ID A0A2J5I8F7_9EURO Unreviewed; 1344 AA.
AC A0A2J5I8F7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BDW42DRAFT_92369 {ECO:0000313|EMBL:PLN86283.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN86283.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; KZ559499; PLN86283.1; -; Genomic_DNA.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000235023; 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 Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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, ECO:0000313|EMBL:PLN86283.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 239..294
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 334..386
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 426..478
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 518..570
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 610..662
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 702..754
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 776..1001
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1154..1273
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 19..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1203
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1344 AA; 147692 MW; 140C418B2949AAC5 CRC64;
MAGADETLAA ATALLQGLAR DVPGSGPSPP FDFHFPQSTT NGYNSKPPKL PGDHSPAKAA
FENELEALIR RVHHLEFQSV SHQPSPGHPL GLAQSALCPS TRETEFLCSF GLSRSTSREG
SNASSILQQQ NPNHSARPRR PSADPHDPEP EEEVDDEDSD EDDELEPGTR LVREEDISYL
RNHVQKLAEE ISYQKDIIAQ VRDELKQQEE QTRRALTKVE NEDVVLLERE LRKHQQANEA
FQKALREIGG IITQVANGDL SMKVQIHPLE MDPEIATFKR TINTMMDQLQ VFGSEVSRVA
REVGTEGILG GQAQITGVHG IWKELTENVN IMAKNLTDQV REIAAVTTAV AHGDLSQKIE
SRAQGEILEL QQTINTMVDQ LRTFATEVTR VARDVGTEGV LGGQAQIEGV QGMWNELTVN
VNAMANNLTT QVRDIATVTK AVAKGDLTQK VQANCKGEIA ELKNIINSMV DQLRQFAQEV
TKIAKEVGTD GVLGGQATVN DVEGTWKDLT ENVNRMANNL TTQVREIADV TTAVAKGDLT
KKVTANVQGE ILDLKSTING MVDRLNTFAF EVSKVAREVG TDGTLGGQAK VDNVEGKWKD
LTDNVNTMAQ NLTSQVRSIS DVTQAIAKGD LSKKIRVHAQ GEILTLKVTI NHMVDRLAKF
ATELKKVARD VGVDGKMGGQ ANVEGIAGTW KEITEDVNTM AENLTSQVRA FGEITDAATD
GDFTKLITVN ASGEMDELKR KINKMVSNLR DSIQRNTAAR EAAELANRTK SEFLANMSHE
IRTPMNGIIG MTQLTLDTDD LKPYTREMLN VVHNLANSLL TIIDDILDIS KIEANRMVIE
SIPFTVRGTV FNALKTLAVK ANEKFLSLTY QVDNTVPDYV IGDPFRLRQI ILNLVGNAIK
FTENGEVKLT IRKSDREQCA LNEYAFEFSV SDTGIGIEED KLDLIFDTFQ QADGSTTRRF
GGTGLGLSIS KRLVNLMGGD VWVTSEYGHG STFHFTCVVK LADQSLNVIA NQLLPYKNHR
VLFIDKGENA HQADNVMKML KEIDLVPLVV RNEDHVPPPE IQDPSGKESG HAYDVIIVDS
VATARLLRTF DDFKYVPIVL VCPLVCVSLK SALDLGISSY MTTPCQPIDL GNGMLPALEG
RSTPITTDHS RSFDILLAED NDVNQKLAVK ILEKHNHNVS VVGNGLEAFE AVKQRRYDVI
LMDVQMPVMG GFEATGKIRE YERESGLTRT PIIALTAHAM LGDREKCIQA QMDEYLSKPL
KQNQMMQTIL KCATLGGSLL EKSKESRISS SGEMHPVHTG DGKRPTMGMD TRSITATSTV
NRGSSSLTGP NVDKSDELAM ERVR
//
