ID A0A1Y1XZN5_9FUNG Unreviewed; 2083 AA.
AC A0A1Y1XZN5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=K493DRAFT_264816 {ECO:0000313|EMBL:ORX91201.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX91201.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX91201.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX91201.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX91201.1}.
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DR EMBL; MCFE01000337; ORX91201.1; -; Genomic_DNA.
DR STRING; 1314790.A0A1Y1XZN5; -.
DR InParanoid; A0A1Y1XZN5; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00130; PAS; 2.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; 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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000193498}.
FT DOMAIN 1297..1367
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1370..1421
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1422..1492
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1495..1547
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1551..1774
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1955..2077
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1925..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2006
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2083 AA; 234649 MW; 8A4D3F83FB35FC1E CRC64;
MDTFAKTGIR AFLDPQRYPV ALSDLFVKLL SPTTTYKSVT GLKADLDRIL SACKDPKKTN
QIPPELGRYD CPVSLQLPNK LYGREAERAQ LNTILERMSH QVHEGSQSSE LVIITGDPGI
GKTALVNSVL NKAWRQGIFV SCRCRRHFPL GAITQCLRST IKKIIKYSDE DLQRLRLSIL
SQIPNNMRLL LDDIPELKLV VGVHHPPVEP LPPAQAHMRF CITYLKLVRA ITNLEINLTC
FLDRLECASQ ATLSLFSFLM RNSCGRLLVI AARRESDREN QWIRELLEYD VKVTEIPLRP
LSTQDVREFV ADTVSLNTSA VESLVASCST AEGNPFALTQ ILIALYREKR IQFNRASSRW
SWQLDANSKI VDFLDVDLLV RCLRSLSKGL QTLLAHASII GYSFTANLLH ALLKPPYPLE
ENLQIALREG FIRYAPEEEC YYFFHDIVQE ASQKLLDEDA KSQLHLNIGQ LLLKETGTNV
FLIAEHFTYA AGIIRRLEDR ADYKRCLVAA GAKAKSLGAL ENSLIYYQKA ITLVEPLPLR
GHAETNSSYE EAFSLMLECA EMSSACQEFT TASEILNQLL LKARSLTHKC QVYIHIYHIQ
MATNQFEDGV QTILNCLRDF GFDVARDPKD AKLGPLLEEL RYSTLLADTS ALEDRLKWCD
DPQMSTLMDF LAPALYSPYI SWLRHIHIAI SAIMVRLTLK HGLSAHSCEA FVYFGAHYAH
VFESGEFAYE CGKFGVRVAK RFAGPNIQAK VYLVFATFLN HMKNDPHDGL TLLKESQELA
SSAGNLKISA LSSGMAATKQ FFLGLPLGEV LKNARASSLE LLKVHPDNNL TYAITSISRL
VLALQGKCIR GSANLIFDDG QYSEENLLRV ITSEARFNRS MVWHSRVRIF AFYFLGYYPE
ALQEAQRSEE ISDSNESIDN FKKWAVSFHS LTLAALIRKG QLNDNQAKQA LETIRQNQLT
TQKWIVHQVY GPHTTLFLIV EAELYALNGE PMKALDLYEQ AAQQSRQLKL VHYEALSYEL
YAEFLLRRGY ITTGMMMLEQ SIKTYSKWGA YEKAQLLQRM QDNWVTSLPA LSKTPSSASV
ACQTDEALEE DDSSRFATNE IVATPPSQQP SPGGRTLTDF IETLQHLSSE LEYEPLIHQI
LEQTPRFVSI HSGSLILLDQ GKLTVSARWE HDEGAFLLSP AIPHDDVSFV CSALVDKALA
SKSVEFFDYD TTNPLENVSA KVREHIDRRS AGKKFTAAVF PLIHKNTLVG ALYFENTALP
EPDLQEIEQL CKHIALCLVN ASLLRTTQLK LRETEQAKNH YLTLVNALPC VVWIGNRDGS
SWFVNEKVEE ITGVTSNQFL GWGWSQFIHP DDIDSMMSKW RSCIAKLQAC ELEFRMLSRD
GTYRWVLGRH VCVRDTYGKY TWYSMWMDID IHKQALYHVE EGKRRYSLLL ECIPCQVFTA
QPDGIIDYVN SSWCKYTGQN IQQATASNWT SCIHQDDLKA HQEQYTQCLQ NGLTLECECR
IRGASGAYRW FIIRAMPLKD SCGTLIKWFG MCTDIDEQKQ QQRLKSNFLA NMSHELRTPF
SGVIGMLSLL LDTSLNSEQL EYVEMCKQSC DVLMQVVDDL LNFSKLEAGK VVLEQLPFHV
EDLLGDVCEL LTTLVSKKNL EVAFYVDPRI PSTLIGDGNR LRQILLNLLG NAIKFTPKGY
IVVRCHVAQE PSQDGELVVK IEVEDTGIGM TIEEQAYLFQ PFSQVDGSTT RLYGGTGLGL
SICSQLVKLM HGRIGVISQK GKGSNFWFTA TLKQESDAVS VENAPEILQL ISRIHSLKES
PRFLISLHQS IAPMITNYLG PFDCVTCENA LEISEGINAA KEANQPFDIV ILDAAMDQEQ
WEMLVEASLL DGVKTLVLTY PSSVKMDEEA PSFKGLEIRR ITKPVRRSKF LKCVVDLFDG
NSSPDGAQTL STATSSTMPA EPNTANEPNG EGTMHVLVAE DNFIAQQLIT RMLQRMGHDV
TVTNNGLEVV DVYKSQPYLY ACIFMDKMMP LCDGYEATRR IRAFESESSI TRRIPIVALT
ADAQSKTKKE CLGVGMDMWL TKPCDKKNLM RVLAEVAALQ PEL
//
