ID A0A2S6CFA6_9PEZI Unreviewed; 1171 AA.
AC A0A2S6CFA6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_11397 {ECO:0000313|EMBL:PPJ58415.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ58415.1, 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 -!- 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:PPJ58415.1}.
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DR EMBL; PNEN01000459; PPJ58415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CFA6; -.
DR STRING; 357750.A0A2S6CFA6; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000237631; 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; 2.
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; IPR000014; PAS.
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; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 513..587
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 668..940
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1039..1166
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 969..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1095
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1171 AA; 130166 MW; CA8EE2B308AF430A CRC64;
MDTANEVPAN LRAVAAFLSL DESPTTIVTH LTRDEQPSER DWRVVYSNPA FQKLPDVAHQ
LDDICHSLNR SLPVNQPLIA LHGQVLDGGS WQTRVSEDYC IVIAKARDEQ VPATVKDGIS
HTSKATDLNW IQSDRPGLSP WRKLFCGHDW ASTSLGPMSS WSEVLRLYVL SMMSNPQPRL
LVWGADMALI YNEQVVPLLG AKHPSCLGQN VKHAFAESWS EILPVVEAAY DGEVKSVNCF
PLPILRHGFL EECYFSFTAL PVVDRDGRSC GMLSELTEST TLVTAERRRY TVNQLGTQLN
KLNDLAELWP VVLAQMDAAE LDVPYAILYT VNTEVTKTVA SETTSIDSRA VLPKHAQLVG
TVGVSEDHPG VLKSFPLSDT KAEGRDIWQA CNEAWSSGEM VVLSSENETL PPALAIAVPH
RGFGDQVKTA TISPIKAMAG SEPLAILVWG LNPRSVFGGE YQIFRSVFVD ILAKAAALIQ
LPHEQQRAQK IAEDVNHALA QQLRLTTLKA ERSEARFKRL ADVSPTGMFL FDASGLPLYA
NEQCLEMLRI TEAEYLAIRD SDGLAQRVHE EDVDEYREVW TTMTEKKMPI TAEFRLRPSL
QANKQNGTES DTWLSVTAFP EIESDGTVSS MQGWLTDISH RKFNEELLAQ RLEDALENKR
QTENFMDMHS HEIRNPLSAI LQSADSIETL LSSIKLPLHD ENMVVPTHVG EDIMDAVQTI
ILCAQHQKRI VDDILTLSKL DASLLVMSPD KVQVPSLVTK ALKMYEAEIG RAGIDAQLCI
EPTYDELDVN WVVLDSSRLL QVIINLLTNS IKFTQYSEER KIKICIGASY QKPTGKHHGI
SFIEPQQIRT SRSPVQEWPG GEDLYLQFAV YDTGRGLSED EMKLLFQRFR QASPKTYKQY
GGSGLGLYIS RELCELQGGQ IGVSCGDGRT VFTFFVKAKR WVPSEEEDIA ALPVPVRYAS
ASSSPVVYSK GGSTTLNDEA DQLGTPREEN GNMIENFHPR QQPFARQQSF GAANQMPVFY
TSQVKTRKDS SDSTQKALHV LIVEDNLINQ KVMSQQLRRA GCTVHVANHG IECLNFLESS
TYCSSTTPLS VVLLDLEMPE MDGLTCIREI RRREAIGSIV SHVPVIAVTA NARSEQINNA
IEAGMDQVVT KPFRIPELVP QMERLVAEVG G
//