ID A0A1S3RKY9_SALSA Unreviewed; 1951 AA.
AC A0A1S3RKY9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
GN Name=taf1 {ECO:0000313|RefSeq:XP_014052482.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014052482.1};
RN [1] {ECO:0000313|RefSeq:XP_014052482.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052482.1};
RG RefSeq;
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 RefSeq; XP_014052482.1; XM_014197007.1.
DR GeneID; 106603388; -.
DR OrthoDB; 5482320at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
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:UP000087266};
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 1469..1539
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1592..1662
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1546..1573
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1231
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 1766..1789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1951 AA; 221432 MW; FA1C3510450BB0EC CRC64;
MSESDSDEDQ DRPFSLTGFL FGNINEDGQL EGDSVLDTES KKHLAGLGSL GLGNLITEIT
ASEEDDLDED GETGGTDSEG WVKNDADAVD YSDINEVAED ETKKYRQAMG SLQPTRRTDD
EDDYDADCED IDAKLMPPPP PPCLPTPGGK KDDSSPTSAS VGDEGDGIIL PSIIAPSSLV
DKVDFSSSSD SESETDRPSA GPGSGGSPAC LSLPLAGIMQ KDAAKALPGV TQLFPEFRPG
RVLRFLRLFG PGKNMPSVWR SARRKRKRKH RDPQPGTPPP EGAEPMEQQG PEKKSGWDYE
YAPPPPPEQC LSDDEITMMA PIESKFSQTS GDGDKVAESR PKVAEWRYGP AQLWYDMMGV
PDDGSGFHYG FRLKEEDDDE QEKRERPEPP PPLQHPKEDG SGDEKDKQAL ENELFLMVTQ
LQWEDDIIWN GEDVKHKGTK TQRASLAGWL PSSMTRNANA YNAQQGIHDV YLHSTGLSRS
NSQLVPPTPP PMPKAPSIGS GSKRDKHHHD HHATHEDDAP WFSIFPIDNE ELVYGRWEDN
IIWDDQAMDR MLSPPVLTLD PNDENIILEI PDEKESECMS HSPSKENKKE SSLKKSRILL
GKTGVIKDEP QQNMSQPEVK DPWNLSNDEF YYPKQQGLRG TFGGNIIQHS IPAVELRQPF
FPTHMGPMKL RGFHRPSLKK YSFGTLSQPG PHAAQPLLKQ IKKKAKMREQ ERQASGGGDM
FFMRTAQDLT GKDGDLILAE YSEEYPPLIM QVGMATKIKN YYKRKPGKDP GAPDCKYGET
VYCHTSPFLG SLHPGQLLPA FENNLFRAPI YLHKMPETDF LVLRTRQGYF IRELVDIFVV
GQQCPLYEVP GPNSKRANTH IRDFLQVFIY RLFWKSKDRP RRIRMEDIKK AFPSHSESSI
RKRLKLCADF KRTGMDSNWW VLKPDFRLPT EEEIRAMVSP EQCCAYYSML VAEQRLKDAG
YGEKSFFAPE EENEEDFQMK IDDEVRTAPW NTTRAFIAAM KGKCLLEVMG VADPTGCGEG
FSYVKVPNKP TQQKAQDDRE PQPAKKTVTG TDADLRRLSL KNAKQLLRKF GVPEEEIKKL
SRWEVIDVVR TMSTEQARSG EGPMSKFARG SRFSVAEHQE RYKEECQRIF DLQNKVLDST
EVLSTDTDSS SAEDSDFEEM GKNIENMLQN KKTSSQLSRE KEEQERKELQ RMLMGEESDR
DHKGRKGFSS ALSTGSHKDD DTSSVTSLNS SATGRRLKIY RTFRDEDGKE YVRCETVRKP
SVIDAYTRIR TTKDDEFIRK FAVFDEQHRE EMRKERRRIQ EQLRRLKRNQ EKDRFKGPPE
KKAKKVKERP DLKLKCGACG AIGHMRTNKF CPLYYQTNAP PSNPVAMTEE QEEELEKTVI
HNDNEELIKV EGTKIVLGKQ LIESADEVRR KSLVLKFPKQ HLPPKKKRRV GTTVHCDYLN
RPHKSIHRRR TDPMVTLSSV LESVINDMRD HPNTYPFHTP VNAKVVKDYY KVIPRPMDLQ
TLRENVRKRV YPSREEFREN VELIIKNSAT YNGAKHPITQ VAQTMLDLCD EKLKEKEDRL
VRLEKAINPL LDDDDQVAFS FILDNIVTQK MMAVPDSWPF HHPVNKKFVP DYYKVIVQPM
DLENVRKNIS KHKYQNRDVF LFDVSLVHTN SVKYNGPDSP YTKTALEIVS VCKQTLAEYD
EHLTQLEKDI STAKEAALDA ADLDCLDPMT PGTYTSQGRH RRLGEEESDV DIEGFEEEEY
DCKPKTPAPA EDGEGDLEDE DDEEEMLLPP PRRRLQGHND DDYEEDEGSS RPAQASVLYQ
DLLMSDGEDD ASEEEGDNPF SSIHLSESGS DSDREVEVRP PPPPRPHQET ARMGLEQDDS
MMSYGEEVPD ETHLEDSNVS YGSYEEPEGQ TQNSSMGNGE GYGMSEEEEE DEEAARRRGP
SVLSQVQLSE DEEDSEEFRS IGGDSDMDSD N
//
