ID A0A151X0H3_9HYME Unreviewed; 3380 AA.
AC A0A151X0H3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Histone-lysine N-methyltransferase trithorax {ECO:0000313|EMBL:KYQ53432.1};
GN ORFNames=ALC60_07442 {ECO:0000313|EMBL:KYQ53432.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ53432.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ53432.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ53432.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ53432.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ982629; KYQ53432.1; -; Genomic_DNA.
DR STRING; 64791.A0A151X0H3; -.
DR Proteomes; UP000075809; 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:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 1.20.920.10; Bromodomain-like; 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; IPR036427; Bromodomain-like_sf.
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KYQ53432.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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, ECO:0000313|EMBL:KYQ53432.1};
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 906..956
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 953..1005
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1033..1094
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1366..1474
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 3242..3358
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3364..3380
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 112..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1928..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2215..2282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2215..2280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3380 AA; 374858 MW; ED504E30EC31A60A CRC64;
MGRSKFPGKP PKTATRKRIK VLGQPEAAQN DPVTVAENIY YGLSLFNETF GDNEKEHPPF
HGFSTKEANL SASYIKTQQH DAEKTSDRLP SVTVENLAPQ SSTKKDVIDV KNSPTDIENS
TEKFTNSNPK PVKDVTRLQP VTNPNTKHSK IHRAKSRKNC KNIKFSNYLK NPVLKSVNNI
LDQHQRTRQL RNSTAKRLLQ RAKSGNNTRN LVVQSGEKPS TVRKFVLPVR SVHSSRVIKP
NKRFIEELEE ISTTEYSENE IGVHVKKTKL NSDKLSNLES KLKGDTVSKL CTKFKEARSK
PKRVIQSVDS NAEITQSVKN IEKSANSVQN TQISKPAHRE VKKPHTISCK NKVSNSTSDN
SNSNQECSQN SSRTTQTVKS TISRNQKQIS IPTKVLPDSN VPHFESSRVQ TRSGTQNEIA
SDLINNQVSF DSGAGLTEGG CAETENQLGH GNKTAVSTFN SFETENNLSE SESEHSNHSE
GEPSDFSGMK LHGGKVILRK ARLKLDNKCL AGTEGPFSTT STSNTMGGST NLGLTGTIKC
GVCGAVRFYR FVKQARKFGI HSCESCRKFI SKMIKRQACA KSSNNVLPIL QCHKGDGLCL
VPPVVRSQQW NLMRCVYKAR CPACWLKMCL KCYNIPSPLR TGLNALLPPL MRDPLSISLP
LGQDEDGQGQ KLCSSKLSWP AEDSSERNLF KSAMSWRNFE MGHKTSYQGT GGFLYTKIDK
FDSSMSISPN KKRRKNNRIK VRKKIKNPVV ASSSGSQHSQ SLRQRLELKG PRVKHVCRSA
SVALGQPIAT FPTVDAKEDN EHGKNIPKTV KEIERIEKRD DIIKEKEIQK HNEDNNLNLS
VHTVQQSHSR RGKPQQSVST LHFPGVSKAA VDTVYTVSID FWEQYDPSEV GAKGFALIGS
