHPETVIYLP NDITAICQSF
TMISIRKNAF VEDDPILRYV PYLGDGQEMV IDNDLYSGTT MSKERQIAVF GEGKELNVIK
PSARDDEILE YVLRVIIEKC GTSEHVFRAL EEAGFSQPRI DYLGMKEQAR ATKVTATRMA
KVKELVAAQQ KSFRDEQSGN TVAGKNVYKA LYNLAQHQWF LQNTSEHQSL GVRLQPPLSV
FESNYANAPE ALGIRDRAAY EGLVEWHRDL FCRRCYSYDC SEHGIQNPQR RARADPVYPM
VIALDVLLAG QETMSRESLV ADECSPKDTT LSVESEEAIV LTGSDSSSSL DDEAQNNTNQ
PILVDQPSSD PAALNRRSRR TQTRISSLAS KSLQSQEKML EIQRLAKLER QRKRREKFSR
APDNSEYLDD SYLPAVTATQ QMLLSETQPC GPFCKLSAGD IGQSDSCEPM RRIDAVLVRK
LAATLGPNAC MLSAMVRSPW CTCAQIFNFL TEEKKRSDSG DYSGNENNLL MATQRQQKGR
HSAVAGLNRS LSKRVREHCS FDHEKKLSYE PCNHEGVCDG TCQCTQRGHS CNKTCSCSRD
CPNRFQGCKC SAGKCYTLAC PCYTAGRECD PDYCFHCGAS DAAVMAFHPT LSSQSCYDLH
ICCNVNMLRN STQKKIGVAF SATHGWGAFA LEPIRRDEFV LEYTGELITD EEAERRGAMY
DRKFVSYLFG VNSEYVVDAA RKGNKAKFAN HRTKKKANMN VKVIVSNGEH RIGLFAREAI
EVGAELFFDY GYTHDSAPIW SHHGRSMSEQ FVYDIIGDEN ELDNALHSSW
//
