ID M7AUL5_CHEMY Unreviewed; 1139 AA.
AC M7AUL5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Histone-lysine N-methyltransferase EHMT1 {ECO:0000313|EMBL:EMP28409.1};
GN ORFNames=UY3_14498 {ECO:0000313|EMBL:EMP28409.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28409.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB563898; EMP28409.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AUL5; -.
DR STRING; 8469.M7AUL5; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 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; 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 Methyltransferase {ECO:0000313|EMBL:EMP28409.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP28409.1}.
FT REPEAT 612..644
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 645..677
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 678..702
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 712..744
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 778..810
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 900..963
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 966..1083
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 107..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 128402 MW; ECEE3DC91CCF821F CRC64;
MPQAHRFKAC ATCRKPMPVS HPPRLVSTFC LGEEHQTELC KICKAFKPRT KKERVFSLKQ
LLMEAALQPP ARSAQRRLRL PRCVVLRSRR ETRDRLNTES CWPHRARLGP GTARPPQCGP
WRSQKEGVDV PRIGGRRLPR PRAPIRVERP LYRYRRLQRH KSHRAHHASK DPKEARDTRD
QKESKEEGNK NVLEFGKPPP LPPFPGFHQS LPQNQSYVAT TKSQTAAAVS RKKKRRMGTY
SLVPKKKTKV LKQRTMIEMF KSITHSTAGA KGEKDLIGIS PHMNGESTEV DSGEEDSDDL
EEEDERGAEQ PAASPSQDNR IPKEGSSDAD SARQMEDGES EEEQESGESG EEEEDGDESD
LSSESSIKKK LLKRKGKTDS PWLKPTRKRR RRNKKKQASL SNGPEAMEMD GLQEVPLCSC
RMETPKSREI TTLANNQCMA TESVDSELGR CTNSVVKYEL MRPSNKVQLL VLCEDHRGRM
VKHQCCPGCG YFCTAGTFME CQPESSISHR FHKNCASQVN DTSYCPHCGE EASKAKEVTI
AKADTTSTVL LTYEQEKPMA LEGRADTTTG RPKKLRFHPK QLYFSARQGE LQKVLLMLVD
GIDPNFKMEH QNKRTPLHAA AESGHVDICH MLIQAGANID TCSEDQRTPL MEAAENNHLD
AVKYLIKAGA LVDPKDAEGS TCLHLAAKKG HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA
TEYKHVELVK LLLSKGSDIN IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD
SPLHIAAREN RYECVVLFLS HGSDVSLKNK EGETPLQCSS LNSQVWVALQ MNKTIRESST
DKPAQIEKTV SRDIARGYER IPIPCINSVD SEPCPTNYKY VSQNCVTSPM NIDRNITHLQ
YCVCIDDCSS SNCMCGQLSM RCWYDKDGRL LPEFNMSEPP LIFECNHACS CWRNCRNRVV
QNGLRVRLQL YRTQKMGWGV RSMQDIPLGT FVCEYVGELI SDSEADVREE DSYLFDLDNK
DGEVYCIDAR FYGNISRFIN HLCEPNLTPV RVFMSHQDLR FPRIAFFSTR QIEAGEEIGF
DYGDRFWDIK GKYFSCQCGS PKCKHSSTAL AQRQASTSSQ DTQETGLPDT SSAMAAGPF
//
