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Database: UniProt
Entry: J4GMI3_9APHY
LinkDB: J4GMI3_9APHY
Original site: J4GMI3_9APHY 
ID   J4GMI3_9APHY            Unreviewed;       377 AA.
AC   J4GMI3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=TFIIS N-terminal domain-containing protein {ECO:0000259|PROSITE:PS51319};
GN   ORFNames=FIBRA_02142 {ECO:0000313|EMBL:CCM00115.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00115.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM00115.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00115.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE796965; CCM00115.1; -; Genomic_DNA.
DR   RefSeq; XP_012179398.1; XM_012324008.1.
DR   AlphaFoldDB; J4GMI3; -.
DR   STRING; 599839.J4GMI3; -.
DR   GeneID; 24095026; -.
DR   HOGENOM; CLU_045275_2_0_1; -.
DR   InParanoid; J4GMI3; -.
DR   OrthoDB; 12240at2759; -.
DR   Proteomes; UP000006352; 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:UP000006352}.
FT   DOMAIN          201..279
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  42860 MW;  31DFFF21108971AC CRC64;
     MERDKGHLDL EEQIFGRDSD DELSSPEEDE PPPRRNVRAS SGIPDDAESS GDSGDEYVQE
     KAAAKVKQSR RRSRRVAEEG ERQPKQRKRK RKQLDEIDLS QLPPEQASKL RLDMQIEAIL
     KPKKSSKSRR KKKDDEDVLD RYADEEVSRL REAMLSAAQD DDQSNREKLP ATAKLRMLSQ
     VMEVLRKNSL SQSITDNNLL EGVRRWLEPL PDRSLPALDI QKEFFPILKK MEYIDSSALK
     ESGLGRVVIF YTKSKRVTAD IARHANDLIS AWSRPIIKRS ASYRDRIVPT AQTGDGEGAR
     GGERLNTILA RARETDKNRV RKNAVMIPQR ELGSYTVAPK PNAGFGKGSM SVDVDIERRK
     RGAERLRSLT RKMATKS
//
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