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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//