ID A0A158P1U0_ATTCE Unreviewed; 1147 AA.
AC A0A158P1U0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=[histone H4]-N-methyl-L-lysine(20) N-methyltransferase {ECO:0000256|ARBA:ARBA00012188};
DE EC=2.1.1.362 {ECO:0000256|ARBA:ARBA00012188};
GN Name=105627042 {ECO:0000313|EnsemblMetazoa:XP_012063748.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012063748.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012063748.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; ADTU01000072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012063748.1; XM_012208358.1.
DR AlphaFoldDB; A0A158P1U0; -.
DR STRING; 12957.A0A158P1U0; -.
DR EnsemblMetazoa; XM_012208358.1; XP_012063748.1; LOC105627042.
DR GeneID; 105627042; -.
DR KEGG; acep:105627042; -.
DR eggNOG; KOG2589; Eukaryota.
DR InParanoid; A0A158P1U0; -.
DR OrthoDB; 5396777at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd19186; SET_Suv4-20; 1.
DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR InterPro; IPR025790; Suv4-20_animal.
DR InterPro; IPR044426; Suv4-20_SET.
DR PANTHER; PTHR12977:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 1.
DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 144..255
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 524..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1114
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 129211 MW; F3848DBC0DDD59CE CRC64;
MVVDYCLSIQ ASATAVRKQE RRLGGTVGAK MQPNSGGGCG MTPKELSDND DLATSLVLDP
YLGFTTHKMN IRYRPLKANK EELRKIICEF IQTQNYEKAY KKLMGGDWGA RLPHTKSKQQ
QINLENHIKR YLRVFDKDSG FAIEPCYRYS LEGQKGAKIC ATKKWMKHDK ISCLVGCIAE
LSEKEEAALL HPGKNDFSVM FSCRKNCAQL WLGPAAYINH DCRANCKFVA TGRDTACVKV
LRDIEVGEEI TCFYGEDFFG DGNCYCECET CERRGTGTFA SQKPGEEMSS GYRLRETDNR
INRTKHRQQP LNRNKQQADT ALTERNAVLV GNAAVAPQSL SMKELRRKGL TKYDAELLIA
QGCRFSDINQ QQPAINNGEN MLQTRAHPSA IATSVTRSLR NKQMCKFDGN TSDGNAIKNT
QSLRASRLHK RTESKKGKIN MKPPLLCLSN PAVKDTEVAD ISHRKEDSDR EPVHKENLYS
RLQKHHLSNA SEMDRGFHME QTRQRIVTVE SNEDACPLRL MEIEDTGDGD SMEDDRGIPD
LTAEVDPETV DNVNSSSYKK GHYSTNACDS IRLSSTSQAH VQQHLHTEES NPEDTNYRSR
DYHSSSPMRH KESENVPCST IEEANCINKR SKSHGKQLSS TDEQDDRKTP NEESSYEFED
DESPSPLIEE KKMLQTNFRE NILHETNSRS DDECCDLNST KVIVVHDVEK EEESENCESP
IAVDTSAASR SDSVEFCGLN SDGVIEAEAD TENILKCYNN TISNQEGKQD VVTKSDTYVA
SVEPGVRSEM TMLCATEMNS RINIIEGNNA MIFNNVQITN YNSDLTSHMN LEDNRNSALV
KKSTSRLSKS SRKLQKRLSN AKSKFGVLTE GVQDDLKSHS KGKSKNKSTK SQRRDRQRSA
TTEIGEADDD SGIQGDIYEF SEKESNLEDI GILSIIRRGK HESRHASSSS IAVSPVQEMQ
CNDEYNKAEP PVLIPEEPWP PTMAQSEHGV ESNSGVQSRE NCDVEGSLDR LTSYENNSTQ
SRKSSTTPSE CQWRTSNPSN CRVCPVTPER TSGRLKLTLR MKRSPVLDDI VESGTSGLSE
DSYEPEYEVL RVEGLERRKR RKKHKSRDRE RRHKKSRVLN LDPPPPPMKR LRLILGNETR
TIDLTHS
//
