ID   T2FA_XENLA              Reviewed;         524 AA.
AC   Q04870; Q6IRR6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=General transcription factor IIF subunit 1;
DE   AltName: Full=Transcription initiation factor IIF subunit alpha;
DE            Short=TFIIF-alpha;
DE   AltName: Full=Transcription initiation factor RAP74;
GN   Name=gtf2f1; Synonyms=rap74;
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 [MRNA].
RX   PubMed=1480494; DOI=10.1093/nar/20.24.6736;
RA   Gong D.-W., Hasegawa S., Wada K., Roeder R.G., Nakatani Y., Horikoshi M.;
RT   "Elucidation of three putative structural subdomains by comparison of
RT   primary structure of Xenopus and human RAP74.";
RL   Nucleic Acids Res. 20:6736-6736(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC       to RNA polymerase II and helps to recruit it to the initiation complex
CC       in collaboration with TFIIB. It promotes transcription elongation.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase
CC       II-like kinases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
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DR   EMBL; Z17426; CAA78999.1; -; mRNA.
DR   EMBL; BC070569; AAH70569.1; -; mRNA.
DR   PIR; S35551; S35551.
DR   RefSeq; NP_001082258.1; NM_001088789.1.
DR   RefSeq; XP_018106308.1; XM_018250819.1.
DR   RefSeq; XP_018106309.1; XM_018250820.1.
DR   AlphaFoldDB; Q04870; -.
DR   SMR; Q04870; -.
DR   MaxQB; Q04870; -.
DR   DNASU; 398325; -.
DR   GeneID; 398325; -.
DR   KEGG; xla:398325; -.
DR   CTD; 398325; -.
DR   Xenbase; XB-GENE-974839; gtf2f1.L.
DR   OMA; NNMKEFR; -.
DR   OrthoDB; 893557at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 398325; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR008851; TFIIF-alpha.
DR   InterPro; IPR011039; TFIIF_interaction.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13011; PTHR13011; 1.
DR   Pfam; PF05793; TFIIF_alpha; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50916; SSF50916; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..524
FT                   /note="General transcription factor IIF subunit 1"
FT                   /id="PRO_0000211232"
FT   REGION          56..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  58699 MW;  8CF3A74A3BF77BB0 CRC64;
     MASLGTSGQS VTEYVVRVPR NPSKRYSLMA FNAADKVDFS TWNQARMERD LSAKKMYQEE
     EMPESGAGSE YNRKQREESR RKKYGIILRE FKVDDQPWIL RVNGKAGRKY KGVKKGGVTE
     NASYFIFTQC ADGAFEAFPV SNWYNFTPVA KHRTLTAEEA EQEWERRNKV LNHFTIMQQR
     RLKDQVGDED EDEEGGGKLE KGGKGKKKKK KSDLKIHDLE DDLELSSTES ENSDEEGESR
     KKPQKKVPAK GGKKKKRKSD DEALEDSDDG DFEGQEVDYM SDESSSDEEL PGKIKPAKEE
     EGPKGLDEQS ESSEESEEEK AEEEEGEEEK KAPTPQDNKK KKKGDSSDES ETSEDSDIDG
     ASSSLFMQKK KTPPKKDKKG GSNSSSRGNS RPGTPSPDTG NTSSTLRAAA SKLEQSKRGT
     VSNTPAAKRL KMEAGPQNTS GKSTPQPQSG KSTPSSGDIQ LTEEAVRRYL TRKPMTTKDL
     LKKFQTKKTG LSSEQTVNVL AQILKRLNPD RKVVHDKMHF YLKE