ID R7YQH4_CONA1 Unreviewed; 1456 AA.
AC R7YQH4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_03395 {ECO:0000313|EMBL:EON64165.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON64165.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH767567; EON64165.1; -; Genomic_DNA.
DR RefSeq; XP_007779482.1; XM_007781292.1.
DR STRING; 1168221.R7YQH4; -.
DR GeneID; 19900706; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_5_1; -.
DR OMA; EIEKWFG; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
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; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 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; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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:UP000016924}.
FT DOMAIN 501..571
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 574..626
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 785..1008
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1098..1226
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1153
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1456 AA; 160537 MW; DA508DAF2F3122E8 CRC64;
MRPLAQPPAG SGSSLNHHDD LASLHTPSPA YTSDVSEEDG YFSVRSRGNR SPASVRSQHL
SVKMPPSPTT TAIALTALEY LPMPLLVLSS QKTVVLANEA MGRLLGLEVN AIVEDEDRGP
TAVLSVTDLL CDYSMSQLGI DVLQNGSPIW VNWDDFLNSI LEQITQSAGG ASSDNIESLR
EDNDGSTPTV TPRGQRPPHT PISQSLPRLS SSNLVKTTVH DVKVDVLISP QSDSLFRPAP
AADKAAPLPE PISASMIVST WTLEGKQFFT LTFTSATPHA TANSQPSSRT VLRTSTGFRR
SPGSANSSSS SSGRRSAISS APTTSGALAV TSPLLEPAPR LPHGPASRTK SSSAPSIFHK
ASRMKDAVLN SMNMPSYAMW KDRSFGIPNK AFLRLMPDNE NYVFNSTNQH EFLAQYTFYT
EDFQRLMDVD ELPIIELCRT QKRVEGKRVG MRHPKTDARL TYDVSGEPVV DEATGEFLGG
IVVMKDVTEY TKRIAAQIEE NERQFEYIAN LIPIMVWTTT PSGQHDWFSQ RWYDYTGLTE
EKSLGQGWQL PFHPEDMPAT SERWNHSLQT GDEYITEYRC QRHDGEWRWM LGRAVPFLDE
DGKIIKWFGT CSDIHDLVIA RDEAKQVKEQ LQRVVEHAQT TLWAVDKERK LIVLEGSLMW
QSSDEDISKK SIGLNVYDVF GQHQGAEYMP PLRKAVEATL ERKASDEIVE MHIDGNGRHY
RTRIVPLLRN SRNGGVEGES YVDGVIGISM DEEEVKEQER ENAKLTANAV AAKAASKMKS
QFLANMSHEI RTPIAGVIGM SELLLDMPLD QEARDCAENI QRSANGLLTV INDILDLSKV
ESGRLDVEEV QFSLSVVIRD VNKMMSFAAE RKGLTYESFI QPEIERDIKV MGDPGRVRQI
LTNLLTNSIK FTSEGSVKLS VSIIGVTTDI VKVNFEVEDT GIGIEEDVRK RLFKPFSQAD
SSTARRFGGT GLGLTISKNL VQLMRGEINL ESKLGTGTKA TFWIPFNKAQ YNDQGSPTLL
DLSSIPDRLQ SDVSVSYGSS DEHGHGRVTP PQTPTGYNGG ARHARGHSGS LPPGTPSITH
NLPDHMMNLT EEERSKIHVL VVEDNHINQQ IALKTIKKLG FSVSAVWNGK EVLDYLLAKP
SGDRPNPDII LMDVQMPIMD GYLATHTIRT QEPFKDSASI RSTPIIAMTA SAIQGDREKC
QEAGMDDYLA KPVKGKHLEK MLVKWAIQRK INQIEEKRRN GSPPDPEQQA QQPNGAPNQR
SQSTEANAND PFDSHDTLRT ISASNSSSTV TSTPLTTNAV GRPGPGPLQE TQPSRSSLRA
DRASELSAAL GRLDYTNRAA LSKSAESDAD RVLRRVNDEE KASSLRDDRL MASGEDPRSA
RTGTERKRDR GEKKEREGGP SHMLTTENMQ RFGVEQDKKA GEMRAVGSSG KGSVGTSAAP
YLRTESVDRK PDEGQK
//
