ID A0A3Q7RN93_VULVU Unreviewed; 1276 AA.
AC A0A3Q7RN93;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Histone-lysine N-methyltransferase EHMT1 isoform X1 {ECO:0000313|RefSeq:XP_025843731.1};
GN Name=EHMT1 {ECO:0000313|RefSeq:XP_025843731.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025843731.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025843731.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025843731.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025843731.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025843731.1; XM_025987946.1.
DR AlphaFoldDB; A0A3Q7RN93; -.
DR STRING; 9627.ENSVVUP00000040421; -.
DR KEGG; vvp:112911417; -.
DR OrthoDB; 5481936at2759; -.
DR Proteomes; UP000286640; 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:UP000286640}.
FT REPEAT 751..783
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 784..816
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 817..841
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 851..883
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 917..949
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1039..1102
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1105..1222
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 13..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 139627 MW; 601ED56BE28714CC CRC64;
MKTELLREEI SMAADGGSAE KQGGEAPVAA DSEANGSCGT SEASSHMTAV QHTQENSAVS
PQEGTNKLAR IAENGVSERD SEMGKQNHVN TDDFTQTSVL GSNGYFLNKP SLQEQPMRIT
STLASSLPGH AAKTLPGGSG KGRTPSAFSQ TPATAPAKLG ETSKDAEDRK PMAPGADVKV
HRARKTMPKS ILGLHAASKD PREVREARDH EEPKEEINKN LSDFGRQQLL PPFPPLQSLP
QNQCYMATTK SQTACLPFVL AAAVSRKKKR RMGTYSLVPK KKTKVLKQRT VIEMFKSITH
STVGSKGDKD LGASTLHVNG ESLELDSEED ESEELDEDED QGAEQAAAFP TEDSRTSKGS
VSETDRTQKT DGESEEEQES AGTGEEDEDG DESDLSSESS IKKKFLKRKG KPDSPWIKPA
RKRRRRNKKK QSGVLGSEAY TSSSGSTEQA APGDSTGYME VSLDSLDLRV KGTLPSQVEG
LANGPDVVET DGLQEVPLCS CRMETPKSRE ITTLANNQCM ATESVDHELG RCTNSVVKHE
LMRPSSKAPL LVLCEDHRGR MVKHQCCPGC GYFCTAGNFM ECQPESSISH RFHKDCASRV
NNASYCPHCG EEISKAKEVT IAKADTTSTV TLAPGQDKNS LVEGRADTTT GSTAGPPLLE
DGKPQSTAPQ AAEGFDPTGP AGLGKPAPGL SQGPGKETLE SALIALDSEK PKKLRFHPKQ
LYFSARQGEL QKVLLMLVDG IDPNFKMEHQ NKRSPLHAAA EAGHVDICHM LIQAGANIDT
CSEDQRTPLM EAAENNHLDA VKYLIKAGAL VDPKDAEGST CLHLAAKKGH YDVVQYLLSN
GQMDVNCQDD GGWTPMIWAT EYKHVELVKL LLSKGSDINI RDNEENICLH WAAFSGCVDI
AEILLAARCD LHAVNIHGDS PLHIAAREDR YACVLLFLSR DSDVTLKNKE GETPLQCASL
NSQVWDALQM SRALRDAAPD RPVPMEKTVS RDIARGYERI PIPCVNAVDS EPCPSNYKYV
SQNCVTSPMN IDRNITHLQY CVCIDDCSSS NCMCGQLSMR CWYDKDGRLL PEFNMAEPPL
IFECNHACSC WRSCRNRVVQ NGLRARLQLY RTQNMGWGVR SLQDIPLGTF VCEYVGELIS
DSEADVREED SYLFDLDNKD GEVYCIDARF YGNVSRFINH HCEPNLVPVR VFMSHQDLRF
PRIAFFSTRL IEAGEQLGFD YGERFWDIKG KLFSCRCGSP KCRHSSTALA QRQASASQDG
QENGLPDTSS STADPL
//