TAF3_XENLA
ID TAF3_XENLA Reviewed; 845 AA.
AC Q5EAW9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Transcription initiation factor TFIID subunit 3;
DE AltName: Full=TBP-associated factor 3;
GN Name=taf3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of tbp and TBP-associated factors (TAFs).
CC {ECO:0000250|UniProtKB:Q5VWG9}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein tbp, and a number of TBP-
CC associated factors (TAFs). {ECO:0000250|UniProtKB:Q5VWG9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC090215; AAH90215.1; -; mRNA.
DR RefSeq; NP_001089280.1; NM_001095811.1.
DR AlphaFoldDB; Q5EAW9; -.
DR SMR; Q5EAW9; -.
DR DNASU; 734328; -.
DR GeneID; 734328; -.
DR KEGG; xla:734328; -.
DR CTD; 734328; -.
DR Xenbase; XB-GENE-940285; taf3.L.
DR OrthoDB; 320730at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 734328; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..845
FT /note="Transcription initiation factor TFIID subunit 3"
FT /id="PRO_0000245531"
FT ZN_FING 781..831
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 59..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..742
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 93203 MW; FCB5655CA81F63FF CRC64;
MGVNIHELED YIHNIEPVTF PHQIPSFPVS KNNALQFPPP GSKDAEDRKE YIPDYLPLII
SSQEEEEEEQ VPTDGGTSAE AMQVPLEEEE EEGEMEDDET VNDENYLSKR PLDSPETMEM
PFAKRIRLMN NKGDILDGSL EPREPLSSIN SQKVPSVLSP AHKIDSQDLD VSYSDQIMLS
PVSKSQAPPP SESKSLIPKT KSKGGSPGQK IKSPKATPIS TVIGSPIRSP KSGPKERKSP
GCAKSPKSPK SPKVPLAAPP PAIKTETPNR TPLATLSEKI GRENIQIKQN QTPLDSDQLN
VEIPSKKPSI ADNTIEDSID AVIARACAEQ EPDPFEFSSG SESEGEVFTS PKRLNISELT
TPKVSASGIN PGKTSSTSVP ASGGTSSSDI SWTMDDSINE VIRKVSQETP TNTPANNPPC
FSSPSASPPT PEPLLKVFED KAKLPPPVEL KKKTKKEQRA KKKKDKDKLK DKERSKDKNK
DRSKDKEKDK EKDGTKDGKV LWKDSNKDED SELHRFKLKD FNEIDSKSKQ KENCGKKDKE
KHKDKKKDKE KGKKDKDKKG KDKTKEEKMK SPSTPIMLSS KDIALPMIST PNTVRLPSLL
SSMSPLLPEK LFEEKEKSKE KDKKKDKKEK KKKKDKEKVK EKEKEKKEKE KEKEKEKKEK
EKVKAELSIP APSPVIPRLT LRVGAGQDTI VISKVVSAPE SKAVPPPSLP KSPPPTPSPA
PAPVLVVPPQ APPAPAAASP APTPAPSALT SNAGSSKTPV RSVVTETVST YVIRDEWGNQ
IWICPGCNKP DDGSPMIGCD QCDDWYHWPC VGINAAPPED EQWFCTKCES KKKDKKQKKR
KHKAH
