ID A0A091JE06_EGRGA Unreviewed; 1499 AA.
AC A0A091JE06;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Histone-lysine N-methyltransferase 2E {ECO:0000313|EMBL:KFP18133.1};
DE Flags: Fragment;
GN ORFNames=Z169_02706 {ECO:0000313|EMBL:KFP18133.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP18133.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP18133.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP18133.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK501840; KFP18133.1; -; Genomic_DNA.
DR STRING; 188379.A0A091JE06; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15550; PHD_MLL5; 1.
DR CDD; cd19182; SET_KMT2E; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044434; KMT2E_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46462:SF2; INACTIVE HISTONE-LYSINE N-METHYLTRANSFERASE 2E; 1.
DR PANTHER; PTHR46462; UPSET, ISOFORM A; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KFP18133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Transferase {ECO:0000313|EMBL:KFP18133.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 316..433
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 229..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..596
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 231..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..652
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1499
FT /evidence="ECO:0000313|EMBL:KFP18133.1"
SQ SEQUENCE 1499 AA; 167164 MW; DEFB164DED4DF867 CRC64;
MSIVIPLGVD TADNSYLEMA AGSEPESVEA SPVVVEKSNS YPHQLYTSSS HSHSYIGLPY
ADHNYGARPP PTPPASPPPS VLISKNEVGI FTTPNFDETS SATTISTSED GSYGTDITRC
ICGFTHDDGY MICCDKCSVW QHIDCMGIDR QHIPDIYLCE RCQPRSLDKE RAVLLQRRKR
ENMSECLCFK DGDTSATESG DEVPVELYTA FQHTPTTITL TATRVTKVND KKRKKSGEKE
QNIAKCKKGS APEIDPTDSS NFGWETKIKA WMDRYEEANN NQYSEGVQRE AQKIALRLGN
GNDKKEVSTS NLIFKPPVES YVQKNKKILK AAKDLPPDAL IIEYRGKFML REQFEANGYF
FKRPYPFVLF YSKFHGLEMC VDARTFGNEA RFIRRSCTPN AEVRHVIEDG TIHLYIYSIH
NISKGAEITI AFDFDYGNCK YKVDCACLKE NPECPVLRRS EPTENINTGY ETRRKKGKKE
KDVSREKETQ NQNITLDCEG AATKMKIAEN KQRKLSPLRL SISNNQEPDF IDDIEEKTPI
SNEVEMESEE QIAERKRKMT REERKMEAIL QAFARLEKRE KRREQALERI STAKTEVKAE
CKEAQILNDA EFIQEQAKEE TATKPTPAKV NRAKQRKSFS RSRTHIGQQR RRHRTVSMCS
DIQPSSPDVE VTSQQNETEN AALVAEPETE TVVTEMVTET EAPALNKCPT KYPKTKKHLV
SEWLSEKSDK TGKPTDSLSE RPLRITTDPE VLATQLNSLP GLTYSPHVYS TPKHYIRFTS
PFLSEKRRKK EPVENITGSC KKRWLKQALE EENSTIDRFN SPSQERSRSP AINGENKSPL
LLNDSCSLTD LTTPLKKRRL YQLLESAFSE TSTPTPSPYA TPTHADITAS EPSVFATPPR
VKTEDEACRN GYKPIYSPVT PVTPCIHGNT MHFENISSPD SSPEIKRRAY SQEGYDRASI
LALNSFRNSN LTEMGLQEIK TIGYSSPRNR TDVTRQCTGE MESVSDLQLG LEVIEQSALH
KNLEAPAHDR TDSNSQLETA HCGRGTIYSS WVKSPDRTGV NFSMNSNLRD LTPSHQLEVG
GGFRISESKC LIQDDARGMF MEASVFCTSE DGIASGFGRT VNNDNLMDGN CTPQNPPQKK
KVSLLEYRKR QREARKSGSK PENFPLVTVS PHAAGGGNTS SNNGANDGYN NSGENGEQTD
NAASLPLPLP TTVYNAAPED IGNNCAVKES SSSEKSEPEV QWTASTSVEQ VRERSYQRAL
LLSDHRKDKD SGGESPCRPC SPSHVQSPPS SHSNLISQLQ LKVPSFTEFM EEPDPESLEP
TSECPSPDAS QKTCKSPSKA SKPSSPSPVV STQSLGKTPT KPDSHWEAAA NAPEAESANH
PKPELQQKQL TNNVQALSKN HPSQPHLRSS AEQLSHSQKL PSAPLKLHCP PSPHVENPPK
PSTPHAPVQH GYLSPKPHSQ QLGSPYRPHH PQSPQVATPQ RETHRNFYPA APTLQPGSQ
//
