ID A0A1G4M706_LACFM Unreviewed; 633 AA.
AC A0A1G4M706;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN ORFNames=LAFE_0A06568G {ECO:0000313|EMBL:SCV99591.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCV99591.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCV99591.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCV99591.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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 {ECO:0000256|RuleBase:RU366044}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366044}.
CC -!- SIMILARITY: Belongs to the TFIIF alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00005249, ECO:0000256|RuleBase:RU366044}.
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DR EMBL; LT598487; SCV99591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4M706; -.
DR STRING; 4955.A0A1G4M706; -.
DR OMA; FEEFYPW; -.
DR OrthoDB; 1469444at2759; -.
DR Proteomes; UP000190831; Chromosome a.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR PANTHER; PTHR13011:SF0; GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 1; 1.
DR PANTHER; PTHR13011; TFIIF-ALPHA; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF50916; Rap30/74 interaction domains; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU366044};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366044};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU366044};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU366044}.
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 71737 MW; 322C0A6A61A08C25 CRC64;
MSNPLRSSGN SASPFIKREQ HRREFLRSRS KKNATPKPFV KKEDPDAYDE RTSQILQGSG
SSSKKVKQEN GAEYNEFPLR AVSSEKLENI RTHILKFQSK KKIDPTKDFH LPIRLHRKDT
RNLQFQLTRA EIVQRQKEIA EFKNRADEEE KGDENSSKTN TPSVIDVEEA PSTSSVKEEP
KSPETPAQPT PPVTVLEEAG PAEDPTKVGM VKYDGQEQPA IDEDESADPF ADVAPDGGGR
YRRGNSKRKT RQLKLLDENA KRLRFEEFYP WVMEDFDGLN TWVGSYEAGN SDSYVLLSVE
NDGSFTMVPA DKVYKFTARN KYATLTIEEA EKRMEKNGKG VPRWLMKHLD DIGTTTTRYD
RTRRRLKAVD AREGDDEDRG DNSEVELDFD EEFADDEEAP IIDGNEQENK ESEDRIKKEM
LQANAMGLRD DEEIDDDLFG EKKIDDEGER VKKALQKSDA AALYESDDDE LNPYLSESDL
EDQDANTVKQ EDQENGKSSR KGSPKKKSSR GSPTAPQIYV KSIKDCMIVL KAGKSVLNNF
PSGEWNPQAK KRSSEQPADL GSAKGGAESD ENAENLLTED DIINAVSGKR MTLKQLIREL
REKVSKHPSN KERMKLLVKR LVKLNDGYLE LNK
//
