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 26-FEB-2020, entry version 141. 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; Holometabola; 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 trimethylates 'Lys-9' of CC histone H3 (H3K9me3). H3 'Lys-9' methylation represents a specific tag CC for epigenetic transcriptional activation. Functions in segment CC determination through interaction with genes of bithorax (BX-C) and CC antennapedia (ANT-C) complexes. Acts as an activator of BX-C. Involved CC in the very early regulation of homeotic genes expressed only in the CC posterior region of 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 FlyBase; FBgn0014844; Dvir\trx. DR ChiTaRS; trx; fly. DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 2. 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; 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 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 3767..3768 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000250" FT COMPBIAS 28..41 FT /note="Poly-Ala" FT COMPBIAS 66..71 FT /note="Poly-Asp" FT COMPBIAS 160..164 FT /note="Poly-Asp" FT COMPBIAS 173..182 FT /note="Poly-Ala" FT COMPBIAS 221..228 FT /note="Poly-Gln" FT COMPBIAS 243..251 FT /note="Poly-Ala" FT COMPBIAS 253..258 FT /note="Poly-Thr" FT COMPBIAS 292..296 FT /note="Poly-Ala" FT COMPBIAS 538..546 FT /note="Poly-Asp" FT COMPBIAS 1072..1075 FT /note="Poly-Glu" FT COMPBIAS 2483..3271 FT /note="Gln-rich" FT COMPBIAS 3333..3339 FT /note="Poly-Asp" FT METAL 3770 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 3816 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 3818 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 3823 FT /note="Zinc" FT /evidence="ECO:0000250" FT BINDING 3700 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 3702 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 3744 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" 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 //