ID A0AA38SDN5_9PEZI Unreviewed; 1009 AA.
AC A0AA38SDN5;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Protein byr4 {ECO:0000313|EMBL:KAJ9165024.1};
GN ORFNames=NKR19_g805 {ECO:0000313|EMBL:KAJ9165024.1};
OS Coniochaeta hoffmannii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=91930 {ECO:0000313|EMBL:KAJ9165024.1, ECO:0000313|Proteomes:UP001174691};
RN [1] {ECO:0000313|EMBL:KAJ9165024.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EXF-13287 {ECO:0000313|EMBL:KAJ9165024.1};
RA Gostincar C.;
RT "Fungi with potential for degradation of polypropylene.";
RL Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
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:KAJ9165024.1}.
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DR EMBL; JANBVN010000007; KAJ9165024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA38SDN5; -.
DR Proteomes; UP001174691; Unassembled WGS sequence.
DR GO; GO:1990334; C:Bfa1-Bub2 complex; IEA:InterPro.
DR GO; GO:0044732; C:mitotic spindle pole body; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IEA:TreeGrafter.
DR InterPro; IPR034586; Bfa1/Byr4.
DR PANTHER; PTHR35140; MITOTIC CHECK POINT PROTEIN BFA1; 1.
DR PANTHER; PTHR35140:SF1; MITOTIC CHECK POINT PROTEIN BFA1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP001174691}.
FT REGION 34..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..310
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..494
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..645
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 111415 MW; C5416BB60E230341 CRC64;
METLRLKPRQ PVEDDVENWD DDDFMIEGED LTFQSQANSA KAPSHRRDSH SSLRSEFESI
SGDVEEHVHI PGDDEESTLD AIAAAAKAGI PLPTNVPSSA LMGGTIKRLG GRKIKKIIQE
DWGDDLEFPE SGQGLTIKTP DTSKFPEVLR QVSGSSIAES PTKTFKVASP PLVQQEKLPN
KLNILTGGVD LDRFRDEDDD DDFFGDGGDT IKVSKSRQPA KPISLITPPT PQKRGEVVED
DFETDFDLPS DGKLKLTTRR DIPKTPAVNS LDDFDWGEGS LGTRFGGTRR DGRSNRSSSA
SALSPSIASS ITAESEDEAL DGLVLPTGPL NWEDRLNRRR QSRSPERPEK LEPLPEEPPK
SAKTSPPPEA DKEDFLAGLD IGDGEVFDSR KLTLHRNIQV KETRPASPSR PKTAVALKFT
NKPVAGSRLP RPMGPMASHH ERSHTQSSLE PVSESGGPIP PSRRSLSRLG GHSAQSSVSS
IPTPTTPLSA TSLPPTTPRR KELGQKTSNV SLREGPTTTS AQLLRLKRSL PVMRPQQTST
RPAASRNSYD RPPSRSDMYG RPPSSLRPKT PTERPRTMES PAAQARKPPV PFLPAGASAN
QSHNINARTA RTFRRHDSDN SIGSSVDFRP TSRAMSRSTM RSPSPRKYRN VEKIAHEGPW
HQLNKPRRVR HFGDGHELDG FDDLPTSTQT EAKFMRQPVT SGPKAQLRSK MYQNVIPDRT
STPSPLTPYS QSRFDNVPSF ARDTAASRIA RETALAQRIP SGGPLAPLTA QRVAQLSTRS
NLNPQSPQPT LRSKKTRKPP QLKPHLIANL NPPKESKMVN GMFYNPETFR WEGNDNALGA
FDVPASSPST VSIPPYMLRE KENSTPRPAL ITNINATKGV QVVGGMVFDP QNMCWLKLGP
QTGQTEQSDP MDGFNGIDSD DDVFKDIPDL EDHTMNESEG GQGRVSDIKD DWLVGEEFDV
GPEFVRRQRE EEERWRRKCE SWITGGEASR DRTAWRWAIR DIVSSSVRD
//