ID W1PFJ4_AMBTC Unreviewed; 2409 AA.
AC W1PFJ4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00017p00244380 {ECO:0000313|EMBL:ERN08747.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN08747.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KI393256; ERN08747.1; -; Genomic_DNA.
DR STRING; 13333.W1PFJ4; -.
DR EnsemblPlants; ERN08747; ERN08747; AMTR_s00017p00244380.
DR Gramene; ERN08747; ERN08747; AMTR_s00017p00244380.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_229200_0_0_1; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046975; F:histone H3K36 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd19172; SET_SETD2; 1.
DR Gene3D; 3.30.40.100; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF07496; zf-CW; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1071..1125
FT /note="CW-type"
FT /evidence="ECO:0000259|PROSITE:PS51050"
FT DOMAIN 1185..1235
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1229..1354
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1362..1378
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 537..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2233..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2344..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2389..2409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1826..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..2003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2173..2198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2233..2261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2304..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2350..2365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2409 AA; 261918 MW; 64F3445A8B7BDA18 CRC64;
MVEFSNDERW SGVEKIEEVL PKGDDFGERL FPEFEHMIDK EYPVCDSHVL LNEEMPMPLL
TVSTSMGSAM ALQEEKKQED SVCINSKEAE PNRPILNMEL EESKPGALIK GSPEMGSCNS
SERFASLVSQ FLEGTKASAS SNGQFVSANA SQLASREIKK QEVGVFVKSK ETETDDPMSH
MFLKGGKAGI LTEGSPEIDS SNSSAGYASL VSKFLEVTKA TASSDLQFAS TNSSALALQE
KKKQTDGVTV NSKESEANLQ MPIMLPEENM PGVSNERSSR MGSYISGNSF ASLVSKFIEV
TNASSSSSIY YLSSDASALA FQEEKKQADG VYVNLKENES NKPISSWLLE ESKPVALTEG
SPEMGSCNSG DGFASLVSQF LEGKKVSASS SSQPVSADVN ARSCLSGALA SSSGHGEREY
FNIGNTIVKP GVTVTECAHS SSSSKKFSTP IRVFGRLTRA RKAARDKNMA AALLLKDASW
FFNKTKGKRS VISKAARSSV WGGLGSLIQV FQVQQSDNAA SGFPLELVKS IGGKKVERGR
SRGRYRAKAK VSTKSQKPKN PAQVKSRRAK AQRKDQLIAK ESPLSLYHHD GGNVNLSVGC
LKSEAMDNNS GMFKASHEIS NENSKAAMEN FDVKFGLDGC DTKQVHEVAV QDASVDGFKK
SVLSVDVDVP IGDLKHGDKD SESTLTQDTT AENLIGSSSF MLSSFEYGVD ALGEGFSSMH
LDFGASPHLM DSDETERNAT VTDRKDDLCL HETLQCGRSF PVTADTSLSS QELSEKRFCC
KIPSHGMDST TETTYLEDLQ DEAPTCSQAG IDPIITPPLD LKQYGRKKGR RKEEGSRNQS
LLFADLPKQE TLQGDLLVSV NQSTARRSTK SRSEQTSKRS SKPRKNSDLK SMGNPFGENC
RDGELYVEQA PLRIREFKMD QGAMELASSC ERITLSGPMG IGAAPSEEAG GEMLQLNANK
KAQRHPKKSN EVNKCGSYTP TSGGCKKGRG NGSQKKKVVP GQHATLTGEL DSGVFFHGGS
SDKEQETLQD QWRKDGGKGA AVQDGAGSVI LGESGANAVN KSALDAEVQS LPPRVAWVLC
DDCQKWRCIP ATLADIIEET NCKWTCKDNL DKAFADCSIP QEKSNAEINA ELDISDASGE
EDNCGSRHCP KGLDARQLTA SQQMSWTLIE HNIFLHRSRK SQTIDEIMVC HCKSPVDGIL
GCKDDCLNRM LNIECVQGTC PCGDLCSNQQ FQRRKYANFK WIRCGKKGYG LQLQEDVSQG
DFLIEYVGEV LDMATYEARQ KEYAARGQKH FYFMTLNGNE VIDACVKGNL GRFINHSCEP
NCRTEKWIVN GEVCIGLFAI RDIKKGEEVT FDYNYVRVFG AVAKKCVCGS SECRGYIGGD
PLNPEAVVHS DSDEDYPEPV MIHENGGTGI LADDTISNNG RTEILADDTN SSTKGNSITG
ISANDTISKT EEIGGTEILA IDNISNSKEA GRTEILANEY NSIMKEDGGA EILANDNNSN
LKENGRTEVI YDDSNNTCST NWTDAVVPRE IASLPAGDVS NRPIADNMEV SHKDKKAVSS
IKKSSRSIKM GRSNTNQLKA SKPRKLLPGI DRGRFEGVDE KLNELLDAEG GISKRKDATK
GYLKLLFVTA ACGDNVHGEA FQSTRDLSLI LDALLKTKSR MVLVDIVNKN GLQMLHNIMK
QNRRNFNKIP IIRKLLKVLE YLATKEVLTL EHINSSPPRA GIESLKESIL KLTWHNDVQV
HQIARSFRDK WIPRTTRKAK YSDREGADYH HQSNGRNGHW NRFHKRWQSP ALRHSDAIEC
KSRALEPVPV SSSPSLPKNP PSPPVVCANT DKQTDATPSS TTTNGTRRRK RKSRWDQPKD
GEEEQPSLNT EHRQCSEVMP DHPPGEKLVS SLAESVQAPL TIESSSHSTL VRAVPCSEGA
HLDDEKVPPG FSVPSGTQTA YPEEQRFECN AQKKSFIGSQ LCPAEQHSPL GFQSPPLPSP
FPKEQRRRHN DAAKYHSHPC DYDEHSVPPG FPPPSCNAQV NSLSPVEQGC GMANKGYDEQ
IPPGFQPPLS SPQVVPTPPN SSAVALDPPS YQHNSWGVNQ QGTTCISPSV PSSFPGAPRP
QAPNFQTNPI GSSIGGAPPM PTLNWSLPPP RPPPMPFQLL PPPPPGPPPL HHMVRPPCSE
EIMRSPQFVP HVLGPAPSQP VPINPPLPPG PPPASARPVS GSFPCGSHSP PLAPQPMLAA
PFQCMPPPTN QPMPPFHCPP PPPPPPPPPP PPPPNPPMMH GDPFPMQNQA TMPPPPLPNT
CNAVPQRQNQ APMQPPPPPI TNCNVVPNSR EEGSSSYAPP QPCVGGTATA GGMGRRWGGP
QHRCDHVPPW QRSRNNNNSN NHHNSWSARG CSRGGFNGFN GKCFRKGGSG GGSSGANKNF
SSTHHHHHH
//
