ID W5NCD5_LEPOC Unreviewed; 1947 AA.
AC W5NCD5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018294.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000018294.1}
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; AHAT01015677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000018326.1; ENSLOCP00000018294.1; ENSLOCG00000014847.1.
DR GeneTree; ENSGT00940000155242; -.
DR HOGENOM; CLU_000572_3_0_1; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000014847; Expressed in testis and 13 other cell types or tissues.
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; 2.
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:UP000018468};
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 1468..1538
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1591..1661
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1545..1572
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1668..1695
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1770
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1923..1947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1947 AA; 220649 MW; 9DC6640F05791736 CRC64;
MSESDSEEDQ DQPFSLTGFL FGNINEDGQL EDDSVLDTES KKHLAGLGSL GLGNLLTEIT
ASEDDPPQDE RDSSGTDAEG WVKSTEDAVD YSDISEVAED ETRKYRQAMG SLPALHRTDD
DDDDYDADCE DIDAKLMPPP PPPVLPTMPK RDEPAAPGPS VGDEGDGIIL PSIIAPSAAG
EKVDFSSSSD SESETDRPSK GAGGGSEGSL TLPLAGIMQR DATKLLPSVT DLFPEFRPGK
VLRFLRLFGP GKNMPSVWRS ARRKRKKKHR EPHPGTPPPG DPEHGEAGPE KKSGWDYEYA
PALPPEQCLS DDEITMMAPV ESKFSQSAGD GDKVAETRPR VAEWRYGPAQ LWYDMLGVPE
DGAGFDYGFR LKGSQPEEPE QKTNYWVLAP VCFPLVEAEP EEGGGEPEAE LLENEHFLMV
TQLRWEEDII WNGEDVKHKG TKTQRASLAG WLPSSMTRNA NAYNAQQGLS RSNSQLVPPT
PPPLPKATPP GTQGSGKIRD KHSQEQQVSM EEDSPWFSIF PIDNEELVYG RWEDNIIWDD
QAMDDMPTPP VLTLDPNDEN IILEIPDEKE EMTSNSPSKE NKKESALKKS RILLGKTGVI
KDEPQQNMSQ PEVKDPWNLS NDEFYYPKQQ GLRGTFGGNI IQHSIPSVEL RQPFFPTHMG
PMKLRQFHRP TLKKYSFGVL SQPGPHPVQP LLKHIKKKAK MREQERQASG GGDMFFMRTA
QDLTGKDGDL ILAEYSEEYP PLMMQVGMAT KIKNYYKRKP GKDPGAPDCK YGETVYCHTS
PFLGSLHPGQ LLQAFENNLF RAPIYLHKMP ETDFLILRTR QGYYVRELVD IIVVGQECPL
FEVPGPNSKR ANTHIRDFLQ VFIYRLFWKS KDRPRRIRME DIKKAFPSHS ESSIRKRLKL
CADFKRTGMD SNWWVLKPDF RLPTEEEIRA MVSPEQCCAY YSMLVAEQRL KDAGYGEKSF
FAPEEENEED FQMKIDDEVR TAPWNTTRAF IAAMKGKCLL EVTGVADPTG CGEGFSYVKV
PNKPTQQKDD KEPQPAKKTV TGTDADLRRL SLKNAKQLLR KFGVPEEEIK KLSRWEVIDV
VRTMSTEQAR SGEGPMSKFA RGSRFSVAEH QERYKEECQR IFDLQNKVLE STEVLSTDTD
SSSAEDSDFE EMGKNIENML QNKKTSSQLS REREEQERKE LQRMLLGEDS GPDRDKNRKD
RRDRKGCSSA LSTSSHKDDD ASSVTSLNSS ATGRRLKIYR TFRDEDGKEY VRCETVRKPS
VIDAYTRIRT TKDDDFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE KEKIKGPPEK
KPKKIKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ EEELEKTVIH
NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG TTVHCDYLNR
PHKSIHRRRT DPMVTLSSVL EGIINDMRDH PNTYPFHTPV NAKVVKDYYK IITRPMDLQT
LRENVRKRMY PSREEFRESV ELIVKNSITY NGAKHPLTQV AQSMLDLCDE KLKEKEDRLV
RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD YYKVIINPMD
LENIRKNISK HKYQNREAFL DDVNLIYTNS VKYNGPDSPY TKTAQEIVNV CKQTLAEYDE
HLTQLEKDIS TAKEAALDAA DLESLDPMTP GPYTPQARHG RGRLGEEESD VDIEGFEEED
DGKPKTPTPA DDGDGDLEEE DEDLSQRRCE DEDDDEGSSR PAQASVLYQD LLMSDGEDDE
ASEEEGDNPF SSFHLSESGS DSEPEGGMRP QQPRVHQETA RLGLDQDESM MSFEGDGAEH
SQLEDSNISY GSYEEGEGRT RRHPASLGSS AGYGLSEEEE EDEEEEEEDA GRRHGPCVLS
QVHLSEDEDD SEDFRSIGGD SDMDSDT
//
