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Database: UniProt
Entry: G1PD06_MYOLU
LinkDB: G1PD06_MYOLU
Original site: G1PD06_MYOLU 
ID   G1PD06_MYOLU            Unreviewed;      1870 AA.
AC   G1PD06;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008322.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000008322.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000008322.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; AAPE02004130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02004131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02004132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000008322; -.
DR   Ensembl; ENSMLUT00000009134.2; ENSMLUP00000008322.2; ENSMLUG00000009092.2.
DR   eggNOG; KOG0008; Eukaryota.
DR   GeneTree; ENSGT00940000155242; -.
DR   HOGENOM; CLU_000572_3_0_1; -.
DR   InParanoid; G1PD06; -.
DR   OMA; IWDSENM; -.
DR   TreeFam; TF313573; -.
DR   Proteomes; UP000001074; 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; 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; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   SUPFAM; SSF47055; TAF(II)230 TBP-binding fragment; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; 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:UP000001074};
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          1396..1466
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1519..1589
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          149..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1662..1870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1473..1500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        198..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1662..1684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1716..1732
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1736..1750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1791..1821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1846..1870
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1870 AA;  211894 MW;  E22C3A4489A9EFD9 CRC64;
     MGPSKDLQVP AAAAGATAAI MSDTDSDEDS TGGCPFSLTG FLFGNINGAG QLEGESVLDD
     ECKKHLAGLG ALGLGSLITE LTANEELTGN DGALVNDEGW IRSTEDAVDY SDISEVAEDE
     SRRYQQTMGS LQPLCHSEYD DDDYDADCED IDCKLMPPPP PPPGPLKKDK DQDAITGVSE
     DGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQEATQ AESEDGKLTL PLAGIMQHDA
     TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEEQIQEVE
     CSVESEVNQK SLWIYDYAPP PPPEQCLSDD EITMMAPVES KFSQSTGDID KVTDTKPRVA
     EWRYGPARLW YDMLGVPEDG SGFDYGFKLR KMEHEPVIKG RMIEDFRKFE ESSGTDLLAD
     ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFAATLD
     DDKPWYSIFP IDNEELVYGR WEDNIIWDAQ AMPWLLEPPV LTLDPNDENL ILEIPDEKEE
     ATSNSPSKES KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG
     LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPV LKKYSFGALS QPGPHSVQPL
     LKHIKKKAKM REQERQASGG GEMFFMRTSQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK
     IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE
     TDFLIIRTRQ GYYIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSA
     DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM
     VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTQGPFI
     AAEGFSYVKI PNKPTQQKDD KEPQPVKKTV TGTDADLRRL SLKNAKQLLR KFGVPEEEIK
     KLSRWEVIDV VRTMSTEQAR SGEGPMSKFA RGSRFSVAEH QERYKEECQR IFDLQNKLAL
     LTKCLGKNNQ SKIAENESGL KSFQNFVLKK METLAMPQEN GHGECVEIFF CLAAAGSAAA
     GNNHRDDDTA SVTSLNSSAT GRCLKIYRTF RDEEGKEYVR CETVRKPAVI DAYVRIRTTK
     DEEFIRKFAL FDEQHREEMR KERRRIQEQL RRLKRNQEKE KLKGPPEKKP KKLKERPDLK
     LKCGACGAIG HMRTNKFCPL YYQTNAPPSN PVAMTEEQEE ELEKTVIHND NEELIKVEGT
     KIVLGKQLIE SADEVRRKSL VLKFPKQQLP PKKKRRVGTT VHCDYLNRPH KSIHRRRTDP
     MVTLSSILES IINDMRDLPN TYPFHTPVNG KVVKDYYKII TRPMDLQTLR ENVRKRLYPS
     REEFREHLEL IVKNSTTYNG PKHSLTQISQ SMLDLCDEKL KEKEDKLARL EKAINPLLDD
     DDQVAFSFIL DNIVTQKMMA VPDSWPFHHP VNKKFVPDYY KVIVSPMDLE TIRKNISKHK
     YQSRESFLDD VNLILANSVK YNGPESQYTK TAQEIVNVCC QTLTEYDEHL TQLEKDICTA
     KEAALEEAEL DSLDPMTPGP YTPQPPDLYD TNTSLSMSRD ASVFQDESNM SVLDIPTTTP
     EKQVTQEGED ADGDLADEEE GTVQQPQASV LYEDLLMSEG EDDEEDAGSD EEGDNPFSAI
     QLSESGSDSD VGSGGIIPKQ PRMLQENTRM GMENEESMMS YEGDSGEASH GLEDSNISYG
     SYEEPDPKSN TQDTSFSSIG GYEVSEEEED EEEEQRSGPS VLCQVHLSED EEDSEDFHSI
     AGDSDLDSDE
//
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