GenomeNet

Database: UniProt/TrEMBL
Entry: B4LCM2_DROVI
LinkDB: B4LCM2_DROVI
Original site: B4LCM2_DROVI 
ID   B4LCM2_DROVI            Unreviewed;      2361 AA.
AC   B4LCM2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Histone-lysine N-methyltransferase ash1 {ECO:0008006|Google:ProtNLM};
GN   Name=Dvir\GJ11874 {ECO:0000313|EMBL:EDW69885.2};
GN   ORFNames=Dvir_GJ11874 {ECO:0000313|EMBL:EDW69885.2};
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 {ECO:0000313|EMBL:EDW69885.2, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW69885.2, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH940647; EDW69885.2; -; Genomic_DNA.
DR   RefSeq; XP_002047543.2; XM_002047507.2.
DR   SMR; B4LCM2; -.
DR   STRING; 7244.B4LCM2; -.
DR   EnsemblMetazoa; FBtr0437490; FBpp0394313; FBgn0199128.
DR   GeneID; 6622796; -.
DR   KEGG; dvi:6622796; -.
DR   eggNOG; KOG1083; Eukaryota.
DR   HOGENOM; CLU_229222_0_0_1; -.
DR   InParanoid; B4LCM2; -.
DR   OrthoDB; 2882778at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0035097; C:histone methyltransferase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018991; P:egg-laying behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IEA:EnsemblMetazoa.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:EnsemblMetazoa.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:EnsemblMetazoa.
DR   CDD; cd04717; BAH_polybromo; 1.
DR   CDD; cd15548; PHD_ASH1L; 1.
DR   CDD; cd19174; SET_ASH1L; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR043319; PHD_ASH1L.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   PANTHER; PTHR46147:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00384; AT_hook; 3.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1461..1509
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          1512..1628
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1636..1652
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          2075..2195
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2241..2276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2335..2361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1684..1711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        12..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2250..2276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2361 AA;  259475 MW;  FC375AC51DD16A38 CRC64;
     MSSGQNEASA AAKKEKVLEA QQRTQESGSE NEETDSITDQ SSQSKSTKSA TQFSVQRSDT
     DGLRMKISAI RNPPSTTATS LTNSTATKET TKTALTTVEN SSRKKLAKVR KMSEAQELSG
     CSADGKEKHR EKEKERDKML STVNTTKKIK VKRKKIAQKS SSSSSNNNNN NSKTLRKPAA
     AFSSDSEDDL PLKVHMQRAP RLLLTAIGGS QGQGENHMGI SSSDNEELVR AADLVKAAIK
