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 31-JAN-2018, entry version 131. DE RecName: Full=Histone-lysine N-methyltransferase trithorax; DE EC=2.1.1.43; GN Name=trx; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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 RT between Drosophila virilis and Drosophila melanogaster."; RL Mech. Dev. 53:113-122(1995). CC -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone CC H3. H3 'Lys-4' methylation represents a specific tag for CC epigenetic transcriptional activation. Functions in segment CC determination through interaction with genes of bithorax (BX-C) CC and antennapedia (ANT-C) complexes. Acts as an activator of BX-C. CC Involved in the very early regulation of homeotic genes expressed CC only in the posterior region of the embryo (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] = CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. 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 CC methyltransferase superfamily. Histone-lysine methyltransferase CC family. TRX/MLL 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 ProteinModelPortal; Q24742; -. DR SMR; Q24742; -. DR FlyBase; FBgn0014844; Dvir\trx. DR OrthoDB; EOG091G001U; -. DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblMetazoa. DR GO; GO:0044665; C:MLL1/2 complex; IEA:EnsemblMetazoa. DR GO; GO:0005700; C:polytene chromosome; 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:0004402; F:histone acetyltransferase activity; IEA:EnsemblMetazoa. 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:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:EnsemblMetazoa. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; IEA:EnsemblMetazoa. 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:0043966; P:histone H3 acetylation; IEA:EnsemblMetazoa. DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblMetazoa. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.20.920.10; -; 1. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 3.30.40.10; -; 4. 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; IPR015943; WD40/YVTN_repeat-like_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 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; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 3828 Histone-lysine N-methyltransferase FT trithorax. FT /FTId=PRO_0000124875. FT DOMAIN 1856 1913 FYR N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00875}. FT DOMAIN 3493 3577 FYR C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00876}. FT DOMAIN 3690 3806 SET. {ECO:0000255|PROSITE- FT ProRule:PRU00190}. FT DOMAIN 3812 3828 Post-SET. {ECO:0000255|PROSITE- FT ProRule:PRU00155}. FT DNA_BIND 725 839 Nuclear receptor. {ECO:0000255|PROSITE- FT ProRule:PRU00407}. FT ZN_FING 1251 1334 PHD-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT ZN_FING 1335 1380 PHD-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT ZN_FING 1408 1469 PHD-type 3. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT ZN_FING 1708 1748 C2HC pre-PHD-type. {ECO:0000255|PROSITE- FT ProRule:PRU01146}. FT ZN_FING 1769 1816 PHD-type 4. {ECO:0000255|PROSITE- FT ProRule:PRU01146}. FT REGION 3767 3768 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT COMPBIAS 28 41 Poly-Ala. FT COMPBIAS 66 71 Poly-Asp. FT COMPBIAS 160 164 Poly-Asp. FT COMPBIAS 173 182 Poly-Ala. FT COMPBIAS 221 228 Poly-Gln. FT COMPBIAS 243 251 Poly-Ala. FT COMPBIAS 253 258 Poly-Thr. FT COMPBIAS 292 296 Poly-Ala. FT COMPBIAS 538 546 Poly-Asp. FT COMPBIAS 1072 1075 Poly-Glu. FT COMPBIAS 2483 3271 Gln-rich. FT COMPBIAS 3333 3339 Poly-Asp. FT METAL 3770 3770 Zinc. {ECO:0000250}. FT METAL 3816 3816 Zinc. {ECO:0000250}. FT METAL 3818 3818 Zinc. {ECO:0000250}. FT METAL 3823 3823 Zinc. {ECO:0000250}. FT BINDING 3700 3700 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00190}. FT BINDING 3702 3702 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00190}. FT BINDING 3744 3744 S-adenosyl-L-methionine. FT {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 //