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Database: UniProt
Entry: M7ATD8_CHEMY
LinkDB: M7ATD8_CHEMY
Original site: M7ATD8_CHEMY 
ID   M7ATD8_CHEMY            Unreviewed;       778 AA.
AC   M7ATD8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Histone-lysine N-methyltransferase SETDB1 {ECO:0000313|EMBL:EMP27949.1};
GN   ORFNames=UY3_14926 {ECO:0000313|EMBL:EMP27949.1};
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:EMP27949.1, 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).
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB565896; EMP27949.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ATD8; -.
DR   STRING; 8469.M7ATD8; -.
DR   eggNOG; KOG1141; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd01395; HMT_MBD; 1.
DR   CDD; cd10517; SET_SETDB1; 1.
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; IPR047232; SETDB1/2-like_MBD.
DR   PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR   PANTHER; PTHR46024:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 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; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000313|EMBL:EMP27949.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transferase {ECO:0000313|EMBL:EMP27949.1}.
FT   DOMAIN          203..276
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          279..743
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..386
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  86299 MW;  33C9B9979BBF0DB2 CRC64;
     MGKAAVNQQY RGSYSSGQPG SSAVQPFHGM MDRVPNEPSY RAPMEKLFYL PHVCSYTCLS
     RVRPIRSDQY RSKNPLLIPL LYDFRRMTAR RRVNRKMGFH VIYKTPCGLC LRTMQEIERY
     IFETDCDFLF LEMFCLDPYV LVDRKFQPYK PFYYIADITK GKEDVPLSCV NEIDTTPPPQ
     VAYSKERIPG KGVYINTGWE FLVGCDCKDG CRDKSKCACH QLTVQATGCT PGGQINPNSG
     YQHKRLEECL PTGVYECNKR CKCNTNMCTN RLVQHGLQVR LQLFKTQNKG WGIRCLDDIA
     KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA KCSSDSSGVD
     LKDEEEENTG TEEQDESNED SSDDNFCKDE DFSTSSVWRS YATRRQTRGQ KENGLSETAS
     KDSGLTRQIS HDEVAMTAAC KLPVSEETSK NKVASWLSSN SMSDSFQDND SASSFKMTEA
     SEVKAGKVEV LGDREKPSTS GLGGKEAFGL DADSKMQKKE ESEEPNKLSL ASETGKVYGY
     NPSPMKLEGI RRPPSKTIMH QSKRHLAPPQ QAADDVLTLS SSTDSEGENG QPAAGQAQGN
     TNDSDDIQTI SSGSEEEDID DKKNSSSGLG PIKRQVAVKS TRGFALKSTH GIAIKSTNMA
     SADKGENMLV RKNTRQFYDG EESCYIIDAK LEGNLGRYLN HSCSPNLFVQ NVFVDTHDLR
     FPWVAFFASK ATAAPRGVLA VAGKQSRSIA AGYAALSPPT SLSHGLLPSK ACEMLLFR
//
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