ID A0A150VH31_9PEZI Unreviewed; 2382 AA.
AC A0A150VH31;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_21100 {ECO:0000313|EMBL:KYG49839.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49839.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49839.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49839.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG49839.1}.
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DR EMBL; JPDO01000015; KYG49839.1; -; Genomic_DNA.
DR STRING; 766039.A0A150VH31; -.
DR Proteomes; UP000075602; 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; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 55..368
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1878..2100
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2151..2274
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2317..2382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1834..1864
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 463..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2344..2366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2205
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2382 AA; 266064 MW; 49A5D307CBF849E0 CRC64;
MTVEKDGAKH GKQDTPQKDS DDHGPAWAKR CYARLSEELP EYEFIENFTP FHSSYDSWHF
LGRQRPRSAL EERKGSADSS RPASVHSRSE YEGSTDEEKE SDLWIVARLS THHLRLEREF
ILCQNLHSES DPESKHFVRP IKFGQLHARL PGDVHYSYSI VEAPGKNYLR ELVDFGANYY
WGSPQSPRVP VERVSLSKFL DFAIGAAQCL ELLHHGNEVV HGEIRGDAFH FQAETGMVKM
VSFGSGARSF EHGLTSAGWS SLMLERGVEH KLQYVAPEQT GRLSAEPDLR TDLYSTGVLY
WTMLTGRPAF EGKTPLDIMT NVLSRRIPLV SSIRPDIPDA LSHIIQKMTQ KNIEDRYHSS
SGVKHDLIEL KRILTNGDEE ALANFQVGTA DVSCFFKLPT HLVGRTNQRR FLMDVIETAA
QRSAHAAPIT RKGLYSLSSG ASMLSGDRVP DISTLDELMS ESTSSNGDRD RDRDSRLNSI
SEVAPYELMR TKQFSHESAD SMGTSSRDEG DQRQLDGLSS HGSRSINNVE SLPRSGSTFG
LGNTPSNDSG SLLRTAQKLK RNSRTEVIAI YGAAGFGKSA LIQSIVPQAR KVGYFASSKF
DQVRRSPFQP IIAVMSSLFR QIFAEHDLNT PFHENIRTFV RPSWGVLHST LELPAWLLNP
QGNVGDGRAS PPGNAVNSLP ASERKVCSLQ ATQEWIRAGG SNKTSRFMHI FIDVLRLVAI
QKFVCICLDD LQYADQESLE LLQLIVLQRI PIVLILTFRD AQPFQTSIRK ILDKAHKVEL
GPFTDEETTQ YVEDTLHRSR DYCLPLVAVI QEKTGGDPSF VREMVDTAYR RKCVYFCWKC
GKWEFQMDRL FEEFASPDDS KFSSNDFIIR RLKELPEDAQ SLLAWAALLG HTFSFSLVKK
VMSSDVLKVS SKELVPPTAK DPVAGLQAAI AKFVIMATDD DDRFQFSHDR LINAADSLLQ
PRWLREEMHY VLACAMMELQ PYDPATMPST ILFEQARHIC DCISTIKHRA KRKEPFRDLL
YQAAETARET GARKIGLFYF KNCLDLLSSD PWNDEDDDAS YGETLTLMTR AAENFWFCGD
LKESSRLLSE ILTNARDGID KVPARIISSR MHVQDGDNRA AFVPLYSAIM ELGVQLKQET
SWEECDAEFE RLLPMIQAKP FDSEAAQQDI SRRVSTLGAL FIELLSAAFW HDALLFYHIT
LKLMELYLQE GIFPHVGIGL VHLGTIAVGR FNLLQPGLTF GTWAMKVFDT YEREYYTIGR
GLTLYSCFLG HLQIEMRDNF QALNRGLEAA GVAGDKILYL LNMSFSAAFR IWCSEDLAET
EAFVASIAEE VPDWQESVRG GAILLAVRQF SRALQGKTFA RSSAIDVMSD DHHSTYEYEK
SVASRASNAT QALSAYNALK LELLFNFGYY KEALMLGERL LLTIGDNFSL RFVYSTYFYM
ALSVLASIRE DPQGKDIDQL LLKVSEYRAR IDLAGKVNPI NYTMLTALLD AEIADITMQY
GSVLQHYETA INHSVLHGFV LEEALGLELY GDWLVRRGAS RPARGVVLDA ISAYRRISAF
GKADHVAERH EFLLHGTRSL SAQDAGTQTM NTEGIHSAYN LDKMESHAHA QTASDRTQEW
LEPHLIKGTQ LMKETPATLS GGFSAVGLDM IDLASILESS QLLSSELDVD RLLSKLTEII
VDSTGADLCG IVVEEDGGGW CVAAIGSQEE TSPPPAAIPL DQIDDQVVKQ VTMYVLRFKE
QVFLRQVLDD DRFANVPASW LEKNPDGASM IALPILHGDN VLLGSLYCQA SPNTFTERTV
TLLKLLVNQI AISIANALLF KQVEKVSAGN ASMLEVQKQA LAQAREAEKK AKAAEAKAME
MVRLKDEAAK AKSMFLANVS HELRTPLNGV IGMSELLKGT PLSKEQEEHA DSIRVCADTL
LNIINDILDF SKLEAGKMQV FSVPLSLTET IREVVRALSY TNLERNLRTV EELEFDPHLI
VMGDPMRLHQ ILMNLMSNAY KFTSKGSVTV RAKVDWEDEN FIQVTVSVID TGIGISEEQQ
KKLFLPFSQA DSSTARSYGG TGLGLSICKA IIENVMKGRI WMESLPEVGT TVSFSLPFKK
VKASANGDKN GLAVHGHGRE ADPMAIFTPP EEESGQRPIF SLVNVPREEL KVCIAEDNPI
NQKIAINFVK KLGFNCEAFS DGQQTLDALA RASKDGKPFH LVLMDVQMPV LDGYNATRAI
RKHADPKVRD ILVIAMTASA IRGDREKCLE AGMNNYLAKP VRADTLKQML ESYLNQPTRI
IPNLQQEADK LVNTVVSEID QEENNGKQVQ YNNSVALASQ SSPERPKSAR GEGTAIQLKP
EEMAQETHNI TVSRQLKQSM STRPLARRQG GNRLDDTKEC ER
//
