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Database: UniProt
Entry: A0A226F5M3_FOLCA
LinkDB: A0A226F5M3_FOLCA
Original site: A0A226F5M3_FOLCA 
ID   A0A226F5M3_FOLCA        Unreviewed;      1274 AA.
AC   A0A226F5M3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Histone-lysine N-methyltransferase eggless {ECO:0000313|EMBL:OXA65093.1};
GN   ORFNames=Fcan01_00674 {ECO:0000313|EMBL:OXA65093.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA65093.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA65093.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA65093.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA65093.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
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:OXA65093.1}.
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DR   EMBL; LNIX01000001; OXA65093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226F5M3; -.
DR   STRING; 158441.A0A226F5M3; -.
DR   OMA; ISACMEC; -.
DR   Proteomes; UP000198287; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd10517; SET_SETDB1; 1.
DR   CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR041292; Tudor_4.
DR   InterPro; IPR041291; TUDOR_5.
DR   PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR   PANTHER; PTHR46024:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF18358; Tudor_4; 1.
DR   Pfam; PF18359; Tudor_5; 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; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:OXA65093.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OXA65093.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        105..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          972..1045
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          1048..1249
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1258..1274
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1122..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1148..1168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  144419 MW;  BCB5F836BE858389 CRC64;
     MTQKVEIDIK NTKSNLAPKN PKSDPAPKTS KSDPAPKNSK SDPTPKNLKS DPAPKNPKSD
     QASKNPKPGP PAKNPKSDPS SQTPEPVNEC IATAGICISA CMECFMVTAA CSMFLMILYF
     FGILMLCFLA SKGYDVQDYL DPWNMFCKVG LFVVKAIAVL LILAICIEMA SSLYQNSALI
     GKMFCDVTTK SWRLVRSTKW GWPNKSLPTC KLVKEKAPID VGKKGVQEIK FDDIVKIENE
     KNCDDVAKME MVNECNNANC KSNSDELVIA KEAAILYYRF DMSHKKVHKI CKTCDEDAET
     FMQNSVNALK NDENIFAFKT KPEGMEVDVI EIKDDEEDDN NPAEIQRLET DNNEILELST
     SVDNLIGEVM TKLDLASQIA KCEETTTMEF ENLEEEYCNL KEQVSLVEGH IAETKKIYNK
     VAGYEQPLPV IAVELDLSVT ETLLESMLQN VNDFLNFDDA PPDFQPTPSP ESAESNLNGS
     SAEKENSHSD DDDIVEVVPG EGSPQKLTCP LTRPLKDVPR LVPLIGGSVY AQKRTLLHYW
     ARATIEEILD VGAGKSEFLV RFVRGDGRLK QLTAKQIAYD IPCPFMLIVG TRVIAKFRED
     LKEKPHGPDG HYAGIVAEQP TPRNKFRYLI FFDDGCAQYV GINDILLIHK YSKEVWSDVH
     PDSAEFIKNY LRKYPERPMV RLTLGQVIST EWNGKWWVAR VTELDCSLAK MHFENDGRWE
     WIYRGCTRFS PLFEKYTRQR QRKIARQSTS ALTYHESYQQ SKDGDDWVPS HGRKKRTEPT
     PGTSASALEK QHGDIKRLTR FDYGEFEGTI AKRAIPSDAP LTKEYSPHVC DHSCVYEYDD
     SNPEYKKIGP LTLPLHFGFT REIAESPYRS IYYRGPCGLR LHDMEEMYDY LTQTKCQIQI
     DHFCFDLAED CLNEFRHSRQ HSFLPDLTYG KEPVPVQLVN AFDHEFPPYV EYLSQRVAGS
     GVNFNNDEEF LVGCDCEDDC RDATKCSCWQ MTHSGISFSK FNTPENPITG YEYRRLKNNV
     FSGIYECNQR CKCAKTCCNR VAQNGLKVPL QLFKTAAKGW GIRPIFDVPE GAFICIYAGQ
     VLTEDAANDD GQQFGDEYLA SLDYIEHIEK LKEDYESEVT DIEADEPVAH PKKKIKTRKE
     RPFNTRGKNN AKKTSSGAGN SKNKSGPVIT PPKTKVRRPL REYFGEHDEC YIMDAKTTGN
     IGRYFNHSCE PNIFVQNVFV DTHDLRFPWI TFFASKHIRA GSELTWDYAY EVGSIPDKVL
     LCQCGSPECR GRLL
//
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