ID A0A0N4TY84_BRUPA Unreviewed; 467 AA.
AC A0A0N4TY84;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN ORFNames=BPAG_LOCUS13898 {ECO:0000313|EMBL:VDN95083.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001397001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0001397001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN95083.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|ARBA:ARBA00025232, 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; UZAD01013471; VDN95083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4TY84; -.
DR STRING; 6280.A0A0N4TY84; -.
DR WBParaSite; BPAG_0001397001-mRNA-1; BPAG_0001397001-mRNA-1; BPAG_0001397001.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; 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: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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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: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.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000278627};
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 160..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 53635 MW; 035269AEC5DE6531 CRC64;
MADYSIRMAR EDNKEQAAVN EIRQDYGEGS EYGKALREEA RRKKYGRQFQ TYQHDNQPWV
LSITDPSTKE RRFRSIREGG AGEHADYWVF LKSGEEFHAY KVDEWYQFMP FSTHRTLDID
QAEERFRERN RVMNQFALKA QIQQQLKAMD EDGEQMIKTT KSLKIKDEAS SDENSDGEKG
DDEDDAPVGS SKPKKNSKPT ARARKDKRQR VENADEVAAY ESDDGDDEGR EYDYMSDSGS
ESDRDVVPME QKVDEAMVAV GDETGLKKLI GDDFSDTDSS DMDDTTKKLL FAVEDDDGDE
IKKQFIDVDE RGKLSLKVYS FIFYSSGSDS DDPDKEINSA IFLPVKKTLE EPQSSTRKRP
LENVSFADNE VKRIKTEQAF TAPSLSPTQS TTNQDSLNEE TVRRYLRRKP HTTKELLSKI
KSKCGDMEKS EIVQKLAAIL KRIEPHQFKQ KHGKKEVLFF SLNNNLA
//