ID A0A166LRK6_9PEZI Unreviewed; 1363 AA.
AC A0A166LRK6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Hsp90-like protein {ECO:0000313|EMBL:KZL63856.1};
GN ORFNames=CT0861_11006 {ECO:0000313|EMBL:KZL63856.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL63856.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL63856.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL63856.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL63856.1}.
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DR EMBL; LFIV01000310; KZL63856.1; -; Genomic_DNA.
DR STRING; 708197.A0A166LRK6; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000076552; 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; 3.
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; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 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; 3.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 855..1143
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1202..1350
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 119..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 683..710
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1275
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1363 AA; 152240 MW; 2AEE0B7AAA02D6AB CRC64;
MHPPPLLGVG VVDLLESDPR PSFVVAIPPS LKDPANAEVV YSNPALASKP ALYEVLVSIS
SRHHTRFWDW ITAQDANPSQ SFLYNNHFWT RNTVLSEWVV VSSNDFPVES EPPRKIRLDA
SGGREPGSGI LHPHTSTVSS MSSPESSEED ILSHPRIVRA TTEPPLVLPE FMPDQEPFLD
MVDSVDWSAT PLGPMDRWPS LLHHSYSQIL CNSQPTAIYW GNKLTTVYNE AYGEMIGARH
PNLMGRSVTE VFPEITDQLR DMMENPGQSR RANNEEVFRF FVDQRDGPPL ETYLKWSIVP
VMHNDECLGF IHLISDTTLY HLFRRRIQML VDMGEELGTA KDVKSYWSKL IKELSECDPA
YDIPLAMLYS IGCDGSSASG SEPRHECNYI CRLEGALGVP ENHPIMPGTL RLKDTDAGLA
PQFRAALRNQ EPLIINTSDG SLPKNLLTGL QWRGFGDPCK AAIILPIRPT KEEEVMGLLV
LGLNPRRPYD DAYTLYIQLL AQKLATSLAC TVLLEEERRR GRNAAEQAAY DHAMLKEKLA
HQTKEATEYT RLFQTVSDFI PNGFSIGDHQ GNITFANGLW YRITGYPDST AEDGGAFSCV
LEADREKIRE AYKELRTKDE VEFEFRVRGT EHTNNMLTRR SPFKADVYSD LDDKMERYVM
AQAKAERAMD GTIIRTFTCL TDVTAHKRTA DEATRRAQQA ENLKRMAELA TVGMFDMDTG
GRLLGANNVF FELCGINKVD PMEHEVRPWE VSVVKDDLPN LSESVTRLVS EKKPQTAEIR
LKTTWTAEDA GGNQITAPRW VNATLMPVCN SDGIVQSFTG CVSDVSLQKW QLELETQRTE
EAIDSKRQQD NFIDMTSHEM RNPLSAIVHC SDAIIASLAR CEELVSRPLS PMVLKTPDES
SDKHFDVKQL LSDSIENAET IVACAQHQKR IVDDILTMSK LDSKLLAVTP CTVDPVQIGE
EAIKMFDVEA RRVDIDLKMT VDKSYKELGH VYLDLDPSRV KQVLINLLTN ALKFTKSGSI
RNVSVCMKAS RERPTDETSP VTFIPRSCKE ESEYDQPALD GRRDPVYIMF EVKDTGQGLS
EDEKSNLFNR FVQASSRTHV KYGGSGLGLF ISRRLTELQK GAIGVASLPG VGSTFAFFIE
AYVPTEASRR EAESAAAAAR MATLATAAST PLTVPRVRAP TNEQRTPGSR PKPPSHDPRL
DGILVVEDNL INQQITRRGL QDRGFTVDVA NHGIEALERL MQSMSLQHQE EQEYFGQGTP
STQAPAVAIN LILMDIEMPV QDGLTCTRRI RELEREGRVL CASGGRIPII AVSANARPEQ
MQDAKNAGCD DVLVKPYRMP ELIEKMQVVV RRMGGLSPGS PMR
//
