ID Q0UH57_PHANO Unreviewed; 1242 AA.
AC Q0UH57;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_08907 {ECO:0000313|EMBL:EAT84075.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT84075.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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DR EMBL; CH445337; EAT84075.1; -; Genomic_DNA.
DR RefSeq; XP_001799211.1; XM_001799159.1.
DR AlphaFoldDB; Q0UH57; -.
DR EnsemblFungi; SNOT_08907; SNOT_08907; SNOG_08907.
DR GeneID; 5976110; -.
DR KEGG; pno:SNOG_08907; -.
DR VEuPathDB; FungiDB:JI435_089070; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_82_4_1; -.
DR InParanoid; Q0UH57; -.
DR OMA; CNTDISA; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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; 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; IPR001610; PAC.
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 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; 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; SM00086; PAC; 2.
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; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 701..759
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 777..1055
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1098..1230
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 461..488
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1159
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1242 AA; 138998 MW; 79279EB57965B074 CRC64;
MQTVDIRGLY DEDPRPTFVV DCDDQPAGIY HVNSALLDLP HLALSLHAHN ALRDWWDPSS
RVASRHQQEF RHGRYRWAKF TACQRWLIIT LIEQPPQTEE PKGHLQQSSQ LARVASPLHP
HAETIFTVKI QSPELREHIE RLQKVDWGRT SLGPIAGWSY ELNLLVTTLM LETRPTAIFL
GFDHIIVYNL AYGAVSGSRH PAILGQSILD AWPEVADPQT RFADTPEKEY HFMIERNGFV
EESFFMWSLI SLVGVGQING MYSIVTEVTK QRLLERRVNA LLRFGQLSSE AVDAKAFWKS
IREAIYPSEY DFPAAVLYSH CEVETTGSAV TYSKTTSRNC SLEWTIGYRV NHPDIPQKLD
LEQDLPLGRA IAGSAKKGVA TLYRHEDGRL PSTLFTDVEK RGFGDPCKAM LIIPVRTSNE
TITGYIIVGL NTRRPYDTEY QDWIASVALH EEEVRNRKRQ EEEAARDREA LSAEVAVLAQ
EASDVTEKLS NFYQLANAVG LGYFEFAISG ELVHANEAFF HQTGHPRDLS NSRPFAFLEH
VYGPDRELAT EHWRMSASGK STTYEMRWKK KPNADTGSED DTRDYLWTLT ACVPIKTEDG
IVTGIFGCNT DISGQKEATR IALLRVEAER RLASFTQTAP VGFYQCDSDL KIQYCNDQWF
NIVGHPITDI SAIDWTSRIY QDDLEAVTID SHIVMQVNKL HTFSFRVKKL WTGPDDLSTP
TWVLATATAH RDKDGQVVSV MGTLTDVSQL KWAEAIQRSR VEEALESKRQ QENFIDMTSH
EMRNPLSAMV QCADSISSAL AEMEAAINDN ALTTQPSLQT KIKDLVGTSI DAIDTIQACA
THQKRIVDDI LTLSKLDSKL LVISPITVQP DALLQDSYKM FKEEANKARV SLRVHSDASL
KDLQIDYAIL DPSRVLQVLI NLLTNAIKFT RTQPVRKVGV IMSATREPAG RSGIEYVPQK
ALSQDFLDEQ EWGSGEVFYL HFTVTDTGCG LTTEQKNKLF LRFSQASPKT HVQYGGSGLG
LFISRELTEM QGGGIGVQST QGVGSIFSFY VKSRSAAPGR RNSTTFNLPS RAKSHIIQDK
QPMLLETATP PLPSPKYHIL VVEDNLINQR VLCNQLKKIG CTVQVANHGR EALAELAKTK
YWKQPAISEP HDLSVVLMDV EMPVMDGMTC ARKIRSLQES GDITGHVPII AVSANARREQ
IEQAKGAGMD DAISKPFRIP ELLNVIDTLL SGNAGGGNVR RG
//
