ID A0A165K0L1_EXIGL Unreviewed; 2277 AA.
AC A0A165K0L1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EXIGLDRAFT_735021 {ECO:0000313|EMBL:KZV95615.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95615.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV95615.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95615.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV425954; KZV95615.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165K0L1; -.
DR InParanoid; A0A165K0L1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZV95615.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..344
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1729..1953
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2146..2269
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 409..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2198
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2277 AA; 250958 MW; BA591BDB15C3E9F5 CRC64;
MPVASASNTY FKDDVLNVPG YRFGKASPWR DTGSATLLAE GVNLKDGSRV LAKIASAHSN
GSLCLERELH VHSRMAALPE AANTTIKLLE TLTLPPHAGD CVVLILMHPG YNALSRFFPA
EKMNDLLLAG TSPRPPNDDS MLLDTPPVGE SKQLADSESW DAMDIASFLE FAIEAARCLE
VMHKAGLVHR EVRANAFHLS SFSGVVRLVH FGNRSQSLEQ LGGPSALVLK SATDAMDEVE
KQRVKEALCY LAPEQTGSVE TIYEDHRTDL YSLGIVFWML LVGHIPFDGG PMELLHSIVQ
KRPLIVHEAR RDVPLVVALI IDKLLSKSAD KRYNSAFGLK ADLLECQKRL NLSCATPDLS
LELIPIFDIA QQDKFMDFII PSGLFGREAE IEQIGAVIRQ ASTSHSRYLA ASRPTGASSS
SAQDDISHSG SGKSPDIGRQ DTPMSPESLG VGVADYTSSS TTPSHERSLR HDRRDGPKVR
AVVVYGPAGI GKSSLISWYQ ANWRRHGLWG HAKFQDDDST PFAGILACLS SVLRQLMAFQ
SDLHRFTSIL QTRLGPQVHN LPLLFHGAPE LRDVLTLFDI NVAGIDGQLS TEELRVRFQS
LVVNVFCVLS EVRMLALFLD DLHVADQSSV DLITSLAGSR SNILILASFR SETQTAMTRI
NSIFASTPQT VWIPLHPLTQ DALSALVSRT LHRNDEDVAA LTGFLHRISR GNAFSARNML
ITLQRAGYIK FSWEHNYWHY DIAAIENSFV AREWVSNPGD VSFLLAHIQD LPDEARKYLL
WASMFGTVFK VQEIAFVMDR EDADHDPDID GPWGPAPAVP PSIRSGKPSV RGLHLATSEG
WLVQRARDMC SWTHDRYRQA ALESLAMLPP STLEKMSLRI VLMLMQESEP DTYRIAEHCR
RCLTLVSAHP RRDDALRYLL DAAFAASTRG ALEVALQSFC SAKVLLGENA WEVDHAKTFG
IYLKIAELLT WKGDVDASDE MLKQILGHIV EHEDQAKVWR AFSRNSFFRK DFDSAVKNIV
IALRILGVEL NPAVTMRETD EMFESCKGKI LAAGNEQILS APRCTDPKVD LSVALLNDAG
TAAYWAGAPA FMTSVGLTII ELAFRSGLCP GTALGFFWIL GAAAEDRELF RFSVDIARLG
LRIAANHGSS FEKSRAETYY CAMVSGFDNV HLRANIGRCE MAFKLAEAAG DRIYAGFARI
YQICTHIYVC DDLSEVLAVT EDVMKDGAMW GEGSDVSTLA KGLAACVRAL AGQTEATSAA
TVMDTPFWKE REYFEQLHSY GGNVALILNW YNSFKMAVLF GLGFFEEAAA LGYEVFHARH
LHPNHRHSRY ALFWHSLALI QCCRMPRTND KQREAYLEQV ELNQSYIRKW VSPSPVNTGT
WVAIVDAEVA ALSESADAYR LYDVAVRLAI NNDWLMEEGW ALFLQGSHFV RNGVEGLGRE
LQRRAISRQA QWNANGVVNF MSSTLRADLH APLKKNIFSV EIGVQTEVEE EEEAALHRST
IVPTYPTFEQ TTDSVAELDA DDLRAILKWS QIISSDVNLS VCLQRLTEIA ADSCKAQFAS
VVMRTDEGDY SVATSMVAPQ PCTVYENMTS VRSIPDPLRR AVIQHTLNVQ EPLFIPDVSQ
EPRFASEALR SSAHSILCVP MMSNRGQTFG VIFLSSRIAF TLHDSRLLGL LVSQAGISIS
NALLFRSLQQ ATKANLKMIS TQKSALEETR KSREDALKAT KIKSNFLASM SHELRTPFSS
FYGLLDILGE TPLDASQREI VATAKQSCEL LLKIIDSILD YSKLEASALK LEISPFAVED
MIADCMELLL PLAAQKLEMA YNVDPGVPRW ISADYARIRQ VLMNLLGNAL KFTEKGTVTV
TLSIDTEMSA TRPDVLFLKC VVEDTGIGLT DPQMDVLFQP FQQADNSSTR RFGGTGLGLS
ISMQLCKLMG GDIGVSSNAG VGSTFFFRIP VTVAETPASI KAGAELASLR SKLAHPTQVR
VLLCSPSQAT LALLESMLSG LFVAKTASVE EAEAWIRNPS IVALDFAIVD HPDELRVQDL
LRILQASPAH SKAKIIHLFT PTASAARSQH IRWSPTPEPP PQTSPGTAQI SLGNIVRLSK
PPRTMRLLVI LASLKDMLPD MSLMPISEVH APVEDPNGLQ RTLYGNVLIA EDNDVARQLL
VKQLTRYKLT VTATSNGKEA VTAWQAHEPG YFSVALFDHH MPVMDGVEAT KQVRLLEARN
KVPVQLPIVA LSADCQESTK ALCLSAGMNG FLAKPLKRND LTSLLSMFWT LVQPAAG
//
