ID TRX_DROVI Reviewed; 3828 AA. AC Q24742; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-AUG-2022, entry version 150. DE RecName: Full=Histone-lysine N-methyltransferase trithorax; DE EC=2.1.1.355 {ECO:0000250|UniProtKB:P20659}; GN Name=trx; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila. OX NCBI_TaxID=7244; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8555104; DOI=10.1016/0925-4773(95)00429-7; RA Tillib S., Sedkov Y., Mizrokhi L., Mazo A.; RT "Conservation of structure and expression of the trithorax gene between RT Drosophila virilis and Drosophila melanogaster."; RL Mech. Dev. 53:113-122(1995). CC -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' of histone CC H3 (H3K4me). H3K4me represents a specific tag for epigenetic CC transcriptional activation. Functions in segment determination through CC interaction with genes of bithorax (BX-C) and antennapedia (ANT-C) CC complexes. Acts as an activator of BX-C. Involved in the very early CC regulation of homeotic genes expressed only in the posterior region of CC the embryo. {ECO:0000250|UniProtKB:P20659}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA- CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; CC Evidence={ECO:0000250|UniProtKB:P20659}; CC -!- SUBUNIT: Interacts with ash1 via its SET domain. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. TRX/MLL CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. 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; Z50038; CAA90349.1; -; Genomic_DNA. DR PIR; T13857; T13857. DR SMR; Q24742; -. DR STRING; 7244.FBpp0237016; -. DR PRIDE; Q24742; -. DR eggNOG; KOG1084; Eukaryota. DR ChiTaRS; trx; fly. DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblMetazoa. DR GO; GO:0044665; C:MLL1/2 complex; IEA:EnsemblMetazoa. DR GO; GO:0005704; C:polytene chromosome band; IEA:EnsemblMetazoa. DR GO; GO:0008023; C:transcription elongation factor complex; IEA:EnsemblMetazoa. DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:EnsemblMetazoa. DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa. DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:EnsemblMetazoa. DR GO; GO:0106363; F:protein-cysteine methyltransferase activity; IEA:EnsemblMetazoa. 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:0001654; P:eye development; IEA:EnsemblMetazoa. DR GO; GO:0008354; P:germ cell migration; IEA:EnsemblMetazoa. DR GO; GO:0007482; P:haltere development; IEA:EnsemblMetazoa. DR GO; GO:0007507; P:heart development; IEA:EnsemblMetazoa. DR GO; GO:0043966; P:histone H3 acetylation; IEA:EnsemblMetazoa. DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:EnsemblMetazoa. DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblMetazoa. DR Gene3D; 1.20.920.10; -; 1. DR Gene3D; 2.170.270.10; -; 1. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR034732; EPHD. DR InterPro; IPR003889; FYrich_C. DR InterPro; IPR003888; FYrich_N. DR InterPro; IPR016569; MeTrfase_trithorax. 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 Pfam; PF05965; FYRC; 1. DR Pfam; PF05964; FYRN; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF00856; SET; 1. DR PIRSF; PIRSF010354; Methyltransferase_trithorax; 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; SSF57903; 2. DR SUPFAM; SSF82199; SSF82199; 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; PS01359; ZF_PHD_1; 3. DR PROSITE; PS50016; ZF_PHD_2; 3. PE 3: Inferred from homology; KW Activator; Chromatin regulator; Developmental protein; DNA-binding; KW Metal-binding; Methyltransferase; Nucleus; Repeat; S-adenosyl-L-methionine; KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. FT CHAIN 1..3828 FT /note="Histone-lysine N-methyltransferase trithorax" FT /id="PRO_0000124875" FT DOMAIN 1856..1913 FT /note="FYR N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875" FT DOMAIN 3493..3577 FT /note="FYR C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876" FT DOMAIN 3690..3806 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 3812..3828 FT /note="Post-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155" FT DNA_BIND 725..839 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 1251..1334 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 1335..1380 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 1408..1469 FT /note="PHD-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 1708..1748 FT /note="C2HC pre-PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 1769..1816 FT /note="PHD-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 25..179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..390 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 512..589 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 933..1036 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1075..1094 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1131..1170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2252..2272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2464..2510 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2826..2848 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2897..2973 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2988..3031 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3117..3178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3314..3338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3457..3487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..61 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 69..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 97..122 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 358..390 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 528..553 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 561..585 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 957..978 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 980..1033 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1137..1170 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2480..2510 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2897..2930 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2956..2973 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3117..3164 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 3700 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 3702 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 3744 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 3767..3768 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 3770 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 3816 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 3818 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 3823 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 3828 AA; 413724 MW; 32059CF303A3C504 CRC64; MGRSKFPGNP SKSINRKRIS VLQLEDEAAS AAAAAAAATA ATTEQHQQSE QSAGSSASRE KGNNCDNDDD DNAPSGAATS GNRGASSGAS DAAPEGGNSY GNGSSTGSKT TNGGNVNGGS HHKSATAPAE LKECKNQGNQ IEPNNCIAAE PDGTEDTNND DDDDSSNDKK PTAAAAAAAA AAFVPGPSAL QRARKGGNKK FKNLNLARPE VMLPSTSKLK QQQQQQLQLN CPSASASSLS SSAAAAAAAA APTTTTTTAS ASATLTATAT STSTSSLPGT PLSVIAGGGG GAAAAALLLA NPFASVETKV VEVNAAATAA ATAAATAAAG AGEDVGMLKA SIEMANEAGL EAPAVAVKSS GSSPNPNHNP NAVAGSTSAA APGAPTATKQ KKTVTFKNIL ETSDDKSVVK RFYNPDNRVP LVSIMKKDSL NRPLNYCRGS EFIVRPSILS KILNKNSNID KLNSLKFRSV HASSNSIQES SSSTTNLFGS GLSRAFGAPI DDEDAVSGGV