ID A0A072PUZ2_9EURO Unreviewed; 880 AA.
AC A0A072PUZ2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Transcription factor BYE1 {ECO:0000256|ARBA:ARBA00021616};
GN ORFNames=A1O9_04189 {ECO:0000313|EMBL:KEF59345.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59345.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF59345.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59345.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF59345.1}.
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DR EMBL; AMGV01000003; KEF59345.1; -; Genomic_DNA.
DR RefSeq; XP_013261935.1; XM_013406481.1.
DR AlphaFoldDB; A0A072PUZ2; -.
DR STRING; 1182545.A0A072PUZ2; -.
DR GeneID; 25279122; -.
DR VEuPathDB; FungiDB:A1O9_04189; -.
DR HOGENOM; CLU_009292_0_0_1; -.
DR OrthoDB; 5491784at2759; -.
DR Proteomes; UP000027920; 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; IPR019787; Znf_PHD-finger.
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.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 87..139
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 288..418
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 95460 MW; 2F71762F774F463E CRC64;
MAGKHWQQTS RVASPMITTT APPLSCQIIN TVADEPRRSG RATKGQHTKD RDPNEDAPTP
ATKKKGKGKG SKAKQVEEEV EEEAEEIIRC VCGKYEEEED VPRAMICCDN CSAWQHNGCM
GLPEDYEVDT YFCEQCKPET HKELLAAIAR GEKPWEAAED TKKGERGKKK GGRKGRKSGG
ARASDVAAPA SSQEPQESQE PEKPKEPTPQ PAPVTGQKRK LEELPPTPEV KNKKVRGTPA
ADTNGAKSTT PVERKPSQST TPSRQGSKSE QSIGPAIVSD LKELTNASRK GAAQSLMKLI
EQQIKELVKQ GEYAVPTHST AQDIASQTGL RIEHALYHIQ ASGSGEPNDA YKQQLRAITF
NVKKNHALGV KLLQGDLTPH KLASMDPKDM ASEEQKRKDA ATMKEMEKQH TIIEQEGPRI
RRTHKGEEYV DESRQVAAES VTSNAPVRKS SMAEQDGDAK SPELAIKSPS QASRPSVDTA
RRQSSANFDI DKVWSNVANS PTGGGDGEGP RFGELPLQQS PVVSARDPSG PGTKTDADID
ELLKDEEVES PPYSPKDTTE SDGTVWQGVV NGGSLGKFHI SARHAAGATP DSDTLRMTYH
QLLPETIVIA GRIQPSKAEE YLCGLEYSNT SDLVIVYMPE PPKTTPDQVQ FDKFFRYFKS
KDRFGVGNPH PIPAVKDLYL IPLEAGQELP TFVKKLETDF PDPTNERMLL IPIVIKNSEL
PHNVSTSSVA SPGGGPVAQT PMTPLDGTFE TQQSSVYSQS PAPGHYAMNG TPQLPHVQSN
SATPHPYPTP GLPAQYPPQP QFNPLPPQQQ LPPSPAVLNA QRVLGPLATA PAVVQLCAQV
PTAGEHEFGV IKEILEKNPE AANSLEVLTG MLQHFSAASK
//
