ID K1WUW5_MARBU Unreviewed; 791 AA.
AC K1WUW5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|RuleBase:RU366044};
GN ORFNames=MBM_00568 {ECO:0000313|EMBL:EKD21455.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21455.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD21455.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21455.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921428; EKD21455.1; -; Genomic_DNA.
DR RefSeq; XP_007288457.1; XM_007288395.1.
DR AlphaFoldDB; K1WUW5; -.
DR STRING; 1072389.K1WUW5; -.
DR GeneID; 18756503; -.
DR KEGG; mbe:MBM_00568; -.
DR eggNOG; KOG2393; Eukaryota.
DR HOGENOM; CLU_025955_0_0_1; -.
DR InParanoid; K1WUW5; -.
DR OMA; IPIMTTK; -.
DR OrthoDB; 1469444at2759; -.
DR Proteomes; UP000006753; 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:EKD21455.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366044};
KW Protein biosynthesis {ECO:0000313|EMBL:EKD21455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
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..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 86626 MW; 28A65537E12F0B37 CRC64;
MSASPSGQSN GPTPKGDAPL YVRRSKAADP LRPRKKPVRR TGAAPHASTY KPNGLPVAGR
PTPQYPVNGK LPPRGAGPGP NQSSNVPGAG NSSAKGGWTT SPEGQFMDYP LFTTKRAMRE
GLRYHIARFA SKKPVDPSDQ NEFTRPVLLH RRDPRQPPPG KGVKDEDQTT MEAPMDSKER
EKQEIAKAEK EKQRALDLAQ IAPTGNNAAA LAAKKTQAFR HEKTTQVYRL DKTEEQKKLS
DLKYEEALAW HLEDADNKNT WVGNYEAALS DTNVIFVIEG ASFKMIPIEK WYRFTPKGQF
KTYTIEEAET QMAKKHKESR WVMKTNEQNE SQRAVQESRK AMGSLFTVKA ESNTFKSVGK
REVQEMDDMD FEEGDLFQDD DEQVTFDPEN DEDAKDAQER VKRDRQGANV FDQTNEADVD
EEEAEDKKAK EARKKLGKDV TKALRKRERN FVYNSDSDHP YSDSSEDDTS DEEKQKEIDK
KKDEEAKNKE KAEEAKNKEK AKLDSTSKPP SGASTKGANT PSGRPKHTDP LEKVKNLKRA
GSPNLSESSG NESTRKKLKK KHQTSASGSS TPVPGSRPMS PAPQQAGPGQ ISRKGSLVNI
KVNQGKLSDI VSAPPNPSPV RGSAAGDGEA TGGEGSDGGK APQKIKIHIA SRAGSRAGSP
AAASGKIFRL CKRRSGGYIE HPVLIRFAAS SHTENHLLTY ATGESPSSRA QSPSARAQSP
SARAQSPGAG PVGPVQAHEI RKALPARGIP MKDLLKVFVG RVTADNRADF IRLVKSNSAY
GQDKLLRPKT K
//
