ID J5Q982_TRIAS Unreviewed; 673 AA.
AC J5Q982;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=B-related factor 1 {ECO:0000256|ARBA:ARBA00031009};
GN ORFNames=A1Q1_05359 {ECO:0000313|EMBL:EJT46148.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT46148.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT46148.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TFIIB family.
CC {ECO:0000256|ARBA:ARBA00010857}.
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:EJT46148.1}.
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DR EMBL; ALBS01000304; EJT46148.1; -; Genomic_DNA.
DR RefSeq; XP_014177566.1; XM_014322091.1.
DR AlphaFoldDB; J5Q982; -.
DR GeneID; 25988871; -.
DR KEGG; tasa:A1Q1_05359; -.
DR VEuPathDB; FungiDB:A1Q1_05359; -.
DR HOGENOM; CLU_010293_2_3_1; -.
DR OrthoDB; 5483352at2759; -.
DR Proteomes; UP000002748; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd20553; CYCLIN_TFIIIB90_rpt1; 1.
DR CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 1.20.5.650; Single helix bin; 1.
DR InterPro; IPR011665; BRF1_TBP-bd_dom.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618:SF4; TRANSCRIPTION FACTOR IIIB 90 KDA SUBUNIT; 1.
DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1.
DR Pfam; PF07741; BRF1; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR Pfam; PF00382; TFIIB; 2.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}.
FT DOMAIN 2..33
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REGION 297..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75836 MW; 0EA64B8E8670F51A CRC64;
MAVKVCPGCK SKNLQTDYSA GNVVCQDCGI EVEQGILVSE IGFSEGAGGR VHVQGTFVSH
NSTGINSNRG VSSENIKEEG RKRIQLICNQ MGIAPSVQRG AQRFYSLAVD NKFNRGRRTD
FVVASCIYLY SRFEKDALML IDFSERLQIN VYELGATYLK LRSCLNLDQI LPEIDPAVYN
IRFANRLDFG AASATVARDA SRLIKRFKAD WMTAGRRPAG ICGACLVIAA RMSDFLRTPE
EVAQVVKVSP LTIKKRLVEF AGTAAANKTV EEWRALTDAD LEAENADELP PIMKKQLAKM
AAQRVKRERS ETADDDSRAS TPSSPRKRSK LSQASDDTTN AIQAVAKGVD IESTGADEAD
EGMEPLAKED YVKDIQDAGD NTEEAIADRK RERRMLMASL KEADGEEADE EELQEMAADN
DAPGQDSKED EAGEGSVLAE VAPAFNPLKD LPAPPDFKDK EALYAYCEKY IFTSEDLLYA
GNSAALRQKI DAWVKGRDPT EVVNEMRRVV WARNEREWFA KHHREDEFDD LDDDELDKYW
VMSEDERQTR ARMWLSHNGK WLEEDKERQE RKAEYNRQHG IDPNKPPPKK KKRKSNAEKQ
KGPYVSTHAA MEAFATQKKF STRINQEVLK RISQGEGLQR MDDDEYDDED GKDDEKDDEK
YDEKEDELYG YIG
//
