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Database: UniProt
Entry: A0A0W8CX27_PHYNI
LinkDB: A0A0W8CX27_PHYNI
Original site: A0A0W8CX27_PHYNI 
ID   A0A0W8CX27_PHYNI        Unreviewed;       658 AA.
AC   A0A0W8CX27;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=B-related factor 1 {ECO:0000256|ARBA:ARBA00031009};
GN   ORFNames=AM587_10004732 {ECO:0000313|EMBL:KUF77158.1}, AM587_10009237
GN   {ECO:0000313|EMBL:KUF88412.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF88412.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF88412.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, and Race 0
RC   {ECO:0000313|EMBL:KUF88412.1};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF88412.1}.
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DR   EMBL; LNFO01005634; KUF77158.1; -; Genomic_DNA.
DR   EMBL; LNFO01001845; KUF88412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CX27; -.
DR   STRING; 4790.A0A0W8CX27; -.
DR   EnsemblProtists; KUF77158; KUF77158; AM587_10004732.
DR   EnsemblProtists; KUF88412; KUF88412; AM587_10009237.
DR   Proteomes; UP000052943; 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; 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; PF00382; TFIIB; 2.
DR   PRINTS; PR00685; TIFACTORIIB.
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   Reference proteome {ECO:0000313|Proteomes:UP000052943};
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          317..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  73842 MW;  298F1DC5DFEFADB1 CRC64;
     MASTICPTCS CTEIDVVDVS GEAVCVSCGT ILEENNIVSS IEFQESGGGA HSVVGQFVSA
     TASKAYGNIG TSGRNYGIES RANTLANGKK KIRQIAGMLR LGDHYVDSAF RLFALALQRN
     FTHGRKTQTV IAACLYIVCR RERSPHLLID FSDKLQINVY VLGGVFLKFC KLLQIHLPLI
     DPSLYIHRFA SQLNFAGKTH SIATTALRLV ATMKRDWIET GRRPSGICGA ALLIAARSQS
     VMCSLHDVMD VVNIGERTLK QRLYEFSLTP TAQLTYDQVG KLEMSRVECD PPSFQRHREK
     EVMEMLLLES EKLPLEQKGR KRLTRGRRDS DDESDDDESG GALAKGMLNK KVQRLKDEEM
     SRFLSGDAYY KKKQAEALLG SNGGAVADKG DDDNDDDEDI DYGFDNANDQ IVNRASRLAA
     QEVLLRVRKK SARYIMRKRE EASFYKTIER DLTMALEEDT SARVKRNGEK EHDDDVNGET
     EHSTSPTTSA DDEAVSTVIR RRRSRDLADS SSEKRRRSRS DGDIHEQEED AEDPEDEDKV
     AEKKDDAEKG EPKKEVVDTL SDLDDDEINS LLLTREEAEK KKLLWEKMNK DFIQEQEQKR
     LLGLSAPDAP KKKRRKKTPD VNAPPPDTAQ HAIYKLKSRR INYEVIDELF GEAASNGF
//
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