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Database: UniProt
Entry: A0A179FER2_PURLI
LinkDB: A0A179FER2_PURLI
Original site: A0A179FER2_PURLI 
ID   A0A179FER2_PURLI        Unreviewed;       730 AA.
AC   A0A179FER2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sensor histidine kinase/response regulator Fos-1 {ECO:0000313|EMBL:OAQ63790.1};
GN   ORFNames=VFPFJ_11389 {ECO:0000313|EMBL:OAQ63790.1};
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ63790.1, ECO:0000313|Proteomes:UP000078340};
RN   [1] {ECO:0000313|EMBL:OAQ63790.1, ECO:0000313|Proteomes:UP000078340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ63790.1};
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT   Phytophthora in bio-control Purpureocillium lilacinum.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ63790.1}.
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DR   EMBL; LSBI01000030; OAQ63790.1; -; Genomic_DNA.
DR   RefSeq; XP_018172985.1; XM_018328456.1.
DR   AlphaFoldDB; A0A179FER2; -.
DR   GeneID; 28893505; -.
DR   KEGG; plj:VFPFJ_11389; -.
DR   OMA; VGFHANP; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
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; 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; 1.
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; IPR000700; PAS-assoc_C.
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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; 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; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OAQ63790.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000078340};
KW   Transferase {ECO:0000313|EMBL:OAQ63790.1}.
FT   DOMAIN          179..252
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          254..305
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          320..541
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          587..704
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         639
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   730 AA;  80625 MW;  781C192286E29FA9 CRC64;
     MIRGRKRPAE DDPLTDRSTL SSTVASFPTP QQPLRISKAP TGGPAAVSEM SGLLDYSPVP
     TLLVSPSNRI QRASIALLEA WDCRRDQLVD RDLFISLYEG SLTERFDRIP LVYAIESAIT
     ARAVRLCHAA YVAGSVSWNA RILPIHRDEE LLGLMLEWEV DKVNVTVADG EVPRNRLPNE
     DAFRILVQAV KELAIFLLDT RGNLVTWKTG AELDEGYEKE EIVGKHFSIF YSADDVQSHK
     PERALEISLR EGRAEDEGWR YRKDGTRFWA NVVIIPIYNH GVHVGFGKVT RDLTERKEAE
     LRLIAAYEES GKLKSDFLAN ISHEIRTPMH GMLSACALLL DSGLTEKQLE MANMIEDSGR
     VMLQIINDTL DYSKLAAYSL SINSDIMDVA SIIASVVGSC RASLNPGVSL KLHLAPDLPK
     WADGDALRFR QVAENIVSNA AKFTERGLIQ MSVSLLTQDA GTYTIMTEVA DAGPGLSNKE
     VPKLFEPFTQ LDTTYQKRRE GTGLGLSIAK SLAGLMGGDI GYRPNPESQG SIFWFTVKLK
     RINNILEVRS VGDQDFGKTT KQLHVTQDDD NSAGELAQLM EIAPAARILA AEDNIINQKV
     LVGTLRAVGF QHITVVSDGA QAVSVLSKTP NAFDLVLMDI SMPIMNGYEA TIQIRNSGIR
     LPILAMTAYA LKGDMERCLE NGADDYIVKP IHRQLLVRKL LQWLIKPCDS RHQEVGHHQS
     AIGDSDVASV
//
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