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Database: UniProt
Entry: Q6SL98_BOTFU
LinkDB: Q6SL98_BOTFU
Original site: Q6SL98_BOTFU 
ID   Q6SL98_BOTFU            Unreviewed;       992 AA.
AC   Q6SL98;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Putative histidine kinase M3YPp {ECO:0000313|EMBL:AAR30106.1};
DE   Flags: Fragment;
GN   Name=M3YP {ECO:0000313|EMBL:AAR30106.1};
OS   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559 {ECO:0000313|EMBL:AAR30106.1};
RN   [1] {ECO:0000313|EMBL:AAR30106.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B05.10 {ECO:0000313|EMBL:AAR30106.1};
RX   PubMed=14665450; DOI=10.1128/EC.2.6.1151-1161.2003;
RA   Catlett N.L., Yoder O.C., Turgeon B.G.;
RT   "Whole-genome analysis of two-component signal transduction genes in fungal
RT   pathogens.";
RL   Eukaryot. Cell 2:1151-1161(2003).
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DR   EMBL; AY456056; AAR30106.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6SL98; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43719:SF30; TWO-COMPONENT SYSTEM RESPONSE REGULATOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AAR30106.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AAR30106.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          508..777
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          831..964
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          809..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         893
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAR30106.1"
SQ   SEQUENCE   992 AA;  111449 MW;  FE176471CAA0A79B CRC64;
     TELGPIDSWP VELRRMCNFL MSDPRPAAMY WGQSRVMMYN EPYMLVTGQK HPGMMGKTFS
     EAWAEVEDAF SDSFNKAYKT GKASTMDDAR FFIERYGYLE ETYYSLSILP FSCNSYGSHI
     AFYNPVFDTT RQVVADRRMI FLLRLGQFIA SSREPKDFWQ QLLRGLEPDH PDLPFALLYS
     AGNDVNETLS ESSALSHNSN WVLEGSVRVP DAGKNVPKHI NSENPMEEFL PSFSDLVKLD
     CPTLLHREDG TIPSSLTAAL QGTIAWDTVV FLPIRATTET VLGFLIIGLN ARRKYDDDYR
     LFIQLLSRQL ATSMAAAVLV EDEIQRGRMA AEHAYQDRNR LSMKLEIQAH EASEIESRFR
     KMADLAPVGM FHTGVDGKLI YANELYYNLT ELDRDIATNT GWHEVIMEED WPIVDTQWKK
     LMDGEPVSFE IRLRALFKGA DKIGDEEIDG AIWIIAAAYP EKAPDDTVVG VLGCFTDISR
     QKWAEDFQKR KMLEAIELKR QQENFIDMTS HEMRNPLSAI IQCADMIGLS VKEFDGGTND
     VILPREAVHG YADAASTIIL CAQHQKRIID DILTLSKLDS DLLFVTPTEV QPLPIIQNAL
     KIFDGELQKS DVALRFHVSP SFEELNIDWI KLDPSRLVQV LINLVTNAIK FTQTQPKRNI
     AITVSAALEP PSTPGLVYLS RTNIHKDNTP EGEWGDGEIV YLHIEVQDSG RGLDETERNL
     LFKRFSQASP RTHVQYGGSG LGLFISRELT ELQGGQIGVA SKAGVGSTFA FYIRTRRCDP
     PDDKDSFVPQ MDVQAQNNII TNNSLARVKG PTRHPLRSRR SQSPASSAPK HILIVEDNIV
     NQKVLSKQLR SAGCIVSVAN HGLEALEFLE KSTFSTSLPE GVSGIPCNIL LMDLEMPIMD
     GLTCVRQIRK WEREGRVKGR VPVIAVTANA RSEQIARAKE AGMDSVVTKP FRIGELVPEM
     ERWLIRGVVL DRAKEGARDE RAGVERRDSA PI
//
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