ID A0A401H1M0_9APHY Unreviewed; 1564 AA.
AC A0A401H1M0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Peroxide stress-activated histidine kinase mak2 {ECO:0000313|EMBL:GBE88260.1};
GN ORFNames=SCP_1300750 {ECO:0000313|EMBL:GBE88260.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE88260.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE88260.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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:GBE88260.1}.
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DR EMBL; BFAD01000013; GBE88260.1; -; Genomic_DNA.
DR STRING; 139825.A0A401H1M0; -.
DR InParanoid; A0A401H1M0; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000287166; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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 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; 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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GBE88260.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 907..1163
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1430..1562
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1480
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1564 AA; 170921 MW; E6764EB32DB67918 CRC64;
MDNLSELPRL QSDPLSRSLS SLASDTPLVL SAHAAHAAPH IVLPRLTLPQ KGTRPPRRPS
TASSAEEKLI RLPSAHASSG LSTTSGTPAS TAGSASIISD DGEASMQHTN RWPHAAVASL
RAEPSRLSSS ADVLPSPFDL SPADEQLSQS MTVPEPQDVD VDYDWATFVN AYALGRWDPL
RTPHPPRSHL QPPNLARPSH AVSDDTLADQ SETIFDSPVM ESEVWQTPMS TCGSSFAVDL
GPPPGLDPAV MTISLPSPFV PGTEVGKLER QPNIPLNLPP FPHRLRNSFT DLRSSANSQS
MSPESNRPFS IPSTDATTAA AAIRWAAARV SVAPLALPSP EHELTDPMRG VTATIPGSHP
PDIYPDSLPN TPGVSRKTRL SSFWQGTQDV DDRRALPTIE ASPPVPAEEP SAEVKTATLP
VAGSLVPPAT APVRVVVDRP DVDYFGNAEP SRAENMLGRV EPERRTSAPP LFDREPATVP
ALPRKICLTR QTSAPLPTSS LYERRLRSAR PLSESSVPTL LGRAAKEENM FCELGFLAPP
NPPDELERRR ALYKFNIWNT GRDMNFDRIA HLVKLVFNPK IVTIALVDGT DEFLKSESGI
GTSIIPRIRS FDAHAILQRD DEPTVVLDAR DDWRFAKNPF VTGHPHIRFY AGCPLRTQDG
FNIGTLSIID DTPRREFSPR QRHTLKEFAQ IAMRELELWR DKIQLRIRDR IQNSMEQFTR
ECLEVDKEVD NEKVMSLSVG TSMEQVYERA AKLVKRTLDV EGAIVLDVSH VDVVETMGAE
CTMSITLHDA DAHAGATTKL LSSQEYTRLA EFFEKNPDGK ICEGVVPATL RPFLPTRIQY
ALTVPIFNVD KRPFALLCAY STGERTTPFL EGHELSYLRA IGVIILSAVL KRRMILADKA
KSLFISNISH ELRTPLHGIL ASAELLSETR LGHSQASFLQ TVQACGTSLV ETVNHVLDFT
KLSGNAKSGG VENVIHLSKV DLMQLVEEAT EGCWIGHRAR MFTSEIGSVY SPPMQDQKLA
VALPAPEKHV ETVVDVGHSE NGWTLRCEKA GIRRVLMNVF GNSLKFTSDG YVHVMLRQFP
DGPRNKVRIE LSVIDTGKGI SQSFLKNQLF HPFSQENPLQ TGTGLGLAIV NSIVCSPGVN
GKVDVWSTEG VGTEIKITFT AEAIEDEEVS SSDAEFAKLY DHLQRPRISL LGFDDPHRGV
QLLRDVVSTY LISRWGIQLA DGSDRGEIVI VNEDITPVTQ AITNRDASRP FIIFSSFRGD
LRLMSIVNDY EAIGGFARVI YKPVGPGRIC SVLRLCLHVL NIGRESRSKS TLLHQSQSSP
SLPPGTFELG ESGTHPSAFA RRFSEERGLK LAASGTASGR PSLGPRAVTA HPLSSYSRVT
STSDQDELEP EPAESLSGPE SPVRRTISVG TGGTLLKSSV GTVASNGLVR VLVVEDNSIL
RNLLVKWLTS KGYHCREAVD GQEGVNVFES GGQFDVVLVD LSMPVLDGIG ATTRMRDIES
ARLSREDMQQ NTLSHSKPAR ILALTGMSSL DDKRRAFDAG VDGYLVKPVA FKTLDVMFHK
LGIS
//
