ID A0A0W8DQ12_PHYNI Unreviewed; 1940 AA.
AC A0A0W8DQ12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Hybrid signal transduction histidine kinase K {ECO:0000313|EMBL:KUF87740.1};
DE SubName: Full=L-threonine dehydratase biosynthetic IlvA {ECO:0000313|EMBL:KUF98459.1};
GN ORFNames=AM587_10017378 {ECO:0000313|EMBL:KUF87740.1}, AM588_10011629
GN {ECO:0000313|EMBL:KUF98459.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF98459.1, ECO:0000313|Proteomes:UP000054636};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUF87740.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, Race 1
RC {ECO:0000313|EMBL:KUF98459.1}, and race 1
RC {ECO:0000313|Proteomes:UP000054636};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KUF98459.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNFO01001974; KUF87740.1; -; Genomic_DNA.
DR EMBL; LNFP01000068; KUF98459.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8DQ12; -.
DR EnsemblProtists; KUF87740; KUF87740; AM587_10017378.
DR EnsemblProtists; KUF98459; KUF98459; AM588_10011629.
DR OMA; DVNETMC; -.
DR OrthoDB; 90212at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 10.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 10.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 10.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 10.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 9.
DR SMART; SM00091; PAS; 10.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 8.
DR PROSITE; PS50112; PAS; 10.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:KUF87740.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000313|EMBL:KUF87740.1}.
FT DOMAIN 1..53
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 104..174
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 227..298
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 301..353
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 347..417
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 420..472
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 466..537
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 540..592
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 586..657
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 660..712
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 706..777
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 780..832
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 826..897
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 900..952
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 946..1017
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1020..1072
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1066..1134
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1140..1192
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1196..1420
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1466..1587
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1810..1911
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1701..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1517
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1849
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1940 AA; 214072 MW; A2151CF326D29B21 CRC64;
MDVTGRVTFW NNKLTELSGF PSVDVVGRPI TELVVTDRTA EVTRGLKHAL ADVNTTVHGV
EIELNTPELG RNVKLLVNLT VDVDDNNKAS NIVAIGQDVT VWMQGSQYAR VAQQANAPIV
ELDRDGRITL WNPKAEAVTG YAIDQVVGTP LVDLVHDEFR VLVAELLARV ASTNTSVSEF
ELPLKTASGA RVELLLSLTP QTSVDGAGTT VNRIVAIGQD VTARNVSEME YSKLVDSANA
PIFGVDTQGC VVIFNKKASK ISEYWPGEVM GVDLVSFLIH EDYREKVAAV FQKALRGIET
ANFEFPLITK HGRKVEILLN ATPRYNHAGA IVGVVGIGQD ITERIVQEQE YNRLIDTANA
PIVGVDKKFC VTIWNKKAAT ITDYSYTQAI GKNLLGFIAE HARDTVKDVL SKAMGGIETP
NFEFPLVTRS GRQLDILLNA APRFDHSGAI TGVVGTGQDF TDQRAQEEEY IRLIDTANAP
IFGIDMDGRV DIWNRKAVAI TEYTVLEARG TRLVESFIPH DYRAGVSDVM SKAMEGEGTA
NFEFPLITKT GRRVDILLNA TPRYNQHGDI VGVVGIGQDI TERIVQEQEY SRLIDTANAP
IFGVDMTGLV NIWNDKSAEI TQFTADEVIG KDLVQEFISE GYRSAVGLVL SQALNGVQTA
NFNFPLITKS GRRVEILLNA TPRYNELGEI VGVVSIGQDI TERIAQEQEY SRLIDTANAP
IFGVDKEGCV NIWNKKAAEI MQYSNNEVVG ENLVEKFITE DYREAVGAVL SKALDGIETA
NFEFPLVTKA GRRVEILLNA TPRFNEHGTV IGMVGIGQDI TDRIAQEQEY ARLIEKANAP
IFGVDSEGKI NIWNHKTAEM TRFSKEEAVG KDLVSWAIPE EYRDAVETIL WKALEGDETS
NFDVELKKKN GRTVNIRMNA TARFDQHGQI VGVVGIGQDL TDRIVQEQEY TRLIDTANAP
IFGVDANLCV NIWNKKAAQI TKYTTAEVIG ENLVETFISP EYRPAVADVF SKALNGIQTA
NFEFPLITRP GTRIEILLNA TPRNDMHGNI VGVVGIGQDI TDRIAQEHEY FRLIDTANAP
IFGVDTFGCI NEWNQKIEEI TGYHKSTVLG LSLVDAFINA ENRSEVRKLL NQALIGIDVG
EMELPMTTAA GRSLLLLVNA SSKKDMHGNI RGVIGVGQDY TAKKHMEAAK VNFLASFSHE
LRTPLNGVLG MLELLRDQKL DKTPERYVHI AYISGSLLLN LINDILDLSK IEAGHMEISA
DPFQMEDLLE YSVEIFKFKA REKHIKLTLE CSPKVPKRVI GDVSRLRQVL LNLLSNAIKF
TNEGSITVRC NMVPSPDLPK HCVKLLFQVI DTGVGMDDEE KSRLFSLFTK LERTRKNNPT
GSGLGLAICK QLVELMDGDI DVDSELGEGS EFFFTVVVRR PEDEEDELIQ KFPAVLAAEP
GAVSSLAGNN ARHNASMSEL VPKHARILVV EDNEFNWEVV KSFFMEDNHL LQWETNGLDA
YQMYQEHHDS YDIVLMDCEM PIMNGYESTR NIRVFEKQHK LPRIPIIGVT AYAMSGDRKK
CLDAGMDEFI VKPISKTELR KAIRKWMRVR FLGQHCPRPS RVESVDTSNI DTDALCNQHA
ANLVAASRHK EKLDLDRAIS DLELEDPMMI GQPSGIQTAA GSEALLMSLT TISESKSNST
SSGTVGRTIG PVDVLRETPE ATNSMQHPSG APPTHPGNLV NASNIVGTNL FAAAKAAGIY
PMNVTEPTPY SSPNSFASSD GNNQQDSESS TIVANKPARA YSSTMAPEDI VIPTGDPIDY
SLGVEQCGAN ESLFVNLLEK YAGLSEEFMR RIEEAYSNDD FVVLRRESHS LKGSSAYVAA
MRVSKAAFRV QLATEHVMEE SATEDNYTSL KDAFQLLKSE HRALRGYLRR NFSFRTSTGN
GGQEAKKKNN GGGDNACVVM
//
