ID A0A1S3LNW1_SALSA Unreviewed; 1322 AA.
AC A0A1S3LNW1;
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-like isoform X2 {ECO:0000313|RefSeq:XP_013992234.1};
GN Name=LOC106567479 {ECO:0000313|RefSeq:XP_013992234.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013992234.1};
RN [1] {ECO:0000313|RefSeq:XP_013992234.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013992234.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013992234.1; XM_014136759.1.
DR GeneID; 106567479; -.
DR OrthoDB; 5481936at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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 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 PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR PANTHER; PTHR46307:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 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; 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; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
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:UP000087266}.
FT REPEAT 781..813
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 814..846
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 847..871
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 881..913
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 914..946
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 947..979
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1085..1148
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1151..1268
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 144788 MW; EE3BD98CBFC1BFB8 CRC64;
MCASGEDKEK RNNPFETPAL SLARSLCPSQ PLSSMEPIRR KQPTGLAKGR VVKGESMEDG
MESPGDRVEE GNVSRDEEVA ARLRSSPRAE AELNGTYESA ELGNRHRNPT PLVSQANGSQ
VAIENGMMET DLPHGSTTGS NGYILSKQQQ EGGSSTGSTA APHRTSWLPS GTTMIEHAAK
TFPSLAAGSG HSLGAIRTDT QHAGSPSGQG TSDAETKNGM SASDSPAPSP QSIAIHRARK
TMSMPASNQT LKLLNRKFTE PYGADEESQN GPEEEKSQQT SPSQNQLPPS QSDVPAAATA
KSQTASRKKK RKMGTYSLVP RKKTKVLRQG AVLQMFSQLQ STQSAQSKEV SHVNGERVEN
ESEEGWEDGE EWEEEVEQGG EGVPTALEKI ETSGPALQGE LGEEPDSEES AEEEGEEEGN
ESDLSSESSV KKRLTKKSKG DYFWLRPSRK RKRKPKSEGL PGTGPQGQAG LSKDYTEVPL
HSLNLKAKEM LLSPQHIGVS GGVDEDMVQE LPLCSCRMET PKSREILTLA DRKCMATESV
DRQLSRCQSA VLKHEMMRPS NSVQLLVLCE DHRAGMVKHQ CCPGCGFFCR AGTFMECQLD
VNISHRFHRA CASVLKGQTF CPHCGEEASK AKEVTIAKAD TTSTMPATYA AHSPATPGAT
EGRADTTTGG LSCSSVGGDI SGRADSSLSI PPGHTLDTSF PGASRTGVLT PAVGIGMGIG
MSTTPKETLE SILLALDTEK PKKLRFHPKQ LFISAKQGEL QKVLLMLVDG MDPNFKMESQ
SRRTPLHVAA EAGHQEICHL LVQSGANLDI CDEDQRTPLM EACENNHLET VRYLLSAGAI
ASHKDVEGFT CLHLAAKIGH YNIVEHLLST GLIDINCQDD GGWTAMIWAT EYKHLNQVKL
LLNKGADINI RDKEENICLH WAAFSGSVEI AELLLEAKCD LHAVNIHGDS PLHIAARENR
LECVILLLSR GVDVNLKNRE GETPPDCCSR SSRVWLTLQT NRRIREARSS TQGEKVLNSL
TLGVHWDLSL HLPPHYRDIA RGYERVPVPC VNSVDSEPCP DNYKYVPDNC VTSPVNIDKN
ITHLQYCVCK DNCSSSSCMC GQLSLRCWYD KNGRLLPEFY REEPPLIFEC NHACSCWRTC
KNRVVQNGLR VRLQLFRTSR MGWGVRTLQE IPQGTFVCEY VGEIISDAEA DVRENDSYLF
NLDSKVGDVY CIDARFYGNI SRFINHMCEP NLFSCRVFTA HQDLRFPHIA FFACETIKAG
EELGFDYGDN FWDIKGKHFS CECGSPKCKH SAATIALRQA DSSPLDQQSS ALPDTSSSTT
PF
//