ELFHIPAICY LCGSAGKEPL IHCQCCCEPY HAFCLEPSEW NACAQPNWCC PRCTICQSCH
LRSGPKLSCI RCRQSFHHSC LSKSGVSSRL YSPDRPYVCQ SCIKCKSCGS EGVNVHVGNL
PLCSMCFKLR QQGNYCPLCQ RCYNENDFDT KMMECSECSC WVHARCEGLS DERYQILSYL
PDSIEFTCSQ CSSNSSSSIW RNAIEAELKA GFIGVIKSLS KNRKICTALK WSPRKECLCR
PVSSVRKLEF PEEDKNETNC MKDANYRDGT NKPDLEEHSI DGPVRKGLRR LRQKFHLKEC
SVRVKNCLPK DNLSQDNERK DWSNQDSSVS STDVTECHCS EQQIIARPSP TLMSVKRKVN
SNEYKSLLQF HCDMMHVINR VDSRDLIETY HDILQEVFPW FTPKNFKSSD DNDDTLTATK
DVGEDIALTT KFDDPILEAW KEEVMKAPKA IAAKTANLYN IHVEDSRSCC LCKGLGDGHE
TKEGRLLYCG QNEWVHANCA LWSNEVFEEI DGSLQNVHSA ISRGRLIRCS ECGKKGASIG
CCAKNCSNTF HFPCARNVGL AFNDDKTVFC ISHSNTSHVC KSLQNENEFS LKRPVYVELD
RKKKKFAEPN KVKLMIGSLM VDCLGTVIPE FSDTAEKIIP CDYKCSRLYW STVNPYKIVR
YYIRTYVQVH MPDVSSDMEN NITIDHSKEQ EKDEVPTDGT YLVVKQTLDA LIDFVCNKEV
DENLAEQNNT DLLPPELKEA IFEDLPHDLL DGISMQDIFP KMSYEDFLAM DLKNDGSFST
DLFKDDMLSS EVEETIKPSE SKISKIDSSL LELGAHNDLW VRLEAKTAMQ DLMDDLFNSK
SQKRGGRELK RSKSEVMSNN PLIVGGQRHH QRSCSLTWSC KLDNTYGSNI KRRKLPRNPS
STKSSETGLI VLDAQNERTS MFHELRIPES IMVTVGRGNT PNILSDSVRE LKYCIEDSAG
LNRRVLPARD DVKEHKRLLW HPRQQQPRIV QVDGSVDANS ASECSSPEYN AEEKSTSLQT
SESLSIPQLD GINDEHSSDA SEPSSEMELG LYTRPLNLLH SKRIFGFIRS HVSSNCDKKM
KNGNSNLITA PIIRCTSHKA EVLFKEKNLK VNLQIPQVDG AGDISSDDEC VSSQHMIAHE
RLLHASYESS PFEDIDVTCK RCGLTYRNEE SYNRHLDNCD TMITSDSDSE TMDNKLASPE
SGFSPNMGSV SSQFITLSPS EGHTLTTDYT DIQATSPIEA SVASPHPSMI EPIAQAIITP
QIHATHATVE TVHQTVLTSN DVIVQTQYTR RTTTLPNPAV LPPQESTVQI TEITDPPSIS
SDSNVTAHGI VNTPMNSPDS TSSQTVPSPE MSPSFSSMGV QTAQESMQTN AQITRTSSKK
NLRVAKPKIK NIKPQQHVLK NVMQSSQNVA HNVKFQPTAM SNGPPVIQLH QTTPRPPTVI
LQQVASPGIV SAYVEALQQQ SGQNLQYITT IGDGQHETGF KPQLITANSL VPGTYIQAPS
TDNLLLQNGG ISILPSVQIA QTQPTVLGTI IQQQPNAIQC GVISSEQLLL SSTPTLEMFT
DPTGGMFVSN QPMYYGLETI VSNTVMSSSQ FMAGTVPQVL ASSYQTTTQV FQASKLMEPI
VDVQAMPGVP TVTTMQNVSS MPNISGMPNI AGVPNIASMQ NVSGMSNMSG VPYVVVNQSA
PPLPPAAAPV PSPAPTLASA PMPASASIPA PVSIPTPVSI PTPVSIPTPI SIPTPVSMPA
PISISASTLA VEPIVTPPQI NISATSQDRA YGGIACNVVA PVPCQNATIE HPMASIQVAD
VCSSNATSIS VMTPTLPPPP SSVLPPHAMP TIPRVAVRPS PVTHSVQANH GTAWKITEPL
FGAEQPMSNS VRPYFDSKHV SENTSMIKSS ISSKIPPLSN HYVTQRNLVL NHKSNHDVNS
VHKSYSSGTA LNPNSVVNAG INNSPIVVSN SNSVQNKITM PTNNMPTSRP MNRVLPMQAV
TLKQDPAKKD DLAIEEPTKP VIKPAEPEIV ESKKEIIEQI VQIKKPETTL SNITDNIKLN
TETIEKVKEN FKLELDKEKL QNTSLKIVLQ KQLQDGSYKI TRNMKAVTQS KKTPQVTSVE
ILPSKQVPQI ASLQLLPIKT FTLKANKLED KVKPMDAKVN ILKAKAPPVA VKKPRIVTKS
IRPLRNNPHQ NPPQMHNCSK GPILMYEIKS QDGFTHTASS MTEVWETVYQ AVQNARKIHN
LSPLPHNPLS EGLGLENNAA IYLIEQLPGV NRCSKYKPKF HTLEPPKPDE MENELPAACA
NGAARAEPFK GRKVHDMFSW LASQHRPHPN IITISETESR RAVSTNLPMA MRFRILKETS
KASVGVYYSH IHGRGLFCLR DIEPGEMVIE YAGEVIRSSL TDKREKYYDS KNIGCYMFKI
DDHLVVDATM KGNAARFINH SCEPNCYSRV VDILGKKHIL IFALRRIIQG EELTYDYKFP
FEDIKIPCTC GSRKCRKYLN
//