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Database: UniProt
Entry: A0A1E4TJV6_9ASCO
LinkDB: A0A1E4TJV6_9ASCO
Original site: A0A1E4TJV6_9ASCO 
ID   A0A1E4TJV6_9ASCO        Unreviewed;       522 AA.
AC   A0A1E4TJV6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN   ORFNames=CANCADRAFT_626 {ECO:0000313|EMBL:ODV92040.1};
OS   Tortispora caseinolytica NRRL Y-17796.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trigonopsidaceae; Tortispora.
OX   NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV92040.1, ECO:0000313|Proteomes:UP000095023};
RN   [1] {ECO:0000313|Proteomes:UP000095023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (FEB-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; KV453841; ODV92040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TJV6; -.
DR   OrthoDB; 1469444at2759; -.
DR   Proteomes; UP000095023; 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   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; 2.
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:UP000095023};
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..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
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   522 AA;  59280 MW;  3357E410B535E469 CRC64;
     MSTSDNHAKS TSSSPGGGNY TEFRLKCATP EEVNGIRHNV MKLHSRHKVD LKSFDEPVRL
     SRKDPKLVKH HAATNFSQTP EENSNINNDN ESKPEPKDLS SVAPDGAGRR QYGPNNRKTR
     QVFTGREEAQ KLRYEEHFPW VLEDFEDKNV WVGNYEAAQS NCYVIFVFDD DGFRMVPVDR
     WYRFTPRNQF ATLSLEEAEA KMSAKDKLPR WFMRKLDENK THSPVPAPQR RMRMVLGGES
     STRSGEADRE DLDYEEAFDD DEGAPIIEGP EEENKEVEER IKREMQTANS LDVKDEYDSS
     EEEKLNQEGR KLKKYLRSLE KNALYESDDE DANPYMSDDS DDSLFNDHDD KTDATTGTNS
     ENSNEKRDQK IPRISGVYSR GGMASISSSP VSRSESPPIA TQVKVKKPGS VIIYSSPLKL
     QKAIGDNNNK RSLDEAGNAG GVSKKIKLRM TSPNPATSDE DDPTLLTAED IRRVLEQNEK
     LTAKELLRHL KTKLKDNPKN SERLKGLVKQ VAKLKDNYLV LK
//
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