ID A0A0P8XY56_DROAN Unreviewed; 2109 AA.
AC A0A0P8XY56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JUN-2023, entry version 37.
DE RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
GN Name=Dana\GF17182 {ECO:0000313|EMBL:KPU79562.1};
GN Synonyms=dana_GLEANR_18446 {ECO:0000313|EMBL:KPU79562.1};
GN ORFNames=GF17182 {ECO:0000313|EMBL:KPU79562.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:KPU79562.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:KPU79562.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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,
CC ECO:0000256|PIRNR:PIRNR003047}.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000256|ARBA:ARBA00009064,
CC ECO:0000256|PIRNR:PIRNR003047}.
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DR EMBL; CH902617; KPU79562.1; -; Genomic_DNA.
DR RefSeq; XP_014766301.1; XM_014910815.1.
DR SMR; A0A0P8XY56; -.
DR EnsemblMetazoa; FBtr0390531; FBpp0350051; FBgn0094200.
DR GeneID; 6499969; -.
DR OrthoDB; 5482320at2759; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd05511; Bromo_TFIID; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR Gene3D; 1.10.1100.10; TAFII-230 TBP-binding domain; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR011177; TAF1_animal.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
DR InterPro; IPR041670; Znf-CCHC_6.
DR PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF09247; TBP-binding; 1.
DR Pfam; PF15288; zf-CCHC_6; 1.
DR PIRSF; PIRSF003047; TAF1_animal; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR SUPFAM; SSF47055; TAF(II)230 TBP-binding fragment; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003047};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR003047};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR003047}.
FT DOMAIN 1488..1558
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1610..1680
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2042..2068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2083..2109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1263..1297
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1857
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2109 AA; 237090 MW; 694CCD8E06D3B024 CRC64;
MDTGSDNSDD EGSIGNGGGD LGMDLTGILF GNIDSEGRLL DDEDGEGRGG SGFDTELREN
IGSLSKLGLD SMLHEVIDRR EAEPSSDEED SDKPEAADSG GMSAFDALKA GVKNNEGEDG
AVKAQDDAID YSDITELSED CPRTPPEQKE TASSSYDDLE DAIPASKVET KLTKDDKELM
PPPSAPVRSG TGSGTEETTK TTETSTTTSD SKAIDPKDAD RKLDTPLADI LPSKYQNVDV
RELFPDFRPQ KVLRFSRLFG PGKPTSLPQI WRHVRKRRRK RNQSRDQKPI NNAGSDSPSD
SEEPRKRGFS LHFGPEPTPA ECMSDDEDKL LGDLNSEDLR QEGPENGENS DQKPKVADWR
YGPAQIWYDM LEVSDSGEGF NYGFKTSQNK EDRRANSPEL ESPEQYIADD AFLMVSQLHW
EDDVVWDGND IKSKVMQKLN SKTNAAGWLP SSGSRTAGAF SQPGKTAIPV GGNSGNSNKG
SAASKKAQQN AQAKPAEAPD DTWYSLFPVE NEELIYHKWE DEVIWDAQQM TKVPKPKVLT
LDPNDENIIL GIPDDIDPSK INKNIGPPPK IKIPHPHVKK SKILLGKAGV INVLAEDTPP
PPPKSPDRDP FNISNDTYYT PKTEPTLRLK VGGGNLIQHS TPVVELRAPF VPTHMGPMKL
RSFHRPPLKK YSHGPLAMIS HHAVMPLLKH IAKKAKQREV ERIASGGGDV FFMRNPEDLS
GKDGDIVLAE FCEEHPPLMN QVGMCSKIKN YYKRKAEKDS GPQDYVYGEV AFAHTSPFLG
ILHPGQCIQA LENNMYRAPI YPHKMSHNDF LVIRTRTGYW IRAVNAIFTV GQECPIYEVP
GPNSKRANNF TRDFLQVFIY RLFWKSRDNP RRIRMDDIKK AFPAHSESSI RKRLKQCADF
KRTGMDSNWW VIKPEFRLPS EEEIRAMVSP EQCCAYFSMI AAEQRLKDAG YGEKFLFAPQ
EDDDEEAQLK LDDEVKVAPW NTTRAYIQAM RGKCLLQLSG PADPTGCGEG FSYVRVPNKP
TQSKEEQESQ PKRSVTGTDA DLRRLPLQRA KELLRKFKVP EEEIKKLSRW EVIDVVRTLS
TEKAKAGEEG MDKFSRGNRF SIAEHQERYK EECQRIFDLQ NRVLASSEVL STDEAESSAS
EESDLEELGK NLENMLSNKK TSTQLSLERE EQERQELLRQ LDEEHGDGAG GGAAAKAKAK
EEAAQQQPGA PSNQGRILRI TRTFKGNDGK EYTRVETVRR QPVIDAYIKI RTTKDEQFIK
QFATLDEQQK EEMKREKRRI QEQLRRIKRN QERERLAQLA QNQKLQPGGM PTSLGDPKSS
GGHSHKERDS GYKEVSPSRK KFKLKPDLKL KCGACGQVGH MRTNKACPLY TGMQSSLSQS
NPSLADDMDD QSEKEMAMDD DDLVNVDGTK VTVSSKVLKR HNDDKRRSGS SGLTLKVQRD
AMGKKKRRVG ADIHCDYLQR HNKTANRRRT DPVVVLSSIL ELILNELRSM PDVSPFLFPV
SAKRVPDYYR VVTKPMDLQT MREYIRQRRY TSREMFLEDL KQIVDNSLIY NGSQSAYTVA
AQRMFTSCFE LLAEREDKLM RLEKAINPLL DDDDQVALSF IFDKLHTQIK QLTESWPFLK
PVNKKQVKDY YTVIKRPMDL ETIGKNIEAH RYHSRAEYLA DIELILTNCE QYNGSDSRYT
NFAKKILEFA QTQLVEFTEH CTQLEENIAK TQERARENAP EFDEAWGNDD YDFGRGSRAS
SPGDDYIDVE GNVGHAAPNT IHRGMGAETH TSQAARKPPP PGPGEVKRGR GRPRKQRDPV
EEVKAQNPVK RGRGRPRKDS LASNMSQTQA YFLDEDLQCS TDDEDDDEEE DFQEVSEDEN
NAASILDQGE RIHAPADTMD YIDPKNIKTE VDVEAQQIAD ESMDVDPNYD PSDFLAMHKP
RENLGEPTNL QGAFSNFLQD DNSSYNAPEA STSAAAAAAA AGVGMSLPSQ DDDSVAMQMP
PEMPTTSLNN GMGIDDDLDI SESDEEDDGT RIRIKKEVLD DAEFGMQQNQ HHFQQIGAPI
GQPSQIYDVD SPNEPPTLDY QHPPQLDYSQ HSLGMEQLQQ LQQVIPPPTE QQQPQQQTPQ
GDNDYAWTY
//
