ID A0A2K6A6A2_MANLE Unreviewed; 1252 AA.
AC A0A2K6A6A2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Euchromatic histone lysine methyltransferase 2 {ECO:0000313|Ensembl:ENSMLEP00000035538.1};
GN Name=EHMT2 {ECO:0000313|Ensembl:ENSMLEP00000035538.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000035538.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000035538.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6A6A2; -.
DR Ensembl; ENSMLET00000059137.1; ENSMLEP00000035538.1; ENSMLEG00000041773.1.
DR GeneTree; ENSGT00940000159459; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20905; EHMT_ZBD; 1.
DR CDD; cd10533; SET_EHMT2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR043550; EHMT1/EHMT2.
DR InterPro; IPR047762; EHMT_CRR.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR038034; SET_EHMT2.
DR PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR PANTHER; PTHR46307:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF21533; EHMT1-2_CRR; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT REPEAT 726..758
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 759..791
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 792..816
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 826..858
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 892..924
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1014..1077
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1080..1197
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 136806 MW; 453C26A5A0D884C4 CRC64;
MRGLPRGRGL MRARGRGRAA PPGSRGRGRG GPNRGRGRPR SLLSLPRAQA SWTPQLSTGL
TSPPVPCLPS QGEAPAEMGA LLLEKETRGA TERVHGSLGD TPRSEETLPK ATPDSLEPAG
PSSPASVTVT VGDEGADTPV GATPLIGDES ENLEGDGDLH GGRILLGHAT KSFPSSPSKG
GSCPSRAKMS MTGAGKSPPS VQSLAMRLLS MPGAQGAAAA GPEPPPATTS PEGQPKVHRA
RKTMSKPGNG QPPVPEKRPP EVQHFRMSDD VHSLGKVTSD VAKRRKLNSG GGLSEELGSA
RRSEVTLAKG DPGSLEEWET VVGDDFSLYY DSYSVDERVD SDSKSEVEAL TEQLSEEEEE
EEEEEEEEEE EEEEEEEEED EESGNQSDRV RDGATRGRPQ GRREREGGEP RQSRGVHGVL
GHGGEDPPGV PMGEVQGLPQ LLFFSVQGVS NDTSSLETER GFEELPLCSC RMEAPKIDRI
SERAGHKCMA TESVDGELSG CNAAILKRET MRPSSRVALM VLCETHRARM VKHHCCPGCG
YFCTAGTFLE CHPDFRVAHR FHKACVSQLN GMVFCPHCGE DASEAQEVTI PRGDGVTPPA
GAAAPAPPPL SQDAPGRADT SQPSARMRGH GEPRRPPCDP LADTIDSSGP SLTLPNGGCL
SAVGLPLGPG REALEKALVI QESERRKKLR FHPRQLYLSV KQGELQKVIL MLLDNLDPNF
QSDQQSKRTP LHAAAQKGSV EICHVLLQAG ANINAVDKQQ RTPLMEAVVN NHLEVARYMV
QRGGCVYSKE EDGSTCLHHA AKIGNLEMVS LLLSTGQVDV NAQDSGGWTP IIWAAEHKHI
EVIRMLLTRG ADVTLTDNEE NICLHWASFT GSAAIAEVLL NARCDLHAVN YHGDTPLHIA
ARESYHDCVL LFLSRGANPE LRNKEGDTAW DLTPERSDVW FALQLNRKLR LGVGNRAIRT
EKIICRDVAR GYENVPIPCV NGVDGESCPE DYKYISENCE TSTMNIDRNI THLQHCTCVD
DCSSSNCLCG QLSIRCWYDK DGRLLQEFNK IEPPLIFECN QACSCWRNCK NRVVQSGIKV
RLQLYRTAKM GWGVRALQTI PQGTFICEYV GELISDAEAD VREDDSYLFD LDNKDGEVYC
IDARYYGNIS RFINHLCDPN IIPVRVFMLH QDLRFPRIAF FSSRDIRTGE ELGFDYGDRF
WDIKSKYFTC QCGSEKCKHS AEAIALEQSR LARLDPHPEL LPELGSLPPV NT
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