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Database: UniProt
Entry: A0A150V2B6_9PEZI
LinkDB: A0A150V2B6_9PEZI
Original site: A0A150V2B6_9PEZI 
ID   A0A150V2B6_9PEZI        Unreviewed;       860 AA.
AC   A0A150V2B6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Transcription factor BYE1 {ECO:0000256|ARBA:ARBA00021616};
GN   ORFNames=M433DRAFT_135373 {ECO:0000313|EMBL:KYG44676.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG44676.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG44676.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG44676.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- FUNCTION: Negative regulator of transcription elongation.
CC       {ECO:0000256|ARBA:ARBA00002311}.
CC   -!- SIMILARITY: Belongs to the BYE1 family.
CC       {ECO:0000256|ARBA:ARBA00011050}.
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:KYG44676.1}.
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DR   EMBL; JPDO01000212; KYG44676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150V2B6; -.
DR   STRING; 766039.A0A150V2B6; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd21538; SPOC_TFIIS; 1.
DR   Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR036575; TFIIS_cen_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11477:SF20; PROTEIN PARTNER OF SNF, ISOFORM B; 1.
DR   PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          238..364
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000259|PROSITE:PS51321"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..768
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..794
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  94960 MW;  D42CFA1A9F65EF25 CRC64;
     MSEEPRRSGR ATKGQHTKAS SSPAPNPKPA KGASKAKSKK ITKLEAAEDD SGEDDKIRCI
     CGNDDANDKR AFIGCEACLV WQHNVCMGEP EDEEDVPDHY FCEECRPEEH AETLSALSKG
     EKIWETRNQQ WKAWKKMSAQ RRKSKGKGED TAPPWLKKGG EEKADKETHL ENQETNGKRK
     REFVVANVEP AERPPEVEEQ AAASTRPDKR RKSSQPPGNE APNDADTAIV DIDKLPADRK
     KIAEVLSKII TDDVQSRTKS GFRIPDGHTA KSLGERYGGL IEYACFMNYG DAKDEKYKQQ
     FRTLNANLKR NRLLIERLLT GSLTADELSL MESKDMLSEE KQREQAKLKE ELDRQAIAVE
     EDGPIYRQSH KGYEKIEDET HRASEFASNP APVRDRPGVA DEGSARSPTA DETAKVSSPQ
     TAKAPETKRP SLPAAGERRR SSQHNFDMNA IWNRTAHSPT SSTANPLRPM QVPPRRRSSV
     AHPLPSASMT DGEKHDPDVD RMLQDDDEEY SPSEVIGDDT IVWRGKLAHE SIGDPLVNAR
     FVAGRDLTST ANWRDILPSA LNIDGRLQIA KAEEYLCGLQ WSHNSDVAVL ALTPYDDAAT
     FNRVFDYFSS RQRYAVINKD KPPMVKDLYV IPVEVRSNLP EHIQMLEHCT IKTPVEERLL
     LATCVVSRAP LPPPPPTSTQ QLQLQQNGHH INGTQQPANG TGGAQPAGLP QHMRPDGQGP
     SGSPLNSQAP TFSPGQAGGS QPQPATGYSA PPQQPPHAVP PVVFQPNPYG PQQSPFNSHT
     PAAYPPPQPH HAAPLHGPPL LTNPLIAEIL GPFEYCPTAQ QVIAAQPGIE RAKLENLRKI
     FEEDVQAREN INALAAKLQI
//
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