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Database: UniProt
Entry: A0A1V6QV16_9EURO
LinkDB: A0A1V6QV16_9EURO
Original site: A0A1V6QV16_9EURO 
ID   A0A1V6QV16_9EURO        Unreviewed;       439 AA.
AC   A0A1V6QV16;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=TFIIS N-terminal domain-containing protein {ECO:0000259|PROSITE:PS51319};
GN   ORFNames=PENSOL_c037G07749 {ECO:0000313|EMBL:OQD92867.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92867.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD92867.1}.
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DR   EMBL; MDYO01000037; OQD92867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QV16; -.
DR   STRING; 60172.A0A1V6QV16; -.
DR   OrthoDB; 12240at2759; -.
DR   Proteomes; UP000191612; 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   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 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:UP000191612}.
FT   DOMAIN          263..340
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..86
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  50334 MW;  099EE7A0450C41B8 CRC64;
     MSASPDHKAV SPAASPEPER VATPVAGDDK EGENFNNPTA EAKELTEDVD DELHAADDDE
     DDDDKLSDDE SLLSEVDEAQ FDNFDPENVD VEDRPQLAID EDNLKLIGRH KRKRTEDGES
     RPRRKEGRRE KKSRRADEGG DEGGSSRRRE RKQREDKPEV DEETLDPETR RRRALDRAMD
     EAMKKPAKRR FRKQDGIDLE SMADAEIEDM RKRMTHAAQM DAINRQEGKP AMHKLKLLPE
     VIMLLNRNQY TSALVDPEIN LLEAVRFFLE PLDDGAMPAY NIQRDLLTAI TKLPINKDAL
     IASGIGKVVV FYTKSKRTER RIKEMAEKLL AEWTRPILQR SDDYSKRVYQ EADYDPTKVV
     RRAPPTAEEI QAEDRAREIL PPRLLNRARV DRTNVSYTVV PRQTAVRETQ FARPLGSSGE
     DRFRKMQARQ AAARKASRR
//
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