ID A0A151MF43_ALLMI Unreviewed; 1311 AA.
AC A0A151MF43;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Histone-lysine N-methyltransferase EHMT2 isoform A {ECO:0000313|EMBL:KYO23148.1};
GN Name=EHMT2 {ECO:0000313|EMBL:KYO23148.1};
GN ORFNames=Y1Q_0005594 {ECO:0000313|EMBL:KYO23148.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO23148.1};
RN [1] {ECO:0000313|EMBL:KYO23148.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO23148.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO23148.1}.
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DR EMBL; AKHW03006215; KYO23148.1; -; Genomic_DNA.
DR RefSeq; XP_006273912.2; XM_006273850.3.
DR STRING; 8496.A0A151MF43; -.
DR GeneID; 102564850; -.
DR KEGG; amj:102564850; -.
DR CTD; 79813; -.
DR eggNOG; KOG1082; Eukaryota.
DR OrthoDB; 5481936at2759; -.
DR Proteomes; UP000050525; 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:KYO23148.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000313|EMBL:KYO23148.1}.
FT REPEAT 784..816
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 817..849
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 850..874
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 884..916
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 950..982
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1072..1135
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1138..1255
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 11..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..316
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 144961 MW; 2C0D9758EF88561A CRC64;
MRIWNMQLFE SSSKEDNRCL QQTVQSKGES RKDICMKTEL LKDITNNKEE GFNAMAADES
ATEKQVGEPK MAVDGETNGS CERSEAGSHP NPAKNTQDNT KVSQQDSSTK LNRIAENGIS
ERDGETGKQN HMKPNDFTQT SVTGSNGYIL TKQMAQEQPL RTTSTFASLT GHAAKTLPGG
ASKGRTVGTF SQMQATMPAK LGEGSKDVDA KKATPANAEI KVHRARKTMP KPTPSLHANR
DPKEGRDARD QKESKEEGNK SVLEFGKPAP LPPLPGLHQL LPQNQSYMAT TKSQTAAAVS
RKKKRRMGTY SLVPKKKTKV LKQRTVIEMF KSITHSSAGA KSEKDLSDGS PHVNGESIEV
DSEEEDSDEL EEDDEHGVEH PAAFPTEDNR ISKEGASDAD NSRKMEDGES EEDQESGESG
EEEEDGDESD LSSESSLKKK LLKRKGKTDS PWLKPTRKRR RRNKKKQASA LGAEAYKPPL
GGREGAGQEN SMEYMEVSLD SLDLRVKGIL SSQSEGLSNG PEAMEVDGLQ EVPLCSCRME
TPKSREITTL ANNQCMATES VDNELGRCTN SVVKYELMRP SNKVQLLVLC EDHRGRMVKH
QCCPGCGYFC TAGTFMECQP ESSISHRFHK NCASQVNDMS YCPHCGEDAS KAKEVTIAKA
DTTSTVSLTY EQQKPAALEG RADTTTGSGT GMRLSEEDKP ESSAAEGFDM AGSSVFVKPA
TGLTQGPVKE TLESALIALD SEKPKKLRFH PKQLYFSARQ GELQKVLLML VDGIDPNFKM
EHQNKRTPLH AAAESGHVDI CHMLIQAGAN IDTCSEDQRT PLMEAAENNH LETVKYLIKA
GALVDPKDAE GSTCLHLAAK KGHYDVVQYL LSNGQMDVNC QDDGGWTPMI WATEYKHIEL
VKLLLAKGSD INIRDNEENI CLHWAAFSGC VDIAEILLAA KCDLHAVNIH GDSPLHIAAR
ENRYECVVLF LSRGSDVTLK NKEGETPLQC SSLNSQVWVA LQMNKTLKDS SSDKPAQIEK
VVSRDIARGY ERIPIPCVNS VDNEPCPSNY KYVSQNCVTS PMNIDRNITH LQYCVCIDDC
SSSNCMCGQL SMRCWYDKDG RLLPEFNMAE PPLIFECNHA CSCWRTCRNR VVQNGLRTRL
QLYRTQKMGW GVRTMQDIPL GTFVCEYVGE LISDSEADVR EEDSYLFDLD NKDGEVYCID
ARFYGNISRF INHLCEPNLI PVRVFMSHQD LRFPRIAFFS TRHIEAGEEI GFDYGDRFWD
IKGKYFSCQC GSPKCKHSSA ALAQRQASTS SQDAQENGLP DTSSATAAGP F
//