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Database: UniProt
Entry: A0A1C7M7J4_GRIFR
LinkDB: A0A1C7M7J4_GRIFR
Original site: A0A1C7M7J4_GRIFR 
ID   A0A1C7M7J4_GRIFR        Unreviewed;      1361 AA.
AC   A0A1C7M7J4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=dhkJ_1 {ECO:0000313|EMBL:OBZ72870.1};
GN   ORFNames=A0H81_06703 {ECO:0000313|EMBL:OBZ72870.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ72870.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ72870.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ72870.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:OBZ72870.1}.
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DR   EMBL; LUGG01000007; OBZ72870.1; -; Genomic_DNA.
DR   STRING; 5627.A0A1C7M7J4; -.
DR   OMA; CLAAQMD; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000092993; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 5.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 4.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 5.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 7.
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; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR   PROSITE; PS50885; HAMP; 7.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBZ72870.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          210..263
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          303..355
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          395..447
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          487..539
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          579..631
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          671..724
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          764..816
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          838..1064
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1209..1333
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1263
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1361 AA;  146898 MW;  59CA41F16637C678 CRC64;
     MARRMYTAEE ALSSIRETEK CGPESKKRRS VGDSPPMSSS GSSQPDTSCT DTNGFLNGAV
     SHSPFFTPVS SVESIPSTLS SIPSDIEMID SPRLPVDGEP TPIASQSAPA TATSAPGTGR
     TPSPMNINLD GLEKMRVRTN GTGIASAPPT VHADHVMCPG CGRIITDTAT ISKIVDITQI
     AGSNSPLVVP PGPLAAAAFE SGLSAVDELK LLKTQVQDVA RVCNAVARGD LSQKITVPVQ
     GVVMIQLKDV INAMVDKLGQ FAKEVTRVSQ EVGTEGKLGG QALVLDVEGT WRELTGVVNK
     LAANLTNQVR SIAKVTKAVA LGDLSKQIEV DARGEILELK NTVNGMVVRL RALAAEVTRV
     TLEVGSKGQL GGQAHVPDVE GVWLELTRNV NRMCSSLTDQ VRSIANVTTA VARGDLTQKI
     DIEVEGEMLT LKRTVNSMVD QLSAFASEVT RVALEVGTQG ILGGQAKVEG VQGTWADLTR
     NVNKMATNLT DQVRSISEVT KAVANGDLSR TVNVDVQGEM LDLKTTVNLM VARLSTLASE
     VTRVSLEVGT EGIMGGQAYV PDVQGMWKVL ADNVNLMAMN LTNQVRSIAE VTKAVAGGDL
     TKRITVDVRG EMLDLKETVN GMTESLSIFA DEVTRVAKEV GTEGRLGGQA QVTNVGGTWK
     DLTDNVNVMA ANLTLQVRTI AVATTAVARG DLTAKVTGVP VSGEILDLVN TINRMIDQLA
     IFAAEVKKVA REVGTEGKLG GQAEVGNVEG IWQEITMSVN TMASNLTTQV RGFAQISAAA
     MDGDFSRFIT VEASGEMDSL KTQINQMVFN LRDSIQKNTA AREAAELANR SKSEFLANMS
     HEIRTPMNGI IGMTELTLDS DLNRSQRESL LLVHSLARSL LLIIDDILDI SKIEAGRMTM
     EQVSYSLRQT VFGILKTLVV RASQNQLDLT YDVDPDIPDQ LIGDSLRLRQ VITNLVGNAI
     KFTPSKVSRK GHVALSCRLL ALDDQSVTLE FCVSDTGIGI AKDKLTMIFD TFCQADGSTT
     REYGGTGLGL SISKRLVTLM QGNMWVESEV SSGSKFFFTI SSQISPMSMD ATLAKMQPFQ
     KRNILFVDTL YDRTGVVQRV LELGLRPYVV HDVSEVADKA TCPHIDTIVV DSLNVTENLR
     EYEHLRYIPI VLLSPQSTPR LNLKWCLDNS ISSQVTTPVT AQDLASALIS ALESNTVTPV
     VAENDVPYDI LIAEDNLVNQ KLAVKILEKY GHQVEIAENG SLAVDAFKAR VQRNRPFDVI
     LMDVSMPFMG GMEATELIRS YETSHGLDPV PIIALTAHAM IGDRERCLQA GMDDHITKPL
     RRSDLMNAIN KLAGERKLHL ARNRVQHRSS FPMQTLLRGF R
//
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