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Entry: A0A2L2SUA2_9HYPO
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Original site: A0A2L2SUA2_9HYPO 
ID   A0A2L2SUA2_9HYPO        Unreviewed;      1372 AA.
AC   A0A2L2SUA2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI60992.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LN649230; CEI60992.1; -; Genomic_DNA.
DR   STRING; 56646.A0A2L2SUA2; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000245910; Chromosome ii.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 3.
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; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 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; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245910};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          559..629
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          863..1156
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1209..1359
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          120..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1284
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1372 AA;  152461 MW;  38083B73674774DC CRC64;
     MPPSALHNLG LVDLVASDPR PTFVVALPEQ ASCTHDSSAK ILYRNPALQN LHTLDQSISF
     IPQDASHSPF WNWVTSPPPA PASEGDAAGP AMTNTQHSLP YLGVFWTRSI VLSQWVVMSG
     NETPPSSEPP RKVRIEGKQG EETRKYPQKS PLDNARLPSR KKSESKTPMV YRDESNPGLM
     VPVSDSEAEP FLDVVQSVDW ESTSLGPMAD WPAQLQYTFN QLVSDSRPVA LYWGPEYITI
     YNEAFSKYCG ARHPELLGQP ATEAWPQLKT RLDEMTASPM KNYSNAEDES KFFIPQADGA
     FEETYAKSSM VPIVYEQNCL GIQHSLLEMT SKRLWERRMK MLLDLGEALV STKDAKSYWS
     RMIEELERWN PAYDVPLAFI YSVEESDVDS TSSKYDCSKT CRLEGSLGVP LGHAIAPSVL
     KLKDTDDGMA SILRRSLDER QPVLLQTKDG TLPKDLLRGL EWRGFGDPCQ AAVVLPVRPT
     KEEHVMGVLF LGLNPRRPYD NDYRQFILLL NQKLTSSLAS AVLLEEEARR RRNITEQAAY
     DNAMLTQRLE YQTKQAERST KTFTAVAEFI PVGMCFVDNQ GNITFANDAW HRITGYPKGP
     IAQGALLESV LEEDKEKVMQ AYKDVQKLDT VTFEYRIART ENTTEPPSFR SSAGPLPVMD
     EGVSRHILAS TKAERAPDGS VIRILTCLTD VTVQKDTAEE AVRRAQEAEN LKRLAEFATV
     GMYDVSMDGR LLSANNLFWE LTALEKVDLT KVDVRPWPEC VVEEDLYILQ ESLDKLVESG
     RTETAEFRLR NGWVSEDGNG NSSVAPRWVL ATFMPVKSSD GVIQSFTGCL SDVSVQKWQL
     EQEKLRKEEA IESKRQQENF IDMTSHEMRN PLSAILHCTD AIIASLARVQ DISDNSAPLT
     PTRNGTSGEG RRIGERSVEE RKLLEDSIEN AETIVTCAQH QKRIVDDILT MSKLDSKLLA
     VTPCTVDPIQ IVNGALKMFE VEARRVDIEL TSYVDKSYKD LAYDYLDLDP SRVQQVLINL
     LTNALKFTKS GTTRNVTLGV KGSLTPPGED MTAVQFIPRF CDVSEEYDQP ALKERTKAVY
     LLFEVKDTGQ GLTAEEMGSL FNKFVQASAK THTKYGGSGL GLFISRRLTE LQNGAIGVLS
     QPGVGSTFAF YIEAYVPSEA SRNEALAAAA AARLITGGSD ADSADGKQNC RDIRLQKHQN
     PGGNVRLDGI LVVEDNLINQ QITRRGLTDR GFMADVANHG VEALEILRRR QSTVPGLGLN
     GVPGRSGRSH THSLPIAINL VLMDIEMPVQ DGLTCTRIIR ELEAEGEIFC ASGGRMPIIA
     VTANARPEQV MEAKQAGCDD VMVKPYRIPE LIEKMQVVVR RMGGLSPNSP VR
//
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