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Database: UniProt
Entry: A0A158P0I0_ATTCE
LinkDB: A0A158P0I0_ATTCE
Original site: A0A158P0I0_ATTCE 
ID   A0A158P0I0_ATTCE        Unreviewed;      3408 AA.
AC   A0A158P0I0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Histone-lysine N-methyltransferase trithorax {ECO:0008006|Google:ProtNLM};
GN   Name=105626604 {ECO:0000313|EnsemblMetazoa:XP_012063288.1};
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_012063288.1, 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_012063288.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; ADTU01005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012063288.1; XM_012207898.1.
DR   STRING; 12957.A0A158P0I0; -.
DR   EnsemblMetazoa; XM_012207898.1; XP_012063288.1; LOC105626604.
DR   GeneID; 105626604; -.
DR   KEGG; acep:105626604; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   InParanoid; A0A158P0I0; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd15506; PHD1_KMT2A_like; 1.
DR   CDD; cd15508; PHD3_KMT2A_like; 1.
DR   CDD; cd15489; PHD_SF; 1.
DR   CDD; cd19170; SET_KMT2A_2B; 1.
DR   Gene3D; 3.30.160.360; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR047219; KMT2A_2B_SET.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45838:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE TRITHORAX; 1.
DR   PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          537..650
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          904..954
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          951..1003
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1031..1092
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1384..1492
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          3270..3386
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          3392..3408
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          332..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1899..1964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2231..2301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2969..2996
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        349..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1904..1950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2231..2297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3408 AA;  378260 MW;  B12994A15E7B12F4 CRC64;
     MGRSKFPGKP PKTATRKRIK VLGQPEAAQN DPVTVAENIY YGLSLFNETF GDNEKEHPPF
     HGFSTKEANL SASYIKTQQH DAEKTSDKLP SVTVENLAPR SSTKKDVIDI KNSPTDIENS
     TEKFTNSNPK PVKDITRLQS VTNPNTKHSK IHRAKSRKNC KNIKFSNYLK NPVLKSVNNI
     LDQHQRTRQL RNSTAKRLLQ RAKSGSNTRN LVVQSGEKPS TVRKFVLPVR SVHSSRVIKP
     NKRFIEELEE ISTTEYSENE IGVHVKKTKL NPDKLSNLES KLKGNTVNKL CTKFKEARSK
     PKRVIQSVNS NAEIITQSVK NIEKSANSVQ NAQISKSAHR EVKKSHTVSC KNKISNSTSD
     NYNSNQECSQ NSSRTTQTVK STISRNQKQI SIPTKVLPDS NVPHFESSRV QTRSGTQNEI
     ASDLSNNQVS FNSGAGLTEG GCAEIENQLG HGNKTAVNTL NNFETENNLS ENESEHSNQE
     GESPDFSGMK LNGGKVILRK ARLKLDNKCL AGTEGPFSTT STSNTMGGST NLGLTGTIKC
     GVCGAVRFYR FVKQARKFGI HSCESCRKFI SKMIKRQACA KSSNNVLPIL QCHKGDGLCL
     VPPVVRSQQW NLMRCVYKAR CPACWLKMCL KCYNIPPPLR TGLNALLPPL MRDPLSISLP
     LGQDEDGQGQ KLCSSKLSWP AEDSSERNLF KSAMSWRNFE MGHKTSYQGT GGFLYTKIDK
