ID A0A2B7Z6Y5_9EURO Unreviewed; 731 AA.
AC A0A2B7Z6Y5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN ORFNames=GX50_05053 {ECO:0000313|EMBL:PGH32154.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH32154.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH32154.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH32154.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH32154.1}.
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; PDND01000102; PGH32154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z6Y5; -.
DR STRING; 73230.A0A2B7Z6Y5; -.
DR VEuPathDB; FungiDB:EMCG_04280; -.
DR OrthoDB; 1469444at2759; -.
DR Proteomes; UP000226031; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; 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 Initiation factor {ECO:0000313|EMBL:PGH32154.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366044};
KW Protein biosynthesis {ECO:0000313|EMBL:PGH32154.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000226031};
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..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 80305 MW; 414B25F2F0748E71 CRC64;
MSSTPPNPPP PARRPPGPSG PFMKVRRPKA DPLVRPKKRP IPRPPGQAQP GAGPVANGIV
AARPRPPQTA PRPQPSATQS KPTIPSADDL TVNGFSGPLL SESYVDYPVV TTKRAWREGL
KHHVAKFASK KSIDPRDELQ FTRPVRLQRR DPRASNIGPA ADKDDQPPRR PGELNEAERE
ELEAKKAVRE KERAENLAQI APSAAVTQKK TNAPKQRTQQ VFKSEMTPEE IARARIKYEE
ALPWHLDDFD NKGTWVGNYE AAMSETYAMF VLQNDGKMRM VPIDKWYKFT TKSPFKTLTI
EEAEKFMAKK IKDPRWFMEK EQDRAQKKAL EGYAKQSKLF TGRREGFSGA GEGFEGDDLD
FEEDRFADDE EHVGIFDEDE DAKTAEKRIK EDQLKANIFD LKDEKMYDEE ENQEKKEKEA
LKNFGKRVRK ALQRREKNFD YSSGSDANPY SDESSEDSET ERLKEEQEKL EEEHVKKEKG
KESDKNSGAS TKGTNTPSGR PKHTDPLNKK ATSRAARKRA GSPNLSEASG TDTSRKKPKS
KHADAQPESR PMSPGPSGQR KPGAAGDQAS KKRGRNGPAG SGSGSDGERG AGSGGEMSDS
TTAGAKKLKL NPPGLKSKTG TPRGSRAGSP AGVLPTRTGP GSGANSPGPQ TRTSTPGPTT
PSNLTFPTPS EIHSAIPSTG IASAELLKIF RPRIGDSKEN HRKFIAIVRD VSIYGKEDKL
LRPGVLKDGS S
//
