ID A0A1S2ZWR3_ERIEU Unreviewed; 1279 AA.
AC A0A1S2ZWR3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histone-lysine N-methyltransferase EHMT1 isoform X1 {ECO:0000313|RefSeq:XP_007525784.2};
GN Name=EHMT1 {ECO:0000313|RefSeq:XP_007525784.2};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007525784.2};
RN [1] {ECO:0000313|RefSeq:XP_007525784.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_007525784.2; XM_007525722.2.
DR AlphaFoldDB; A0A1S2ZWR3; -.
DR STRING; 9365.ENSEEUP00000006327; -.
DR eggNOG; KOG1082; Eukaryota.
DR InParanoid; A0A1S2ZWR3; -.
DR OrthoDB; 5481936at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; IEA:InterPro.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20905; EHMT_ZBD; 1.
DR CDD; cd10535; SET_EHMT1; 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; IPR038035; SET_EHMT1.
DR PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR PANTHER; PTHR46307:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
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; 7.
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; 5.
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:UP000079721}.
FT REPEAT 754..786
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 787..819
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 820..844
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 854..886
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 920..952
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1042..1105
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1108..1225
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 13..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 140221 MW; 2B721B337A32D97C CRC64;
MKQDCCMKTE LLAEEVSMAA DEGSAEKQGG ETPSTTDGEA NGSCEQSDAS SHLNAVKHTQ
ESTKVSPQEG SKKLARISEN GISERDIEVG KQNHVRADDF TQTSVIGSNG FFLSKPTLQE
PPLRITSTLA SSLPGHAAKT LPGGAGKGRT PSMCPQMPTT APAKLGEGSK DTEEKKPAVP
GADVKVHRAR KTMPKSILGL HAASKDSREA REHEEPKEDM NTSISDFGRQ QLLSPFPSLH
QSLPQNQCYM ATTKSQTACL PFVLAAAVSR KKKRRMGTYS LVPKKKTKVL KQRTVIEMFK
SITHSTVGPK GEKDLSDSTL HVNGESLEMD SDEDDSEELD EDEDHGAKQA VAAFPTEDSR
TSKESMSETE RAQKMDGESE EEQESAGTGE EEEDGDESDL SSECSIKKKL LKRRGKPDSP
WIKPARKRRR KSKKKPSSGP GSDAYASSSG SAEQAVPGDS TGYMDLDSLD LHVKGTLSSQ
AEGLANGPEV VETDGLQEVP LCSCRMETPK SREITTLANN QCMATECVDH ELGRCTNSVV
KHELMRPSSK APLLVLCEDH RGRMVKHQCC PGCGYFCTAG NFMECQPESS ISHRFHKDCA
SRVNNASYCP HCGEEISKAK EVTIAKADTT STVTLAPGQE KSSLGEGRAD TTTGSAVGPL
LSEDDKPQST AAQAPEGSDL SGQVGLTKPT PSLSQGPGKE TLESALIALD SEKPKKLRFH
PKQLYFSARQ GELQKVLLML VDGIDPNFKM EHQNKRSPLH AAAEAGHVDI CHMLIQAGAN
IDTCSEDQRT PLMEAAENNH LDAVKYLIKA GALVDPKDAE GSTCLHLAAK KGHYDVVQYL
LSNGQMDVNC QDDGGWTPMI WATEYKHVDL VKLLLSKGSD INIRDNEENI CLHWAAFSGC
VDIAEILLAA RCDLHAVNIH GDSPLHIAAR EDRYACVVLF LSRDSDVTLK NKEGETPLQC
ASLNSQVWNA LQMSKALRDS APDRPAPQEK TMSRDIARGY ERIPIPCVNA VDSEPCPSNY
KYVSQNCVTS PMNIDRNITH LQYCVCVDDC SSSNCMCGQL SMRCWYDKDG RLLPEFNMAE
PPLLFECNHA CSCWRNCRNR VVQNGLRARL QLYRTQNMGW GVRSLQDIPL GTFVCEYVGE
LISDSEADVR EEDSYLFDLD NKDGEVYCID ARFYGNVSRF INHHCEPNLV PVRVFMSHQD
LRFPRIAFFS TRLIEAGEQL GFDYGERFWD IKGKLFSCRC GSPKCRHSST ALAQRQASEA
QEPQENGLPD TSSSAADPL
//
