ID A0A0K6G6S0_9AGAM Unreviewed; 1684 AA.
AC A0A0K6G6S0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CUA74317.1};
GN ORFNames=RSOLAG22IIIB_11141 {ECO:0000313|EMBL:CUA74317.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA74317.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA74317.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA74317.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYGV01001432; CUA74317.1; -; Genomic_DNA.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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:UP000044841}.
FT DOMAIN 645..865
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 924..1038
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1054..1123
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1210..1490
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1544..1677
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 163..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1159..1195
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1507..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 972
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1606
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1684 AA; 187958 MW; 4FB0744CBCDD2C22 CRC64;
MLASRELLQH ASLISFLDAY PEPAFILCTN ALPHSSLEFM YGNQALHAIL FGHDDTAILD
DQSFFSALTS DQDVFWLADP LGSHSPITPL TPRSSVGDSH TITIRPDWLP RDHTPLDLEL
TPTLIDLPVI IPGVGSTTHS YVFTASPRKV PMNLYLLRSE THTDQRRDPG LRLSDFPPPP
ASVGTHVRSR KSKSESTSWL SQPQPPMNLV ELPSRMIETY PWEKTAIGPK ESWPMTLKVM
VKYLMEKPVP STIFWGWPEQ VMIYNDTYAQ MLGSKHPISF GKEGKVAWGE LWEMLTPVSE
QCRRGKSTRK NDDQLFFNSL TELHLPEEVY HTWHWTPIWQ EDGTVGGVLN STLETTQKVI
TERRLSGMSE LFARMSDART QEQFGERTLE VLSRNPLDLP FVAMYWCEVE STPTAPTSTK
HKGPALASTY LRHHTDTLIN VKLTLAGSIG IPDGHPIARH TVKYTLDPVT YQPVHMLPEP
ESLESPATSD ATPRIPIAGS PLGSTVSTIQ LPPTSPVKGM EPGIDLARIF VSGSIEVIDP
LPSQLAQGLD GRGFKDVPRA AALLPIHTYM SSNRGHHDGR LLPACVLVLG LNTRRAYDAD
YASWLESVGA SLSNQFTVVL QREADMKLIE EQERIDKAKT MFFTNVSHEL RTPLTLIQAP
LEQLASSDGL NRDTQYRIQL AMRNCKRLKK LVDSIMDMSK LEAGRLVGNF RPVQLGRITE
DLAALFRSMA EKKGIDYHIS CDTDNEPIVY VDIDLWEKII CNLLSNAFKY TSKGRIGINV
VHDEMASHVH VSDTGVGIPK DHLGEVFERF FRVNNNAAEG TGVGLSLTKE LVSFHGGHMG
LSSQTEEEAP GQSGSIFTVT LPHGCAHLPV AFIHEVAPHA NGVSQRQMEY WMELEQPTPS
SIASASDEGE SATSSTLFFE KDDVILVVDD NSDMRAYIRK IFTPYLTVVE GSNGTEALKI
ATSQKVNLLL CDVMMPGMDG PELLRRLREE RKTKLLPVIF VTASDDVNLL DGQADGVVDC
ISKPFRVRDM LARVHLQLQL GKRRVRLEED FEVRSHELQV LTDLSPVGIF RAEANGKLMY
VNPAWHQITG FPSERDRDEW IDHVHPSSRE EMIRMWKACF EREKSSSARI QWMSGCWTHM
AISPLVSPDN VMLGAFGAIT DINEQHRAEE TRIALAEERE QVAASRAEDA EAQRQVEIER
RRAQELLIDV TSHELRQPVS AIIQNAEVVR TNMKGFRNLL HDCRKRNISY TPTDRMLAEL
EDDLQAMDSI TQCGLAQARI ANDVLSLSRI QLNVLSIIPT EFDIKQETTQ ILMVFRNELM
SKNIQFSLDL GRGADVYGLH TISTDRSRYA QIITNLMSNA IRFTDMSTEL REIKVSLELS
PDPPADESCA PPPLHGGRPL LNGRADSEPG DAPVFIYVSV KDSGPGLHKE DLALLFQRFQ
QGSNAHHVFG GSGLGLFVCR QLCNLMGGKI EVVSNLGEGA MFRFFIRANA ALGRIPRPPR
PVGLRTKRSS SVHSRGSGVS KSSVRSGHRP LPETPNLQNN RPLHVLITED NKINQTVLAR
QMKRAGFTYA LASNGLEAIQ AIDKADCQEE IQNDPSFQKF DVVLMDLEMP VLDGFAATRE
IRRREATGNL KTRSFIIALT GNARLEQVQS ARDAGVDDVM IKPYQIDKLI SKMRAGYQVK
TDTD
//
