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Database: UniProt
Entry: Q24742
LinkDB: Q24742
Original site: Q24742 
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   10-APR-2019, entry version 138.
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:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
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}.
DR   EMBL; Z50038; CAA90349.1; -; Genomic_DNA.
DR   PIR; T13857; T13857.
DR   ProteinModelPortal; Q24742; -.
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;
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
//
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