ID A0A437AE01_9PEZI Unreviewed; 1057 AA.
AC A0A437AE01;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DFL_000325 {ECO:0000313|EMBL:RVD89311.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD89311.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD89311.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD89311.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RVD89311.1}.
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DR EMBL; SAEB01000001; RVD89311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437AE01; -.
DR STRING; 97331.A0A437AE01; -.
DR VEuPathDB; FungiDB:DFL_000325; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
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; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
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:UP000283090}.
FT DOMAIN 290..363
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 366..418
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 578..803
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 908..1031
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 838..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 962
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1057 AA; 117489 MW; 113EF89E8752B0F1 CRC64;
MATSRPYNND LEELGLQSLS FTQSSARLLI ADSNDNVLGI NNAARRFLFP SSSSSAPVRA
NGLPSKLKDL PLVLLDQESQ RWIKLDQILA VAREELKRSN ASHHRVEAAT SGSHAKPNTP
VRIESSLIQT SSGTVYSSLC LIPLETDVEA ENFTPAIIPK LMHMKDKILD HLNELVIFCL
SIDGNLLVTN KAAEALLGDS TPKVGKGIDW LKERWKVYEP DFSAEIPFER WGIYALLTEG
VIVRQTIGYY DPTGAPKVIE LGGEPIKDDD GNLVAGIVWL KDETSWHKKG EEKFRRICNS
IPQMMFALTS DIKPEYFNKR WYEYTGLSIE QIRSGYNNPF WNICHPEDQV AVENAWKHAV
ESQSPAQVQF RCRDSEGAYR WMLCRANCYF DDQGQVSKWY GTLTDINEQI EAVEEQCRLQ
NQFSQIIHSS QLCVMTIENT PDRRISTLHG RMIFPVGDKL AVGANFLEAF KGYDTFTEPL
ERLLTKQSEL IGPDITAEIE MKGKWFRCRF TPNRSRSVPA AGKPESVSPT KGGPVDAVVL
FAADVTARYI ADKEKEQLEE RESAAVKESQ LKSTFLANAS HEIRTPISQI IGMSEVLLDT
QLEDQQKEYT TNINRSANAL KAIISDILDL SKIEAKKMTI TTSAFDLSSL LNEIITMFKV
TTSQKGLNFD HISILDESDY LVIGDQGRVR QILTNLMGNA FKFTSEGFIR MITMRDKEQP
DPDRVRIRFT VEDSGVGISD EALKKIFVPF SQADHTTSAR FGGTGLGLSI SKELVELMHG
EIALERSKGG PGCVAWFTIP FQRYDGRKTI DPVPDSDSNN AMNRFRFEME RAMKRHDEEV
SSVGSVSPVP SPRARAAQLH SSPLVPALPS NSSLPRASAT LMPPPDHPAS TSRNVNSATV
DRRGDPIRVL LIDDDHVVRL VSQRHLQGAG CQIYIANNGK KGLELLEETA KRGGIPHLVL
TDCRMPVMDG YTFARKVRTH PLAVIRDLPV VAMSAATTDE EKARCAEVGM TRFLSKPAKK
EELYEVLSEC LLSKRVPTPN LSGPTSAPGL GGGGNSN
//
