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Database: UniProt
Entry: A0A1L9VNR0_ASPGL
LinkDB: A0A1L9VNR0_ASPGL
Original site: A0A1L9VNR0_ASPGL 
ID   A0A1L9VNR0_ASPGL        Unreviewed;       672 AA.
AC   A0A1L9VNR0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPGLDRAFT_45509 {ECO:0000313|EMBL:OJJ85532.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ85532.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878894; OJJ85532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VNR0; -.
DR   STRING; 1160497.A0A1L9VNR0; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_45509; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000184300; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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; 1.
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; 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:SF60; HISTIDINE KINASE G2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          169..436
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          550..668
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         599
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   672 AA;  74713 MW;  CE18195CD9D0204E CRC64;
     MDDSTGDAGS SVTKDIDNTS LQTNESVKQL ADTLPAGLAI INHKGEPVFI NGRFQNPHFY
     GSKKYFDSLS QSIHQDDCDR VESAYQEALR SKSELRIQYR ARNQPDCWQL LLLNPLGHED
     VQYPDLHNHG GFTCTVVDIT AEKTAEIEQA KSAQEAQEHK EKQERFIDMI SHEIRNPLSA
     ILHCTEDIID AVKGKKAHQV QTEDIIQAAE IINLCILHQK KVVDDVLLFS KLDASMLTLS
     PRIVLPRAEI PISLKMFQPE LRNQDIQFEY RLDPSYIDHG IDWVRADLTR ISQVIINLFS
     NAIKFTAKTK GTKRIALCMG ASLERPPSYP PNIVFFQSDE AALRLDATSG PEWGTGEPAY
     IMVAVSDNGI GISTENQKRL FERFNQATPK TGVDYGGSGL GLNVCRKLCH LHGGEIGVSS
     KEGDGSTFGF FFKVLRSSRA SHDEKVSQEG ESAMDKLCNR FESLGHEDQE ANSDSDSKFE
     ISDKPIVTPS SEVMPSAADD ERTQNTAKIV GTDDSWDAKR QKAADGDLSN GDKPETESPG
     PSQGETEKTR ILLVEDNIIN QRIISRKLKS LGFEVSEAND GHEALEAAQT GRFNCILMDK
     EMPVMDGNAA TRAIRQSEHR SIASVPVIGI TANVRPEQEN EMKQAGMDCV IHKPYRMEEL
     VERINQATRK EA
//
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