ID A0A3Q3WTE1_MOLML Unreviewed; 1858 AA.
AC A0A3Q3WTE1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Transcription initiation factor TFIID subunit {ECO:0000256|PIRNR:PIRNR003047};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000021538.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000021538.1}
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 STRING; 94237.ENSMMOP00000021538; -.
DR Ensembl; ENSMMOT00000021895.1; ENSMMOP00000021538.1; ENSMMOG00000016365.1.
DR OMA; IWDSENM; -.
DR Proteomes; UP000261620; Unplaced.
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:UP000261620};
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 1399..1469
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1522..1592
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1476..1503
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1599..1626
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 101..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1839..1858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1858 AA; 211071 MW; 37E757CAAC1B407C CRC64;
MITTGPDPLT LAKRLPFRMS DSDSDEDQDR PFSLTGFLFG NINEDGQLEG DSVLDNESKK
HLAGLGSLGL GSLIIEITAN EEDSQEESKD SGSVDAEGWV KSTDDAVDYS DISEVAEDET
KKYRQAMSSL QPSRKTDDED DYDADCEDID SKLMPPPPPP TLPGSAKKEE PTPQSTNGDG
IILPSIIAPS STGDKVDFSS SSDSESETDR PCQGLGAGGP PDRLNLPLAG IMQKDAAKAL
PGVTELFPEF RPGKVLRFLR LFGPGKNMPS VWRSARRKKK RKHRDPQPGT PPPEGETTEQ
NQEKKSGWIY EYAPPPPPEQ CLSDDEITMM APIESKFSQT CGDGDKEAES RPKVAEWRYG
PAQLWYDMLG VSEDGSNFNY GFKLKEEQSS EPEKQDKPKE MTETLHELFL MVTQLQWEDD
IIWNGEDVKH KGTKTQRASL AGWLPSSMTR NANAYNAQQA SHEEDSPWFS IFPIDNEELV
YGRWEDNIIW DDQEMDHMLM PPVLTLDPND ENIILEIPNE KEEMTSHSPS KENKKETAIK
KSRILLGKTG VIKDEPQQNM SQPEVKDPWN LSNDEFYYPK QQGLRGTFGG NIIQHSIPAL
ELRQPFFPTH MGPMKLRQFH RPALKKYSFG ALAQPGPHAV QPLLKHIKKK AKMREQERQA
SGGGDMFFMR TPQDLTGKDG DLILAEYSEE YAPLIMQVGM ATKIKNYYKR KPGKDPGAPD
CKYGETVYCH TSPFLGSLHP GQLLQAFENN LFRSPIYLHK MPETDFLVLR TRHGYYVREI
VDIFVVGQEC PLFEVPGPNS KRANTHIRDF LQVFIYRLFW KSKDRPRRIR MEDIKKAFPS
HSESSIRKRL KLCADFKRTG MDSNWWVLKP DFRLPTEEEI RAMVSPEQCC AYYSMLVAEQ
RLKDAGYGEK SFFAPEEENE EDFQMKIDDE VRTAPWNTTR AFISAMKGKC LLEVTGVADP
TGCGEGFSYV KVPNKPTQQK DDKEPQPAKK TVTGTDADLR RLSLKNAKQL LRKFGVPEEE
IKKLSRWEVI DVVRTMSTEQ ARSGEGPMSK FARGSRFSVA EHQERYKEEC QRIFDLQNKV
LESTEVLSTD TDSSSAEDSD FEEMGKNIEN MLQNKKTSSQ LSREREEQER KELQRMLMAS
SLSTSSHKDD DTSSVTSLNS SATGRRLKIY RTFKDEDGKE YVRCETVRKA AVIDAYTRIR
TTKDDEFIRK FALFDEQHRE EMRKERRRIQ EQLRRLKRNQ EKDKIKGPPE KKAKKVKERP
DLKLKCGACG AIGHMRTNKF CPLYYQTNAP PSNPVAMTEE QEEELEKTVI HNDNEELIKV
EGTKIVLGKQ LIESADEVRR KSLVLKFPKQ QLPPKKKRRV GSAVHCDYLN KPHKAIHRRR
TDPMVTLSSV LESIINDMRD HPNTYPFHTP VNAKVVKDYY KIITRPMDLQ TLRENVRKRM
YPSREEFREA VEVIVKNSAT YNGAKHPITQ VAQSMLDLCD AKLKEKEDRL VRLEKAINPL
LDDDDQVAFS FILDNIVTQK MMVVPDSWPF HHPVNKKFVP DYYKVIVNPM DLENIRKNIS
KHKYQNRDAF LSDVSLIHTN SIKYNGPESP YTKTALEIVN VCKQTLAEYD EHLTQLEKDI
STAKEAALDA ADLECLDPMT PGPYTPQPAD LFDSGASGSL PREPSSLFSE GPLMVAPEKR
GGQEEEEEDE EEDGGLHRPA QSSVLYQDLL MSDGEDDASE EEGDNPFSSI QLSESGSDSD
REVGVRPPPP RRAQETARMG MEQDESMMSY DGDGPDGPHM EDSNVSYGSY EETESRSQMQ
TSSMANGDYG ISEEEEEDEE EEARRRGPAV LSQVQLSEDE ESEEFRSVGG DSDMDSDN
//
