ID A0A165EUC5_9APHY Unreviewed; 375 AA.
AC A0A165EUC5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=TFIIS N-terminal domain-containing protein {ECO:0000259|PROSITE:PS51319};
GN ORFNames=LAESUDRAFT_677694 {ECO:0000313|EMBL:KZT07780.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07780.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07780.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07780.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Transcription factor involved in RNA polymerase II
CC transcription regulation. May function in both SPT15/TBP post-
CC recruitment and recruitment steps of transcription.
CC {ECO:0000256|ARBA:ARBA00037349}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
CC -!- SIMILARITY: Belongs to the IWS1 family.
CC {ECO:0000256|ARBA:ARBA00037992}.
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DR EMBL; KV427618; KZT07780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EUC5; -.
DR STRING; 1314785.A0A165EUC5; -.
DR InParanoid; A0A165EUC5; -.
DR OrthoDB; 12240at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR46010; PROTEIN IWS1 HOMOLOG; 1.
DR PANTHER; PTHR46010:SF1; PROTEIN IWS1 HOMOLOG; 1.
DR Pfam; PF08711; Med26; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649}; Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 198..276
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 42958 MW; 22EFFD6EBE3206A7 CRC64;
MDQLDLERQI FGRDSDDELS LSEDEEVPQR RIRRESPGAR AEEVESSADS GDEYVQEKRV
AKEKIHRKTR RATAEDGEQR PKQRKRKRRQ REEVDLSQLP PEQANKLKLD MQIEAILKPK
RTSRPKRKKK DDEDVLDRYA DEEVARLREA MLAAVLDDEQ ANKEKLPATA KLRLLPQVVE
VLRKNSLSQS ILDNNLLEGV GKWLGPLPDK SLPALDIQKE FFPILKNAEY IDTNALKDSK
LGRVIMFYTK SKRVSPDIAR LANELVATWS RPIIKRSASY RDRIIPTAPG GEGETVVRSG
ERLNAILARA KENEKNRVRK NAVMIPQREL GSYTVAPRTN SGITRSNVSV DVDIERRKKN
AERLRTLTRK ISTKS
//
