TRX_DROVI
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}.
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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
