ID A0A0N0BI81_9HYME Unreviewed; 1888 AA.
AC A0A0N0BI81;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
GN ORFNames=WN51_09656 {ECO:0000313|EMBL:KOX77334.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX77334.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX77334.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX77334.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX77334.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ435732; KOX77334.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0BI81; -.
DR OrthoDB; 5482320at2759; -.
DR Proteomes; UP000053105; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 2.
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|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 Initiation factor {ECO:0000313|EMBL:KOX77334.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003047};
KW Protein biosynthesis {ECO:0000313|EMBL:KOX77334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
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 1443..1513
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1566..1636
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 60..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1257..1288
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1643..1670
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 66..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1888 AA; 216767 MW; 1C2844A9BF16BCA2 CRC64;
MVDSEEENDK DMMSGINMTG FLFGNIDDNG HLEDDILDPE AKQHIASLNR LGLSSFIREM
MQNEDIEEEK DNDTNDKSEE ENDMVDEKDT NYIEKSPSAL DFSDINELAE DEKEENNKQD
MFDGKTEKEN ADYDADDEEV VNKSDTQLMP PPPIPEEKEA LTAEEVEAAR QRKLETPLAS
MLPSKYANVN VTELFPDFRA NKVLRFSRLF GPGKPSSLPQ IWRGVKRRRK KKRHHDVRDS
DSGSDQEEKK QKFKGWVMQY GPDPTPDICR SDDETKLLMP VEDKEQIDKT GETGENGDMG
PKVADWRFGP AQLWYDMLQV PETGDGFNYG FKLVDKLDEQ NNNDNKDNKN NKDIHEEFSD
DAFLMVSQLH WEDDVIWNGD DIKHKKLNSK NNAAGWVPSS GNRTAQAFSQ PGKGAPVPVA
SNVRLATSQI TTPLHMQSQK TKLNMNKGNQ QQNREENYDD TWYSIFPVEN EELVYGLWEE
EVIWDPENMK NIPKPKILTL DPNDENSENM KKIPKPKILT LDPNDENIVL GIPDDIDPAL
IHKDNGPQPK VKIPHPHVKK SKLLLGKAGV INVLEEDTPP PPPKSPDRDP FNISNDTYYM
PRSSETTLRL KVGGGNLIQH STPVVELRAP FVQTHMGPMR LRNFHRPPLR RFSHGPLAHP
GPHSVLPLVK HIKKKAKQRE QERIASGGGD VFFMRTPEDL TGKDGELVLI EFSEEHPPLM
NQVGMCSKVK NYYKRKAGKD QGPPKYKYGE TAYAHTSPFL GILTPGQSIQ AVENNMYRAP
IYEHKIPETD FLVIRTSMRN VLELINSFST HRQQYFIREV DALFVAGQEC PLYEVPGPNS
KRANNFVRDF LQVFIYRLFW KSRDTPRRIK MDDIKKAFPS HSESSIRKRL KLCADFKRTG
MDSNWWVIKP DFRLPTEEEI RAMVSPEQCC SYFSMIAAEQ RLKDAGYGEK FLFTPQDDDD
EEMQLKMDDE VKVAPWNTTR AYIQAMKGKC LLQLAGPADP TGCGEGFSYV RVPNKPTISK
EEQEAQPKRT VTGTDADLRR LSLNNAKALL RKFGVPEEEI KKLSRWEVID VVRTLSTEKA
KAGEEGMTKF SRGNRFSIAE HQERYKEECQ RIFDLQNRVL SSNEVLSTDE GESSEEDSSD
IEEMGKNIEN MLSNKKTSTQ LSLEREEQQR HELRKMLMGE VQEQDKKSKE KKKDDEEDSP
VNNFNSQQGR VLKIYRTFRN PEGKEYTRVE LVRKSAVIDT YIKIRNSKDE TFIKQFATLD
EAQKEEMKRE KRRIQEQLRR IKRNQERERM LGVSPSKRKK PKLKPDLKLK CGACGNVGHM
RTNKACPLYQ NSITTAPVNV AMTEEQEEEI EKQLNTDDQD LVNVDGTKVK LSSKLIKHAE
EMKRRTLLLK VPKEAVSSKK RRRATGDDHC DYLKRQQRPA NRRRTDPVVV MSTMLESILN
EMRDLPDVQP FLFPVNAKAV PDYYKIIQRP MDLQTIRENL RLKKYQSREE FLADVNQIVE
NSTLYNGSKS SLTVAAKRML ETCVERLGEK EDRLMRLEKA INPLLDDNDQ VALTFILDNV
VNNKLKSMTE AWPFLKPVNK KLVKDYYNVI KRPMDLETIS KKVSAHKYHS RHEFLRDIEQ
ILENCTVYNG KESPFTQKAE LLVKVCKETL DEYDEHLTQL ENNILLVQKR AMEQADIDPS
WLGPDEENYT IVEPEFRGSQ TSSPENAFGK SNMDDFDFVD VEGDMEGDGS RSVNSKKKDV
LEEDLQFSSE DEFDEVPFGT DEQSENAEME TLELNEVREG TENEVVLADD DSQQAAEAMV
QLGNVGFYMA DQQLLQQDES MDVDPNYDPS DFLLAGLPAR DEKSENKIQD DLAVSESDDD
TENNAKQKQK TPQQLSQPED DVGGDLWF
//
