ID F4WGP5_ACREC Unreviewed; 1130 AA.
AC F4WGP5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Histone-lysine N-methyltransferase eggless {ECO:0000313|EMBL:EGI66627.1};
GN ORFNames=G5I_04835 {ECO:0000313|EMBL:EGI66627.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI66627.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL888142; EGI66627.1; -; Genomic_DNA.
DR RefSeq; XP_011052588.1; XM_011054286.1.
DR AlphaFoldDB; F4WGP5; -.
DR STRING; 103372.F4WGP5; -.
DR EnsemblMetazoa; XM_011054286.1; XP_011052588.1; LOC105144993.
DR GeneID; 105144993; -.
DR eggNOG; KOG1141; Eukaryota.
DR InParanoid; F4WGP5; -.
DR OrthoDB; 2877903at2759; -.
DR Proteomes; UP000007755; 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 CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
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; IPR003616; Post-SET_dom.
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 InterPro; IPR002999; Tudor.
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 SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50982; MBD; 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 Methyltransferase {ECO:0000313|EMBL:EGI66627.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
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:EGI66627.1}.
FT DOMAIN 615..684
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 744..816
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 819..1105
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1114..1130
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 488..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 129310 MW; 7074CB5AA8877E56 CRC64;
MAQAQSAEII ELMSDEDEKK TRKTKSKGYN SNCVNFKCRS GINMKVAPSF ACAFYGVSLE
KKKKRIICKE CFDAALQHQK QLVQAFVENR SLLDCYFPDH TMEVEISDSD DSDDEKKKEL
EKDNNEYIPE DVLLDIKDKL NDTLSHIYKK YNVEQHAKVA CETLKQRWRD ICAANDSLNT
EIREIMRTVD KLRNNLYEDF RPQIKMLEEL QINDEITETA HPLVATKKVT QVRVPPSSLL
QDNQLEVLAI EPSCTKEIII PNLPPTGPLL KRSPEIDDIV YVMKSPVMPW IKAKVLNIVS
NPWNIRVRLI QKKYNAAIKT VSGKLLATTE LSKVMIPVGT RVVAIFHDVV SNNYYSGIIA
ETPKSINKYR YLVFFDDGYA QYVVHNDILL VWETSPRIWE DIPSESREFV KKYLESYPER
PMVKLQPGQI VKTEWNGKWW LARVVQVDAS LVQMHFDADK RTEWIYRGST RLGPLFLEVR
KANARQQLQQ SGNVHTRHRI PAPSNKNNLP YVEYTSNVEE DVTQHLQAEK TTVTTSVAST
TPSTALQQPR AVAKKSTAKR QNNVDTTTYN STVETKPSHS IVFYHTQRKY EPKKYVAHKC
GPRCIKGIKV SHDDLKGLSP LSIPLLCGWH RQLCKFSKGK KVILYQTPCG VRLRNMEELH
RYLRITNSTL SVDLFDFDYW VRAFADFVVE KCFINIKDLS YGVENVPIPC VNDLDHTQPD
TIRYTTRREP TEGVYLNLDP AFLCSCDCED DCQDKEKCQC WQLTIQGATL GGKMPNSAVG
YIYKRLPEPV TTGIYECNSG CKCSVKTCLN RVVQHPLRLK LQVFKTGPRG WGIRCLNDIP
HGAFICIYAG RLLTEQGANE GGKNYGDEYL AELDYVEVVE GFKEGYESDV LEPEILMSPT
EDDNKKKATD VSDEEEDNTK ESTNDSDEDF NIDSYVASCN NDLLETTAES SSIRKRLRKR
KRHEIDNQPD VSEENSDDES IMRGLENTAK SSTNENQDMI NISDDDDSRN DVRREPSRFE
PNLEPNQIER PTFKSVRDYF GEDEAVYIMD AKTTGNIGRY LNHSCDPNVF VQNVFVDTHD
VRFPWVAFFA LQYIKAGQEL TWNYSYDVGS IPGKVIICKC GAANCRGRLL
//