TFRKQEPQHK TPEDNDDDGS ASSDAIEDDE DIDDDDAEEN EEAASEKSAE TTASVDEKEA DDRQLVMDKH FVLPKRSTRS SRIIKPNKRL LEVGGICSKR SPSDANGKPK PKNYFGLATL PAKCTPRRRR SAATALSQKL GKETFASFAT AKVNSSFVLR QPRLQFQTDK SRSFVSAKPT LPTTTVLPAS SSAITSANVL SFGALNNANS AVAAASTCAV CSAPVNNKDA PLARKYGVIA CEVCRKFNSR MTKISKLSTP MHSNPSTSTA QSGQQLKCTD GGNCSILSLK SQLKNFKKLY KERCKACWLK KCLATLQLPA GHRSRLSAIL PASMREEVAP KDDKCPELLS PTASLRFTAP TSSASSGTTI KWKSSAETAV NSIKSNPLAE NNVTFGGTPL LRPAILEKPL FLKIGSDNKK AKESKEALGL SPVPSTSEAA VAPGKTTRKA KQDKEKAREL EAEKPLSPNA KKTTEANTPE TQKDEQPAST TTTVSAASSS TSHTSSAATN SSQLETTEAA NASAVPDNLK RQRIDLKGPR VKHVCRSASI VLGQPLATFG DEEEELAAAE AGPAPTTTTT TTSPEVIIKK PKSPQPMQMI IDENDNCASC ILTPTEATAE AQPAVKSVLE SRSSKSNTQT EAKKTPATSG SSKGKVTTRN ATATVTSVAS SLVATKKQRN IEVSSSISSS QAAATQSRRA LAKEVNRLKA LISIDFWENY DPAEVCQTGF GLIVTETVAQ RALCFLCGST GLDPLIFCAC CCEPYHQYCV LDEYNLKHSS FEDTLMTSLL ETSNNACAIS AATNTALNQL TQRLNWLCPR CTVCYTCNMS SGSKVKCQKC QKNYHSTCLG TSKRLLGADR PLICVNCLKC KSCATTKVSK FVGNLPMCTA CFKLRKKGNF CPICQKCYDD NDFDLKMMEC GDCNQWVHSK CEGLSDEQYN LLSTLPESIE FICKKCARRC DVSRNKADEW RQAVMEEFKS SLYSVLKLLS KSRQACALLK LSPRKNWRCC SAGAQPAKAH SQGKLQPKAL QFTYNGLGSD GESQNSDDIY EFKEQHSTNR KPSTPVPCSC LQPLSQSPSF SLVDIKQKIA SNAYVSLAEF NYDMSQVIQQ SNCDELDIAY KELLSEQFPW FQNETKACTD ALEEDMFESC GYEELKESPT TYAEHHTASQ APRTGLLDIP LDDVDDLGGC AVKTRLDTRV CLFCRKSGEG LSGEEARLLY CGHDCWVHIN CAMWSAEVFE EIDGSLQNVH SAVARGRMIK CTVCGNRGAT VGCNVKSCGE HYHYPCARTI DCAFLTDKSM YCPAHARNAL KANGSPSVTY ESNFEVSRPV YVELERKRKK LIVPAKVQFH IGSVAVRQLG SIVPRFSDSF EAIVPINFLC SRLYWSSKEP WKIVEYTVRT TIQNSYSSTL TLDAGRNFTV DHTNPNCSLV QLGLAQIARW HSSLARSDLL DTDWAEFPNS YVPADENTEE EPQQNADLLP PEIKDAIFED LPHELLDGIS MLDIFMYEDL GDKTELFAMS EQSKDGTTAT SQAGGASVII CDEDTRNSNS LNKHLVLSNC CTASNPVDDA MLCAARSSSQ EKECGDVLKK TDTAPTRSWP KLDGGSVAAF KRRKLSKNIA EGVLLSLNQR SKKEMATVAG ITRRQSVCGS SELPAEGSAT MRTKSFTWSA AKCLFEKNES REEPAKLTIM QMDGVDDSIT EYRIIGSDGN LSTAQFTGQV KCERCQCTYR NYDSFQRHLG SCEPMSTSES ESETATGTAQ LSAESLNELQ KQALAAATLS NTGGLNYLQT SFPQVQNLAT LGQFGVQGLQ GLQTLQLQPQ SLGNGFFLSQ PNAAQATSNG NDVLQLYANS LQNLAANLGG GFTLTQPTMS TQAQPQLIAL STNPDGTQQF IQLPQSNGAT TQLLQTAAPL RCNATYQTLQ ATNSDKKIVL LFLEAGDPLQ EVVTQAAQQA TAAAHQKQLK SGHGVKPIQA KLQGQQQQQR HQQHQQHQQH QQQQQQQQQQ QQQQQTPITV AQHGGTTQLL GQNLLQPQLL FQSNAQPQTQ QLLLPQTQAQ NIISFVTGDG SQNQPLQYIS IPTTNDFKPQ QTTSTPTFLT APGGGATFLQ TDASGNLMLT TAPANSGLQM LTGQLQTQPQ VIGTLIQPQT LQLTTGADGT QTATAQQPLI LGGATGGGTT GLEFATAPQV ILATQPMYYG LETIVQNTVM SSQQFVSTAM PGVLSQNSSF SATTTQVFQA SKIEPIVDLP AGYVVLNNAV DASGNTSWLQ QSQTQATDDA TAQLLQNAGF QFQTTPTTST QQTMSTDYAP PLVVTAKVPP VAQMKRNTNA NKSPISVLSK VQPQPQQSQV VNKVLPTNVI QQQQQQQQQQ QQQQQQMQPK QQLAGNANLK LTSQFQRQQQ ANELKNKQAA GQQTGSTCGA PPSIASKPLQ KKTNLIRPIH KVEVKPKIMK QAPKLATSAA SMQHHQQQQS PAAINQVAKV ALLQQRLAPA PQPQQQEPQE EQQHLHQQQQ QQQQQQQHMQ QHQQQQQQLS MPQLLRAQQP IISIVNTAEP QAATQFVIRP ALQAQAQPIQ LQEQQSQQQQ QQPAEQLING KAARLQRYAS NSLPTNVVNP LQQQRCASAN NSSNSNVTQQ NSTITINSRP TNRVLPMQQR QEPTPLSNDV VVQSPTPPKP IEEPVPAGAS TQKPIVKCYA QLEQKSPGYE TELKTNITLD NLEQTNSITT MQLQQPQQGP IYGEQIFEKQ SEAQVQLEKP KHNDLMLLEA TSCQQQQQQQ QHMEMVVDNG FQLTSNESCL LEKHGFNVEA VPMDTEDHYA SMKNGSGGGA AEGIGQVDDA EEDEDDDDDF SLKMATSACN DHEMSDSEEP AVKEKISKIL DNLTNDDCSD SIATATTVEA SAGYQQMVED VLATTAAGSV STDDETFTAT AEAVEAAASY INEMAEAHEL QLKQLQAGVE LDLKKPKLDV PQQQPDTVPP NVVPTAAAPQ QPPPMRDPKK ISGPHLLYEI QSEDGFTYKS SSIAEIWEKV FEAVQVARRA HGLTPLPEGP LADMSGVQMI GLKTNALKYL IEQLPGVEKC VKYTPKYHKR NGNVSTAAGG GHARTAGSNP AALAAGAESL IDYGSDQEEL QENAYECARC EPYVSRSEYD MFSWLASRHR KQPIQVFVQP SDNELVPRRG TGSNLPMAMK YRTLKETYKD YVGVFRSHIH GRGLYCTKDI EAGEMVIEYA GELIRSTLTD KRERYYDSRG IGCYMFKIDD NLVVDATMRG NAARFINHSC EPNCYSKVVD ILGHKHIIIF ALRRIVQGEE LTYDYKFPFE DEKIPCSCGS KRCRKYLN //