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Database: UniProt
Entry: E5AA18_LEPMJ
LinkDB: E5AA18_LEPMJ
Original site: E5AA18_LEPMJ 
ID   E5AA18_LEPMJ            Unreviewed;      1294 AA.
AC   E5AA18;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Similar to sensor histidine kinase/response regulator {ECO:0000313|EMBL:CBY00509.1};
GN   ORFNames=LEMA_P016390.1 {ECO:0000313|EMBL:CBY00509.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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DR   EMBL; FP929138; CBY00509.1; -; Genomic_DNA.
DR   RefSeq; XP_003843988.1; XM_003843940.1.
DR   STRING; 985895.E5AA18; -.
DR   EnsemblFungi; CBY00509; CBY00509; LEMA_P016390.1.
DR   GeneID; 13293191; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_002763_0_0_1; -.
DR   InParanoid; E5AA18; -.
DR   OMA; FDRHTQY; -.
DR   OrthoDB; 12386at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF80; HISTIDINE KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF01590; GAF; 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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBY00509.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          598..863
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1098..1228
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          44..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1158
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1294 AA;  142405 MW;  A7EC1502FC315B11 CRC64;
     MADSLDVARS YAVARRRHKM EQTDSAKIRE QQFYLYYPQH SKSEDLLSRH PSPSPVLHAA
     TPPGTPPQTQ TTADYVPRPS EDKALTAFAQ LGALRLNARR CLISFFDRKD CFLLAEGTKT
     LSLDTGEAEF AEDRLCFGSV VFPKEQSLCY YTVNLAPKFT NLPLDDPSDL PSLVVNDLAR
     DDRFKDLPFV KGPPKSRFYA GVPIRSPSGH SIGTYCVLDD QPRDGLTPHQ LAFLKSMAGT
     VMRHLEMTRA TEDQRRGKIM VKSLGSFAEG KSGLENWWQD PWDLAEQSVT AVIPDTINLP
     MRQQPFALST AALEPIVLDK IQSAGSSVPS TKNSTVTSPA SVQPPSTATP CSITLPENPR
     PLVPTTTSST SANMPTDNIA PEVRATFTRA ANMIVDATEA EGVSFFDAKI STFGGLVDDD
     FDPDILPEPD KPCVLLGSAI SKTARESDSQ SANDVAMSES VLKHLLRLYP HGHIFNLDDD
     MAMSAFNSPS AGGGDLELSD GFPFTTAQKS ESMRSMDDEA YLRTVFPKAR SLVLYPLWDP
     HRDRWFASAV IWSSDPKRVF TSEQELSYLA AFSNSVMAEV ARLDTKLADA AKADFISSIS
     HELRSPLHGI LGMTDLLKDS YIDNQQVSHV ATIETCGKTL LETINHVLDF AKINNLTRGA
     SKRQKKRTQN ARHMISPGQP HTNDIMTLIN DVDMGILTED VVESVFAGYT YAKTSAQTYE
     LSTPTSNKPK LSVVLDINYS GNYVFRTQPG AWRRVIMNLF GNSLKYTPSG FVKVKLEVKR
     KPGALEDRCE FRFSVTDSGI GMSEDYINNR LFHSFAQENP LSQGTGLGLS IVKQIVESLG
     GEVEVRSEKG RGTKFMVKCP LKESSMSPSF CPTGSEQDKK RQLQAIAKRT KGLKVAFRGF
     NTEEDQYVEG LKTKSASKLS LKALDSLCTD WFGMFKCEEG DKATKPDLII ATEACAKILR
     SHQNQKPKDA SEAPPVIVVC PGAAAAQSTT AITVPGIVFE CISQPVGPHK LAKALGSCLD
     RHTDRQDELK SGTGPPAPKI VELDLKENAD RHRTDQFTYL RDGSRPNLSS INSAPEIRSV
     GHCPVKKSIY SAPTRALNCL CVDDNPINLR LLRTFVDKLG HRHVLAINGL KALEHYKAAH
     EPPLSEDESN RVDVILMDIN MPEMDGLEAT RQIRAHEIRN NLPKVTIIAL TGVADTDIQQ
     EANSSGVNLF LIKPVRLGDL EVILKGVVTG QDKADLEFEQ EKEKQKALNA ARLRATSDGN
     EKSRLVSVGV RAISENDPVQ KTVRNQEIKR LSMG
//
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