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Database: UniProt
Entry: A0A1L9RKQ6_ASPWE
LinkDB: A0A1L9RKQ6_ASPWE
Original site: A0A1L9RKQ6_ASPWE 
ID   A0A1L9RKQ6_ASPWE        Unreviewed;      1320 AA.
AC   A0A1L9RKQ6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASPWEDRAFT_40694 {ECO:0000313|EMBL:OJJ35494.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ35494.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; KV878212; OJJ35494.1; -; Genomic_DNA.
DR   STRING; 1073089.A0A1L9RKQ6; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_40694; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000184383; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 5.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 3.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 3.
DR   Pfam; PF18947; HAMP_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 6.
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; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50885; HAMP; 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          191..246
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          286..338
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          378..430
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          470..522
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          562..614
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          654..706
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          728..953
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1106..1225
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          22..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1235..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          150..199
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        103..117
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1244..1277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1155
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1320 AA;  144960 MW;  0EEBB98313A441B7 CRC64;
     MAGADETLAA AAAILQGLAR EVPGIGSSSP PFDFQFSHPS ANGCETKHAK LPGQPSPAKA
     AFENELEALV RRVHHLEFQA QQNSHPPPRT KRTPSGSDGR GPEDEIDGDE TDEDEEADSG
     TRLVREEDIS YLRNHVQKQA EEISYQKDII AQVRDELQQQ EEHTRRALTK VENEDVVLLE
     RELRKHQQAN EAFQKALREI GGIITQVANG DLSMKVQIHP LEMDPEIATF KRTINTMMDQ
     LQVFGSEVSR VAREVGTEGI LGGQAQITGV HGIWKELTEN VNIMAKNLTD QVREIAAVTT
     AVAHGDLSQK IESRAQGEIL ELQQTINTMV DQLRTFATEV TRVARDVGTE GVLGGQAQIE
     GVQGMWNELT VNVNAMANNL TTQVRDIATV TKAVAKGDLT QKVQANCKGE IAELKNIINS
     MVDQLRQFAQ EVTKIAKEVG TDGVLGGQAT VNDVEGTWKD LTENVNRMAN NLTTQVREIA
     DVTTAVAKGD LTKKVTANVQ GEILDLKSTI NGMVDRLNTF AFEVSKVARE VGTDGTLGGQ
     AKVDNVEGKW KDLTDNVNTM AQNLTSQVRS ISDVTQAIAK GDLSKKIEVH AQGEILTLKV
     TINHMVDRLA KFATELKKVA RDVGVDGKMG GQANVEGIAG TWKEITEDVN TMAENLTSQV
     RAFGEITDAA TDGDFTKLIT VNASGEMDEL KRKINKMVSN LRDSIQRNTA AREAAELANR
     TKSEFLANMS HEIRTPMNGI IGMTQLTLDT DDLKPYTREM LNVVHNLANS LLTIIDDILD
     ISKIEANRMV IESIPFTVRG TVFNALKTLA VKANEKFLSL TYQVDNTVPD YVIGDPFRLR
     QIILNLVGNA IKFTEHGEVK LTICKSDREQ PAANEYAFEF SVSDTGIGIE EDKLDLIFDT
     FQQADGSTTR RFGGTGLGLS ISKRLVNLMG GDVWVTSEYG HGSTFHFTCV VKLADQSLSV
     IASQLVPYKN HRVLFIDKGE NGNQAPNVMK MLKQIELEPL VVRNEDHVPP PEIQDPSGKE
     SGHAYDVIIV DSVATARLLR TFDDFKYVPI VLVCPLVCVS LKSALDLGIS SYMTTPCQPI
     DLGNGMLPAL EGRSTPITTD HSRSFDILLA EDNDVNQKLA VKILQKHNHN VSVVGNGQEA
     VEAVKQCRYD VILMDVQMPI MGGFEATGKI REYERDNGLT RTPIIALTAH AMLGDREKCI
     QAQMDEYLSK PLKQNQMMQT ILKCATLGGS LLEKSKESRI SSSGEMHPVH QTGGSENKGQ
     QQQQQQQQQQ QQQLQLHRPG MEPRAITTSG PISRGSLASP NVEKDEDLSM ERALLRSNSS
//
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