ID A0A2S6BR20_9PEZI Unreviewed; 1307 AA.
AC A0A2S6BR20;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CBER1_04660 {ECO:0000313|EMBL:PPJ49900.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ49900.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ49900.1}.
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DR EMBL; PNEN01001796; PPJ49900.1; -; Genomic_DNA.
DR STRING; 357750.A0A2S6BR20; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000237631; 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; -; 3.
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; 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; 3.
DR Pfam; PF18947; HAMP_2; 2.
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; 6.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 203..258
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 390..442
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 482..534
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 574..626
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 666..718
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 740..964
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1109..1228
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 79..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1158
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1307 AA; 143038 MW; 60AF838DC825CB6A CRC64;
MPHEETSAAV ASILSNFAKQ YTPLDAESFP ASAIANGIKS NKITLPGDDT IEKRTLEREL
TNLATRIQFL EARAHSGVSS LPITPNEPLS SAFPSQDASS PKASALNPLN PRQRSASWVN
SLLTKNEGEP HTRQLTEEQF TVLREHIDQQ AQEIKTQKEF IDGIKAQLTH QQTATRAALD
TLGNSQSIEQ LKREIEKNAQ INATYQKVLR EIGTIITAVA NGDLSKKVLI HATEKDPEIA
RFKHTINQMV DQLQEFASQV TSLAKQVGTE GRLGGQAVVP GVAGIWSELT QNVNVMAQNL
TDQVREIAVV TTAVAQGDLS RMIQRPAKGE IYQLQQTINA MVGQLRTFAT EVTRVARDVG
TEGILGGQAQ IEGVQGMWHD LTINVNAMAN NLTAQVRDIA EVTTAVAKGD LTQQVKAQCK
GEILALKTTI NSMVHQLRQF SAEVTNLARE VGTEGRLGGQ ATVHGVEGTW KDLTENVNGM
AMNLTTQVRE IAEVTTAVAQ GDLTKKVQAE VQGEILALKN TINTMVDRLG TFATQVSRVA
KEVGTEGVLG GQARVENVEG EWKTLTDNVN TMANNLTGQV RSISDVTQAI ARGDMSQRIK
VHAQGEIQTL KDTINDMVTR LDAWSLAVKR VARDVGVDGK MGGQAEVEGI TGRWKEITTD
VNIMAQNLTS QVRAFADITH AAMKGDFTKM INVEASGEMN ELKNKINKMV LNLRESIQKN
NQAREAAELA NKTKSEFLAN MSHEIRTPMN GIIGMTQLTL DTELEQNQRD MLNIVFSLAN
SLLTIIDDIL DISKIEANRM ILEEEPFSLR GLVFNSLKSL AVRANEKDIS LIYDTDASVP
DYIVGDSFRL RQIILNLAGN AIKFTEHGEV RVKIFSDTSV ECAEDEVVVK FAVADTGIGI
HSDKLDLIFD TFQQADGSTT RKFGGTGLGL SISRRLVTLM RGKMWVESTY GAGSTFFFTC
VVRRGDPDVH RVMPQLQQYR KHNVLFVDNG FIDNSEQVAA STKALDLVPC VVGNGRTPPS
ELSPEDQYDC VIVDNTDTAQ KLRSLERFKY IPIVMLAPAI SVNFKTALEN GISSYMTTPC
LPIDLGNALV PALEGRAAPI SADHTRTFDI LLAEDNAVNQ KLAVKILTKH NHKVTVANNG
LEAFEAIKKK RFDVVLMDVQ MPIMGGFEAT ANIREYEKQH ELARSPIVAL TAHAMLGDRE
KCIQAQMDEY LSKPLKPNQL IQTILKCATL GGALLERKSD NRSSILSEDA TSDASPDHNR
LMTPKRPGMT PRGQTDNGPA GLESPAIVTV DQEDPLARET LLRANSS
//
