ID A0A1D6P3K7_MAIZE Unreviewed; 1515 AA.
AC A0A1D6P3K7;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Transcription initiation factor TFIID subunit 1 {ECO:0000313|EMBL:AQL04578.1};
GN ORFNames=ZEAMMB73_Zm00001d046579 {ECO:0000313|EMBL:AQL04578.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL04578.1};
RN [1] {ECO:0000313|EMBL:AQL04578.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL04578.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF1 family.
CC {ECO:0000256|ARBA:ARBA00009064}.
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DR EMBL; CM000785; AQL04571.1; -; Genomic_DNA.
DR EMBL; CM000785; AQL04578.1; -; Genomic_DNA.
DR ExpressionAtlas; A0A1D6P3K7; baseline and differential.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Initiation factor {ECO:0000313|EMBL:AQL04578.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000313|EMBL:AQL04578.1}.
FT DOMAIN 348..418
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 1415..1478
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1000..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1515 AA; 170834 MW; 19A7ED114637A957 CRC64;
MQNFSTLKHI HVNEDFVESD SDESISDVTL RLKDSCLSEQ PMKDVHMDIR IVQRSPTCPD
FYPLEHYDWE SDIIWNNSPA TDQQAYAKIC ESEESEDTHG EDQGKDYGQA SRCWDVQSKT
NGSPVIKETF CCTEMPAPAN YCPPGKSYPP LTNEDNLDHI MPNNLDDAVK IDTMVRLNNL
SVLNRELLEG SWLDNIIWDP NEVTPKPKLI FDLKDDHMLF EILDEKNVDH LQSHARAMIV
SQSTKTSTPT VDNFGDQPKP LSGRFNISND KFYSNRKTPQ QAKSHTKKRA LMGIKVVHSA
PAHKLQTMKP VLSNKEIANF HRPRAKWYPH ENKIASQLQG PACSHGRMAV LLMSLGGKGV
KILVNAEDTP VSVKLKASKK FELKPSEKIK LFCSGKELQD DISLAMQNVR PNSIVHAVRT
EVYLWPKAQK LPGEDKPLRP PGAFRKKTDL SIKDGHVFLM EYCEERPLLL SNAGMGARLC
TYYQKTTPTD QTAASLRNNS DGLGTVLAID PADKSPFLGE IHSGSHQSCL ETNMYRSPVF
PHKVAPTDYL LVRSAKGALS LRRIDKLYVV GQQEPHMEVF SPGTKNMQNY LLNRVLAYVY
REFRARERPD AIPQIRADEL PIQSPLTEAI VKKRLKHCAD LKKGPKGHFF WTQRPDFRVP
SEEELRRLLT PESVCCYESM QAGLYRLKRL GILKLTQPVG LASAMNQLPD EAIELAAASH
IERELQITSW NLTSNFVACT NQDRENIERL EITGVGDPSG RGLGFSYVRV APKAPASNSV
LKKKSAAAKG TTVTGTDADL RRLSMDAARE LLLKFGVPEE QIDKLTRWHR IAMVRKLSSE
QAASGITIDE IPVSKFARGQ RMSFLQLQQQ TREKCQEIWD RQVQSLSALD GDDNASDTEA
HSDLDSFAGD LENLLDAEEF DDEDTSTADL RIDKADGMRG LKMRRCSTQA QINKEIEDDE
TEASLAKKLL EDDGNDVKRK KQPVELTNCG TSLVANKMKQ SKTGQTIKSS GYAGALTPKE
NTPREGKEVE NSFVEGGLSS KLKPKMALDV NETVLVKKKS VPGKDGPKEK KQGARGDSLV
CGACSQVGHM RTNKLCPKYR EDPEMSEMDA NSVKPNSMDI NHLQAKTPKR LITKVSSEVT
ETEGPEGIEK TKSVPVKFKV GAPDKSLERN MSVSVSLVSD KRVMDVTDSR STGKVNKIVI
PNKMKSDDFP PDTPKPSVVF RPPAEEKDVP RKKITIKQPK GIDQQRHVES RSVQEPTRKT
RKIVELSSFE DKSREDDHWV GGEPSQVNSS HGRRLGLEGK ISKATMENER SWRDFEERRE
MPQARLFDAT IYASREEDHL KAKKKNKKKK KHEFKDDDLL DHRPYRNDRR VPERHRALKR
SSPAPVVGYA SSAKRRRGGE VELSNILEKV VDHLRGLSGS LLFLKPVTKK EASDYLDIIR
YPMDLGTIRD KVRKMVYRNR DEFRHDVAQI QLNAHIYNDT RYPHIPPLAD ELMEVCDHLL
YENADLLTEA EDAIE
//
