ID A0A1I8HR48_9PLAT Unreviewed; 1191 AA.
AC A0A1I8HR48;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|WBParaSite:maker-uti_cns_0007478-snap-gene-0.5-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0007478-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0007478-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
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DR AlphaFoldDB; A0A1I8HR48; -.
DR WBParaSite; maker-uti_cns_0007478-snap-gene-0.5-mRNA-1; maker-uti_cns_0007478-snap-gene-0.5-mRNA-1; maker-uti_cns_0007478-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd10517; SET_SETDB1; 1.
DR CDD; cd20382; Tudor_SETDB1_rpt1; 1.
DR CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.170.270.10; SET domain; 2.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR041292; Tudor_4.
DR InterPro; IPR041291; TUDOR_5.
DR PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR PANTHER; PTHR46024:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF18358; Tudor_4; 1.
DR Pfam; PF18359; Tudor_5; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 627..699
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 762..834
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 837..1166
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 183..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 500..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..970
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 131816 MW; 12CAEB49F4B1F7E4 CRC64;
MHAWKTLPAM PPGWESRIDA IRRLSVSVLV SCLAEILRAN HSVTGRMGTR RLWDMHMAAL
EEYVPRQMLA RTALEYLRLT EPLVYRAVLP EFEINGKVVE VLVHKFLFQI VNIETAFHNA
LGSDANWSEV VNKIGSLEKT KQKLEETVRH QEKVLDRLEK RSRDQQIAWY GRVVYPASAL
ACSSQDTDAD EPNESDNRND AQTAAAADGS SAMARKSLIM EAATAPHQSQ QQQAASVLVL
PSGAGQPGSQ QAAANVGKYR LVHPEELVSV AVVAQQNQPV FALFDRELWR QAVIADVLEP
AAGTGGTVLY RVSFAKTTKQ LKPSQVALSE TAETRLEQYP VGARVVSSYT DDRGLVFYYS
AIVAEPPGER NSRRYLLFFD DGYAQYAPPS DVRRVLQQTP QNWREVAENS QDFVRAYLDR
FPNRTMLRLR PGLTIRVELR GEWLTAVVER VDASLVQVRF PTRSGRLEWL YRGSTRLEDL
YKAMVARERA AELAAAAAAE SASEQNQNQQ QQQPTPIRQA FARKSSMGGI RRQHKHQHQQ
HQKQSATLTN ADPDAAAAAA AAAEEDACYE EARAGVMVAS IDSESLRQLR PFPHQHGVDC
GVNCLNSGGG SVGGDSSEQN RLASTELVDR NPLDVPLLLG WHRFVVKLGG PGRVRRRELI
EYAAPCGRRI RNPVELDRIL SQTSSRLHPL HFCFDPLIRV ATEFQATGAR RQLADLSYGK
ERIPVPAVNC LDADEPPFID YTPQRMPLLN VCTNEADKGF LVCCDCTDGC RDRTKCACLR
LTAEASATVT GRTDSRPAYE NGRLVRALIG GVYECNSGCS CRQWQCRNRL VQRGLHSRLQ
IFKTSRKGWG LRPLHDLPKG AFVCVYAGEL YSEELAVQYC DQFGDEYQAD LDHLEVMEQE
KFGYEAQAIE PHQQQLKQKS WLRKSQSQSS LTNDNGDNED PDEEPTAEAE EPGAETTEEE
EIDNDDANDE DYCGDSRRKR RLLNKKSANT TANAATNSST AGASANPKRS RLDDEAIGAA
ESGSGSTVPK AGSGCCSQQN AQDHCSMHDD EDAGAIAATA AAAGSPCSQP LSSIANADQM
DEAEDDDVLE AGGPAACLRA LLGEAQPYIM DAKRIGNLGR YLNHSCAPNV IVQNVFVNTH
DPRFPEIAFF TCKRVRAGEE LCWDYNYQVG SVPGKTLRCF CRARDCRGRL L
//
