ID M7U410_BOTF1 Unreviewed; 754 AA.
AC M7U410;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative bacterial transferase hexapeptide protein {ECO:0000313|EMBL:EMR81368.1};
GN ORFNames=BcDW1_10018 {ECO:0000313|EMBL:EMR81368.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR81368.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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DR EMBL; KB708080; EMR81368.1; -; Genomic_DNA.
DR AlphaFoldDB; M7U410; -.
DR STRING; 1290391.M7U410; -.
DR HOGENOM; CLU_013964_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd03357; LbH_MAT_GAT; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR23416; SIALIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR23416:SF76; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF12464; Mac; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000313|EMBL:EMR81368.1}.
FT DOMAIN 326..355
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 47..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 82890 MW; BC984320C31E0F41 CRC64;
MAPNTMNTEN CPLETQELVN LAREILVVNS GSEEGTKISR NILKMASPEG TDKHAESPTA
RFTAVNGRSQ NETSPTTNGN GNGNVTSAGA NGNGVARRGS DERANGQPRI SPPGHEKLTI
TTTQDQDWSS SKNGERTHLP DRQMNTSQNS NHYSDENSHK RKRSGSMDQG SSSANSYHSH
ALPNSTKATP TTATTESDGI RDDGSVRAKS QPHLDTRETY SADSQYRQFM SATDSARDTP
SSDLWHTRHY PQHPQVASDE HIGEVLQRAS QNLDAQQHEY DRRTLSGDDN RYADPQSAYS
QERRELSAQS DLKKRKRNFS NRTKTGCMTC RRRKKKCDES RPECNNCLRG GFVCSGYQQR
GSYPKVEMKQ TPVPLQSKTE YESPSSYTQP SPYGNQPGIP TRREPLPGYR GQSLRVDPHS
RGITDTDDQA SATTLPSASI TSPENNRISA SGYGIQQTPT PVSANSAHPD RYKSEYPRVG
PLHDLSRQEP RTEPDTGTPN SAREPTSALP NLLNHQIHPD SPHSSAQVAA QLALSHPASR
QRTQKEEMLA GRHYFPFDKE LVLERERCNT ACWRFNNSTN PNNGVSPEER ARQFRDILQP
RDHVISPTQA TPVTPVGKVG DNVVVEAPFT CDYGYNISIG QDVAIGKNCT ILDTCEVKIG
DRCNIGPNVN LYTATLHIDP KRRLGSRGPN LGRKIIIQED CWIGGGVTIL PGRTIGKGST
VGAGSIVTRD VPPYTVVCGN PARVIRGLYP PHEG
//
