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Database: UniProt
Entry: F9XM35_ZYMTI
LinkDB: F9XM35_ZYMTI
Original site: F9XM35_ZYMTI 
ID   F9XM35_ZYMTI            Unreviewed;       980 AA.
AC   F9XM35;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:EGP83517.1};
GN   Name=M3YPp1 {ECO:0000313|EMBL:EGP83517.1};
GN   ORFNames=MYCGRDRAFT_63861 {ECO:0000313|EMBL:EGP83517.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP83517.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP83517.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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DR   EMBL; CM001206; EGP83517.1; -; Genomic_DNA.
DR   RefSeq; XP_003848541.1; XM_003848493.1.
DR   AlphaFoldDB; F9XM35; -.
DR   EnsemblFungi; Mycgr3T63861; Mycgr3P63861; Mycgr3G63861.
DR   GeneID; 13396487; -.
DR   KEGG; ztr:MYCGRDRAFT_63861; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_82_4_1; -.
DR   InParanoid; F9XM35; -.
DR   OMA; MACITDI; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000008062; Chromosome 11.
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   NCBIfam; TIGR00229; sensory_box; 1.
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; PF13188; PAS_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGP83517.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transferase {ECO:0000313|EMBL:EGP83517.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          352..422
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          505..781
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          842..972
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          812..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          314..348
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         901
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   980 AA;  108879 MW;  CA6536697F5553FA CRC64;
     MSSWNDRLRR SVNFLMGDPR ASVIMWGPQR TMIYNEHYKC ILEKKHPCAM GRSLGEVWPE
     VPVLADAIAR ADETGCSSQT DRELHFVERL GYLEEVYGSW TLVAVLCGEQ SMFYATIIET
     TEQVVYERQK DSLLRVEKET ADARSEAEYW SGIARGLESN NQDAPWAVVY SSKPARSSSG
     ACTVASHDID FASREWKLEA RLGILDAATP LTIDAEWSAA HFTPSFEAGM TSGEVQLLRL
     SDGTFAPHLH SVSTSRAYGD CCDSAVLIPV GRLNTGYFSG FLIMGINSRR AYAEPYQAWI
     KLLLQQLSSS LSSLNVIEEE NRRIQRAAEQ AALDRTQLTA KLALTEREAR NNELRFRTIA
     DHVPVAMYEI SVEGDILYAN DSYFELLGLD RNNLHPFCWV DTIHESSMET YEAQFEKLTA
     GESVQYEAMM KKPFIANDVL HGKWIEGETW ILMAGYAVRN ADGSIKSIQG ALIDISRQKW
     MERSQERRMQ ELVELKRQQE RFMDMVGHEI RNPPSAITLC AESILDSLES ALETSNSVIT
     IDRESIESHI ENAEVITTCI QHQRRIIDDV LTLSKLDSGL LVIAPCEVQP SHLIEQSLRM
     FTGEFQESGI NLQYNIDQSY YDLDINWVLL DPSRLLQINL NLVTNAIKFT RNEPTRNITV
     TLAASRTKPT HSPNGTTYLD AAMPDKSTPL ASPALTSAEL TDSVYLMIAV HDSGIGIPAQ
     ELSNIFLRFQ QSSPKTHVRY GGSGLGLFIS RELARLQGGK IGVASEHGKG SVFEFYVRTK
     RCAKPEGGKM SFGGPGDAGD GRRTSLRRMV SNYEGKGGRR AGSPKREGGG TGVGQSERKK
     FHVLLVEDNL VNQKVMAKQL MKAGHVVALA NHGREAVEYV QRTKFASGDG AGEELDVVLM
     DIEMPIMDGL EATRLIRSME SSGALHGTVP VIAVTANARG EQQMTAREAG VNAIVTKPFQ
     MAELMHEIHR VAARCRSSNA
//
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