ID A0A397W9F9_9GLOM Unreviewed; 1372 AA.
AC A0A397W9F9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Histidine kinase-like ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C2G38_2237969 {ECO:0000313|EMBL:RIB30871.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB30871.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB30871.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB30871.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:RIB30871.1}.
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DR EMBL; QKWP01000003; RIB30871.1; -; Genomic_DNA.
DR STRING; 44941.A0A397W9F9; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
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; 2.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673}.
FT DOMAIN 367..592
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 990..1215
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1372 AA; 157705 MW; B489AD9F07EDD9A8 CRC64;
MQSPLMMLNK SENSNFIDMV YNFDWSSTPL GPMDTWDPAL KNATNICLKN EFPTCIYLDP
PNWLILYNKA LGRPVKDVWP ERYEAHMGLA FNRVTTTGKG LYYNDRLSML KRDGYDEKVY
FSHTYSPIFK SDGTIGALWC LVQETTHKVL NTRRLKLLGE FGHFSSNIES LESACHIITK
ALRNNEDIPY TLIYFVKHKL NASSESLIAH LMATTFDSDD KEKIKFPDYL PKSHETIDLA
KDANKSYNTY IELKRSAATY SFLKCDSWPI YLVFKEGRNV KVLLNDESQA VLFPIKISLD
KDHVLSVILI YGINRFRALD DRYMEFFNLV TNQIYALLQH GKSVEDEKNQ TKILADMNCQ
KITFFQGISH ELKTPLTLML SPLDDVINKC IQEPLLMSHL QIIRRNAHRL LKLINTLLQF
SNIETSQLKA HYRETNIAEF THELASDFIS MAKTLGLNYN IDIPNPDEFD LDKIYLDRDL
YETIVFNLCS NAFKHTWNGQ ITVRLYPDYK NEKKKVIVLE VSDTGVGIPE SALPDIFQRF
YRVESQGARS HEGTGIGLAL VKELITLHGG DITVSSVVNQ GTTFKCWFPV GCEHFLIDQM
ENQINNGREL YNNRQLYLEE SSQWIKYNKF NKFETQDVEI NQYPVDHQEL DNINIDDDNI
SESDRKYKVL IVDDNNDMRD YLAELLNEFD VYRACDGQDA LQTLKTLRKL PDLILNVSMP
NMDGYELLNV LRSNIKTQLI PVILLSAKAS ETSKIQGFDK GADDYLVKPF STQELLCRIR
ANIECSILRR KILFHQYKQE DIKQLLFSII NMILSESDLD KTLLYITKEI YRRLPCEKIF
IISNEPFKNN KIVIPYENVS EDLTPIINPF TEINEFNNSN SQLFTRSQKY LNENSNVDIS
LDAYCDVVHK NGSILSVKIN LDDNFWGWIK VYRSQNSVWC DSEIELLQQI SNNISLAITY
AKLLEEIGEK EIQIKAAEFA NNAKTQILAN TSHELRTPLG AIVGITSSLE GTTLTTEQKD
MLNIITNAAD IVLSIVNDVL NVAKLEAKKL ILVNRAFELL NSLESTIIIF GKKAATKNIE
LIVNCEIDML PKYVKSDPER VKFTNEGEIV LKISMQPQEV IKGNNEENSS YDQLVKKEKL
LIELSDTGIG MNPRYIKHAW ESFSQSDMSI TKKQDGAGLG LSICKNLVEI NGGEIKVESQ
LGKGSKFSFT WNVEILPMAS LSMESQFNKP TSYVLPHNVR KKRILIIHSA ENLRNSILNY
LKSVEKIDTF DTFEKGINAV KTYKELYDKF TYDIIFIGLY ENNKEETINF ILELKELLID
SNNLAIIFIV FPSNERIILA RELMEKFLGT FVLYTPITLN KLINLFVYME IN
//
