ID I1I3H6_BRADI Unreviewed; 530 AA.
AC I1I3H6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 22-FEB-2023, entry version 55.
DE RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN Name=100846625 {ECO:0000313|EnsemblPlants:KQJ96401};
GN ORFNames=BRADI_3g22897v3 {ECO:0000313|EMBL:KQJ96401.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ96401};
RN [1] {ECO:0000313|EMBL:KQJ96401.1, ECO:0000313|EnsemblPlants:KQJ96401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96401.1,
RC ECO:0000313|EnsemblPlants:KQJ96401};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ96401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96401.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ96401}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ96401};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; CM000882; KQJ96401.1; -; Genomic_DNA.
DR RefSeq; XP_014756956.1; XM_014901470.1.
DR AlphaFoldDB; I1I3H6; -.
DR EnsemblPlants; KQJ96401; KQJ96401; BRADI_3g22897v3.
DR GeneID; 100846625; -.
DR Gramene; KQJ96401; KQJ96401; BRADI_3g22897v3.
DR HOGENOM; CLU_020656_1_0_1; -.
DR OrthoDB; 468460at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; I1I3H6; baseline.
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:UP000008810};
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 206..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58358 MW; 219C44AD31FA7D94 CRC64;
MGSVDLVLKP ACEGCGSPSD LYGTGCKHTT LCSSCGKSMA LSRARCLVCS APITNLIREY
NVRANASTDK AFSIGRFVTG LPPFSKKKNA ENKWSLHKEG LQGRQLTDKM QEKYNRKPWI
LEDETGQYQF QGHMEGSQSA TATYYLLMMQ GKEFHAFPAG SWYNFSKVAQ YKQLTLEEAE
EKMNKRKTSA TGYERWMMKA ATNGPAAFGS DIKKLEPTND GEKESARPKK GKDNEEGNNS
DKGEENEEDE AARKDRLGLS KRGMDDDEEG GKDLDFDLDD EIEKGDDWEH EETFTDDDEA
VDIDPEERAD LAPEIPAPPE IKQDDEENEE EGGLSKSGKE LKKLLGRASG QNESDADEDD
EDDDDDESSP VLAPKQNDQP KDEPVDNSPA KPTPSSGHAR STPPASKSKQ KRKSGGDDAK
TSGSAASKKA KVEPDTKTSS IKEEAPSSLK HTSKASASSR NANVSPVTED EIRTVLLAVA
PVTTQDLVSR FKSRLRGPED KNAFAEILKK ISKIQKTNGH NYVVLREDKK
//