     FDSSMSISPN KKRRKNNRIK VRKKIKNPVV ASSSASQQSQ PLRQRLELKG PRVKHVCRSA
     SVALGQPIAT FPTVDAKEDN EHGKNIPKTV KENERIEKRD DVKEKEIQKH NEDNNLNLNV
     NTTQQSHSRR GKPQQNVSTL HFPVSKAVMD TVYTVSIDFW EQYDPSEVGA KGFALIGSEL
     FHIPAICYLC GSAGKEPLIH CQCCCEPYHA FCLEPSEWNA CAQPNWCCPR CTICQSCHLR
     SGPKLSCIRC RQSFHHSCLS KSGVSSRLYS PDRPYVCQSC IKCKSCGSEG VNVHVGNLPL
     CSMCFKLRQQ GNYCPLCQRC YNENDFDTKM MECSECSCWV HARCEGLSDE RYQILSYLPD
     SIEFTCSQCS SNSSSSIWRN AIEAELKAGF IGVIKSLSKN RKICTALKWS PRKECLCRPV
     LSVRKLEFPE EDKNETNCTK ENEESEECNG DKSIDIDSSS SANYRDGMNK PDLEEHSIDN
     PIRKGLRRLR QKFHLKECSV RVKNCVPKDS QDNEKKDLIN QDSLVSSTST DGTECHCSEQ
     QIIARPSPTL MSVKRKVNSN EYKSLLQFHC DMMHVINRVG SKDLIETYHE ILQEVFPWFI
     PKNFKSSDNN DDTLMPTKDV GEDIALTTKF DDPILEAWKE EVMKAPKAIA AKTANLYNIH
     VEDSRSCCLC KGLGDGHETK EGRLLYCGQN EWVHANCALW SNEVFEEIDG SLQNVHSAIS
     RGRLIRCSEC GKKGASIGCC AKNCSNTFHF PCARNVGLAF NDDKTVFCIS HSNTSHVYKS
     LQNENEFSLK RPVYVELDRK KKKFAEPNKV KLMIGSLMVD CLGTVIPEFS DTAEKIIPCD
     YKCSRLYWST VNPYKIVRYY IRTYVQVYMP DVSSDMENNI TIDHSKEQEK DEVPTDYLAV
     KQTLDALIDF VCNKEVDENL AEQNNTDLLP PELKEAIFED LPHDLLDGIS MQDIFPKMSY
     EDFLAMDLKN DGSFSTDLFK DDMLSSEVEE TIKPSESKIS KIDSSLLELG AHNDLWVRLE
     AKTAMQDLMD DLFNSKSQKR GGRELKRSKS EVMSNNPLIV GGQRHHQRSC SLTWSCKLDN
     TYGSNIKRRK LPRNPSSTKS SETGLIVLDA QNERTSMFHE LRIPESIMVT VGRGNTPNIL
     SDSVRELKYC IEDSAGLNRR VLPARDDVKE HKRLLWHPRQ QQPRIVQVDG SVDANSASEC
     SSPEYNAEEK NANLQTSESL SIPQLDGIND EHSSDASESS SEMELGLYAR PSNLLHSKRI
     FGFIRSHVSS NCDKKTKSGN SNFITAPTIR CTSHKAEVLF KEKNLKMNLQ IPQVDGAGDI
     SSDDECVSSQ HMMTHERLLH TSYESSPFED IDVTCKRCGL TYRNEESYNR HLNNCDTMIT
     SDSDSETMDN KLASPESGFS PNMGSMSSQF ITLSPSEGHT LTTDYSDIQA TSPIEASVAS
     PHPSIQIEPI AQAIITPQIH ATHATVETVH QTVLTSNDVI VQTQYTRRTT TLPNPAVLPP
     QESTVQITEI TDPPSISSDS NATAHGIVNT PMSSPDSTSS QTVPSPEMSP SFSSMGVQTA
     HESMQTNAQI TRTSSKKNLR VAKPKTKNIK PQQHVLKNVI QSPQNIAHNV KFQPTTMSNG
     PPVIQLHQTT PRPPTVILQQ VASPGIVSAY VEALQQQSGQ NLQYITTIGD GQHETGFKPQ
     LIAANSLVPG TYIQAPSTDN LLLQNGGISI LPSVQIAQTQ PTVLGTIIQQ QPNAIQCGVI
     SSEQLLLSST PTLEMFADPT GGMFVSNQPM YYGLETIVSN TVMSSSQFMT GTVPQVLASS
     YQTTTQVFQA SKLMEPIVDV QAMSGVPTVT TMQNVSSMPN ISGMPNITGV SNIASMQNVS
     GMSNMSGVPY VVVNQSAPSL PPAAAPVPSP APTLASAPMP ASASIPAPMS IPTPVSIPTP
     VSIPTPVSLP TPMSIPTPVS IPTPVSIPTS VSMPAPISIS ASTLAVEPIV TPPQINISAT
     SPERAYGGIA CNVVTPVPCQ NATIEHPMAS IQVADVCSSN ATSISVMTPT KLSSSALPTI
     PRVAVRPSPV THLVQANHGA WKITEPLFGA EQPMNNSVRP YFDSKHVSEN TSMIKSSISS
     SKIPPLSNHY VTQRNLVLNH KSNHDVNSIH KSYSNGIALN PNSMNTCINN NNPIIVSNSN
     SVQNKITMPT NNMPTSRPMN RVLPMQAVTL KQDPAKKDDL AIEEPTKPVI KPAEPEIVES
     KKEIIEQIVQ IKKPETALSN ISDNIKLNTE TIEKVKENLK LELDKEKLQN TSLKIVLQKQ
     LQDGSYKITR NMKAVTQSKK TPQVTSVEIL PSKQVPQIAS LQLLPIKTFT LKANKFEDKV
     KPMDAKVNIL KAKAPPVAVK KPRIVTKSIR PLRNNPQQNP PQMHNCSKGP ILMYEIKSQD
     GFTHTASSMT EVWETVYQAV QNARKVHNLS PLPHNPLSEG LGLENNAAIY LIEQLPGVNR
     CSKYKPKFHT LEPPKPDEME NELPAACANG AARAEPFKGR KVHDMFSWLA SQHRPHPNII
     TISETESRRA VSTNLPMAMR FRILKETSKA SVGVYYSHIH GRGLFCLRDI EPGEMVIEYA
     GEVIRSSLTD KREKYYDSKN IGCYMFKIDD HLVVDATMKG NAARFINHSC EPNCYSRVVD
     ILGKKHILIF ALRRIIQGEE LTYDYKFPFE DIKIPCTCGS RKCRKYLN
//
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