ID A0A420IQK7_9PEZI Unreviewed; 1278 AA.
AC A0A420IQK7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE SubName: Full=Putative histidine kinase-group viii protein {ECO:0000313|EMBL:RKF76787.1};
GN ORFNames=GcM3_076006 {ECO:0000313|EMBL:RKF76787.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF76787.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF76787.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF76787.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:RKF76787.1}.
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DR EMBL; MCBQ01007687; RKF76787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420IQK7; -.
DR STRING; 62708.A0A420IQK7; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.30.450.270; -; 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 Gene3D; 3.30.450.20; PAS 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00387; HATPase_c; 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; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RKF76787.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 445..607
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 833..1005
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1123..1255
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 124..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 142650 MW; FEFDA60F0AB1A92C CRC64;
MRSTMRQLLG GKKSHKLAID ENSDNCNVGP NLSSSHNNLA PDGMGTNINQ NGITNETSGG
VMNVMRNGMS HNYVNTPTTD GFRNNTGEST ESSFYNSMSK GNAIDHNMGN NYGNPIMSNM
GMRSNSLGTG QDSNKYYSKY SNEGSENPSS LDTGTTINNA NNTYLSPHFE RLPASPSNSR
TTPSRASAMT GISSMPSQQS AAKNEYRKVT ERSQIINQTA SSPPLVSTGI ESTSTSKNYL
RCEDEPIRVP GAIQSIGALI GLRYSENGDL EVKVASENSR KILGYGPEQL FALGSFLDVL
EDPSRQEIII QLDHCIRSGH TTSTATINPN FFQITLKFPY EPDCRLWCTI HQAPNTDGLI
ICEFEEYSEN YYLKDVNATK SLPQIPFNSS SPDVNPEEFQ KSTTSVSKPI APLKIAEQRD
DKLFSSLDIF CCLSRIQEQI KRCNCVKEVQ DVIVGLVSEV TGFHRVMCYQ FDNNNNGSVE
AELVNPNAST DIFRGLHYPE SDIPPQAREL YKVNLIRLLF DRDDETSRLV WRDGADYEDP
LDLTHCYLRA MSPIHLKYLR NMGVRSTLNI SLVIDDKLWG LISCHGYGEH GIRVSLPIRE
LCRCIGNCAS TNIERLTALE RIRSRRLPQY LPANSVPPSS DLLKLIEADF AILNIGNKVR
AIGRMEPFQE ATIIINYLQS CRVDRISSSQ NIKADFPDIS PPNGINTIAG ILIIPLNIGK
ENDFLVFFRK GQLRTINWAG NPQEKIFKSS NEYLEPRASF KRFTETVNNS SKEWTEDQLD
TASILALIYG RFAETWRMKA SSAYGKDKES EERDTTSARV DDTFNLKAAE ATRVLEALKK
EAQRKALDLT VSIHEDVPTT VIGDADCFKQ VMLYFIRNGF RSSQSLKVDV SLIRVQDDTS
YVELKVQDAG PGMTEEELDV SYPIFIINIY LHMVQETFQE FERAQSNEKW PFPNHVSPPN
PNEVNRGSVT LSVVATFVRS INGQIQVTSE IGKGTIFTVE FPYKCANGSE SSASRKSRNY
LLTSPMPPKR LSPQINSQSD GYERKTKNDV STPISNSFAL SPANSNANEN SRNLSARTPT
QSLVQTLQGT SANENQALAS YEKGGYKQNG NEQSQNFLEK KFTILIADND ANSSRMLESK
LLSAGYSVEV AHDGQECHDR FALNPSKFDV ILMELKMPLV DGVLSTRMIR IAEKEAKHRN
GSDNPQIAKQ RVTIIAFSSI LEEESRFDYI QSGFDGWLLK PVNIQRLDQM LQGLVDPKLR
TDALYVPGQL NKGGWFLP
//
