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Database: UniProt
Entry: A0A094EF78_9PEZI
LinkDB: A0A094EF78_9PEZI
Original site: A0A094EF78_9PEZI 
ID   A0A094EF78_9PEZI        Unreviewed;      1373 AA.
AC   A0A094EF78;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=V498_09374 {ECO:0000313|EMBL:KFY77326.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY77326.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY77326.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY77326.1}.
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DR   EMBL; JPKA01004081; KFY77326.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000445_3_2_1; -.
DR   Proteomes; UP000029270; 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; 2.
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}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          199..254
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          294..346
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          386..438
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          478..530
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          570..622
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          662..714
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          736..960
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1110..1229
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          74..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1236..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1351..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          162..207
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        85..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1159
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1373 AA;  149155 MW;  B69D139616D4A1BC CRC64;
     MTDDAALAAA TAYIQSLATS PTGLSALKAS RKDADTNGVE EIHLPGSSTP AKHALERELT
     SLAKRVRFLE SNAAAPKDHL VPDTPNDSVD SSPADDSIPT ASTSAAREKI VSTLLASRES
     PAGQSTVTYT KLSSEQLEAL REHVDHQSGQ LESQKLELAS VNAQLLRQKQ LQEKALKAVE
     VERVNALERE LKKHQQANEA FQKALREIGE IVTAVARGDL SKKVQIHSVE MDPEITTFKR
     TINTMMDQLQ VFSSEVSRVA REVGTEGILG GQAQISGVDG TWKELTKNVN VMAQNLTDQV
     REIAAVTTAV AHGDLTQKIE RPAQGEILQL QQTINTMVDQ LRTFAAEVTR VARDVGTEGI
     LGGQAEIEGV KGMWNTLTVN VNAMANNLTT QVRDIAMVTT AVAKGDLTQK VQAECKGEIF
     ELKSTINSMV DQLQQFAREV TKIAREVGTE GRLGGQATVH DVEGTWRDLT ENVNGMAMNL
     TTQVREIAKV TTAVAKGDLT EKIGVEVRGE ILDLKITINT MVDKLSIFAF EVSKVAREVG
     TDGTLGGQAK VENVEGKWKD LTENVNTMAS NLTSQVRGIS TVTQAIANGD MSQKIEVEAA
     GEILVLRETI NNMVDRLSIF SNEIQRVAKD VGVDGKMGGQ ADVAGIGGRW KEITTDVNTM
     AMNLTAQVRA FGDITNAATD GDFTKLITVE ASGEMDELKR KINQMVFNLR ESIQRNTAAR
     EAAEMANRTK SEFLANMSHE IRTPMNGIIG MTQLTLDTDL TQYQREMLNI VHNLANSLLT
     IIDDILDLSK IEANRMVMEE IPYSVRSIVF NALKTLAVKA NEKFLDLTYR VDSSVPDHVV
     GDSFRLRQVI LNLVGNAIKF TENGEVSLTI RKADQDNCAG NEYAIEFSVS DTGIGIQNDK
     LDLIFDTFQQ ADGSMTRKFG GTGLGLSISK RLVNLMRGDV WVKSTYGKGS SFFFTCTVRL
     ATSDISFIEK ALKPYQGHQV LFIDKGETGH GKEISSMLSE IGLEPVVVES DSHSDLMQAG
     RPANHPSNYD VVIVDSIETG RRLRSIDEFK YIPIVLLAPV VHVSLKSALD LGITSYMTTP
     CQTIDLGNGM IPALENRAMP SLADNTKSFD ILLAEDNVVN QRLAVKILEK YHHVVTVVGN
     GLEALEAIKL KRYDCILMDV QMPIMGGFEA TAKIREYEYN IGTTRTPIIA LTAHAMLGDR
     EKCIQAQMDE YLSKPLKQNH LIQTILKCAT LGGQLLEKGR EPRQSTKEEK PTKIGPPVKA
     PQPLSPLSPA AKKRAEIKSG GKGNIPLENG RSSSSLARTA AVTSMGSPSR ASPSPGSALG
     ESRSPAKEGE NPLARVSSVV VPVVPVVAAA ASDRRRRETD AAAEAVAKKR KVG
//
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