ID A0A0F8A3H0_9HYPO Unreviewed; 1219 AA.
AC A0A0F8A3H0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HIM_08785 {ECO:0000313|EMBL:KJZ71814.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ71814.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ71814.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ71814.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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; KQ030560; KJZ71814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8A3H0; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000054481; 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; 4.
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; SSF158472; HAMP domain-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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KJZ71814.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 185..240
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 280..332
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 372..424
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 464..516
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 556..608
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 648..700
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 722..946
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1096..1215
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1145
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1219 AA; 133781 MW; 22382FFF0FEFAED5 CRC64;
MIDDAILVAA ADVVASLAAG YTMSVLPAEC VGRKVALPGR ETQAKRRLEV ELQGLVLRIS
HLEDMASRTT LSAPRHTPNK LNYGLFGFNC DPHYPAYSEL TLNRTGVEDI SIGDPPAKRR
RSEQHLGTLQ NHASHESELF HSQHQEFLSP KAQLLTQTQT QHDIYEQDSV ATLQKELLKH
QKANEAFQKA LREIGQIITA VARGDLTMKV HMNAEELDPE IHTFKRTINA MMDKLQIFAS
EVSRVAREVG TEGLLGGQAI IDGVDGTWKE LTDNVNVMAQ NLTDQVREIA SVTTAVAHGD
LTKKIERPAR GEILELQQTI NTMVGQLRTF ASEVTRVARD VGTEGILGGQ ADVAGVQGMW
NDLTVNVNAM ADNLTTQVRD IIKVTTAVAK GDLTQKVQVD CSGEIYDLKS TINSMVDQLQ
QFAREVTKIA KEVGTEGRLG GQATVHDVQG TWRNLTENVN YMAMNLTTQV REIAKVTTAV
ARGDLAKKIS VEAKGEILEL KNTINQMVDR LGTFASEVSK VAREVGTEGT LGGQAQVSNL
EGKWKDLTEN VNTMASNLTV QVRSISTVTQ AIANGDMSQT IEVQANGEIQ VLKETINNMV
GRLSSFCYEV QRVAKDVGLG GKMGAQADVV GLDGRWKEIT TDVNTMANNL TTQVRAFSDI
TNLATDGDFS KLVDVEASGE MDELKRKINQ MISNLRDSIQ RNTQARAAAE LANRTKSEFL
ANMSHEIRTP MNGIIGMTQL ALDTDLTQYQ REMLNIVKSL ASSLLTIIDD ILDLSKIEAR
RMVLEEIPYT LRGTVFNALK TLAVKANEKY LDLTFKVDSS VPDYVVGDSF RLRQIIMNLV
GNAIKFTEHG QVSLTIKEGS RLPQNPGEYA LEFEVGDTGI GIAEDKLDHI FGTFQQADGS
MTRKFGGTGL GLSISKRLVN LMGGDISVSS EAGKGSQFCF TCKVKLASGG TEFIQKQLQP
YHGHRVLFID RALPNIGTEI EEMLEQLGLR PVTFNLEDLS GQAQVGLYSS LPEDCDAILV
NSIDTARRFR ALDEFKDLPV VLLAPVVHVN LKTCLELGIT SYMTTPCQLV DLGASMIPAL
ENRATPVITE NTRTLKILLA EDNTINQRLA VKILQKYNHS VTVAGNGLEA VEAVKERKFD
VILMDIQMPI MGGFEATAMI RDYDRSTGAC KTPIIALTAH AMIGDREKCM QGQMDEYLSK
PLQQNQLLET ILGCVRLSE
//