     RVESDAEDNA SVAAGVAAAK IKQQLPQYQS TLLKDFMEKT QRLNQPGHAT SLPKAAMQPS
     AAAAAAAAVN NSSSNNNTLS QPLQRKRRGR PKKLQPTVAT SAPAALPVAV PTINESADSG
     VISTTPSPKM QQLLISDNAK PKIDMAYLDK RMYATAERVL YPPPRSKRRQ GNKKVNKEEL
     QVDPLWRKID VNKKFRLRTV SGYKSDGGGG GGTSNTICSK ILAAKSGYVS DYGSVRHQRH
     NHNSGYKSDA SCKSRYSSRS CASRRMSRAK SCGYRSDCKE SSGKSSKSLR RRRRASMLRS
     GHEQATQALS DEHDQDILQL AGLSLGQSSE ESNEYISKPS LKCLPSTSAS KKYGEINRFV
     ATGQYFSGAA KPTTTSVAAG ANTTTTTTTT AADNFIQGKM LLQRKHSISQ DTMLPGKSAC
     KIKSRRSSAA SMCSSYVSGA SRVRRRHRRK SFSHAKSLNI DSKLLTEIDI IASTFHARCR
     IQDDRLTASS GKEKLLAEAN KLQATLTAPI AATLPLLNGG GGGGSNSTTS AAATTKPLKR
     ALKKRKLNEP LIDFAMLSAS AGNSNGISNN NSSSSNGAKR RHKKSSSNSG GSNSSSPDDH
     KLPLKKRHYL VTTGAEVASA FASNGKLNAE AWAAAAAAAK SSANTKAQAQ FNAKKLTPKK
     RHLLVSQEVA SGAAATAGSA SPLRIVVDNN SISGGKLLDI SPSSLCSLKQ QRRQGAKAKN
     LLVASAGAVA RELPQQLQSP AGSSSCPPPG IFEPSVELEI QIPIAKLNES VITKSEVESP
     LLAALDIKED ANKKEQCQRV LETLLHKTGG NLLLKRKRKK INRTGFPTVR RKKRKVSVEH
     TLLPQQQQQQ QLEQQQQQLP ARETRSSSTL AAALTMDCER VPKTGEAQET FVARSSNQRT
     PRLSVVALER LQRPQTPANS GGNARGRPRG RGRPKLQKPQ PPAPQQQQQQ SHPVAQLLEV
     QPAKKRGRAA KQTELLVPRL ERKLEPSIKL PAGIDPNTNF SCKIRLKRRK TIQQEAVKQL
     EPAKQPEQQL RLDVSTPLAT SDDRMQIAAE AAAKRSQQPV PASEHEPLPA QESTLNLATD
     YGSCSDTSED KCSTASQRKR TKLKKNFLVA GLFSNYFKQL PAGAAATVPS TAVAVKQPNR
     KATDGEQTEQ QQPQVSVLLP PPSYCERYFR RTLNDFELPY DIWWAYSHDK LPTRHVVPSW
     NYRKIRTNVY AESVRPNLAG FDHPNCNCKP QASGACLDNC LNRMVYTECA PSNCPAGDKC
     RNQKIQRHEV APGVERFMTA DKGWGVRTKL PIAKGTYILE YVGEVVTERE FKQRMASIYL
     NDTHHYCLHL DGGLVIDGQR MGSDCRFVNH SCEPNCEMQK WSVNGLSRMV LFAKRAIEQG
     EELTYDYNFS LFNPSEGQPC RCNMPQCRGV IGGKSQRIKP LPAELKTTAG AESAAAGLKE
     ANGNQHGRQR KHKAKKNAQR LQQAAKEAMV VARVQQLSER EKKLVKQCNI FLVRNFEKIR
     RCKAKRAAAK AQAAASPAAG DSDLPGRRPS TPSSSSLLAA QISALCTPRN MKTRGLTQAV
     QDPELEKMAK MAVVLRDICT ALESLKMFDL LSTLPSSKKK KQLKTTRLDF KTIQAQVEQG
     HYKTPQAYDE HMLQLFAEAR QLHGDDEGKS NALQTLLESY TQQKAANYAQ LLDILGKPEA
     LHSFKPKEEE EEKVAELATA TDQSQENIKP STKVIASATP ETSAAVDVGP ELPPTDEEDV
     IRCICGLYKD EGLMIQCAKC MVWQHTECTK ADIDADNYQC ERCEPREVDR EIPLDEYTEE
     GHRYYLSLMR GELQVRQGDA VYVLRDIPIK DETGKVLPSQ KHTYETIGAI DYQECDIFRV
     EHLWKNEAGK RFIFGHHFLR PHETFHEPSR RFYPNEVVRV SLYEVVPIEL VIGRCWVLDR
     TTFCKGRPME CNDEDHCYIC ELRVDKTARF FSKAKANHPA CTKSYAFRKF PEKLKISKSY
     APHDVDPSLL KTRKQKTDIE VGATPIKMSR HEQKTGQTTG NRKQRNTQAG TATGATASTQ
     VPVQVLTPVA PNGQVLKKKR SRLENVLNTM KLKCLDAQTA QEQPIDLSYL LSGRGARQRK
     TNCTSNGGSS SNNNNSATPC A
//
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