ID M0NWN1_9EURY Unreviewed; 588 AA.
AC M0NWN1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C468_11192 {ECO:0000313|EMBL:EMA62362.1};
OS Halorubrum kocurii JCM 14978.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA62362.1, ECO:0000313|Proteomes:UP000011546};
RN [1] {ECO:0000313|EMBL:EMA62362.1, ECO:0000313|Proteomes:UP000011546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA62362.1,
RC ECO:0000313|Proteomes:UP000011546};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:EMA62362.1}.
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DR EMBL; AOJH01000068; EMA62362.1; -; Genomic_DNA.
DR RefSeq; WP_008848927.1; NZ_AOJH01000068.1.
DR AlphaFoldDB; M0NWN1; -.
DR STRING; 1230456.C468_11192; -.
DR PATRIC; fig|1230456.3.peg.2223; -.
DR OrthoDB; 106630at2157; -.
DR Proteomes; UP000011546; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
FT DOMAIN 10..73
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 121..195
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 197..248
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT REGION 367..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 63951 MW; 5046D1D6BC97957B CRC64;
MAESPDPEVL LDLAGDKIAV LDEDGIFRHL NAAVTDLLGF RSDELVGTDA LALVHPDEEA
RLRAILAEIV SGDPAPDEPL EYRYRTADAG WVWLRTTVHL PEETGIDGYV LTSRDITAEV
ESRRRLETIA SVSGDVFWMF SSGWDELLFV NESVEEVFGV PADALERRPE SFLDAVHPDD
RPYVKRAMKR LSNGESTRID YRLGPADGVT RWVRVPGEPV IENGEVVAVA GFARDVTEEY
RRERQLAVMD NLLRHTIRND MNIVDGTAER IADAVAEADA FDAEVGDGRI DPDALAELGA
GLQEHAETIR RVASDLLTTA EKQRGVIDLL RQRGSPRTVE VAPVVEEALG MVVDDCDEAI
DIGYREPMDD AGASEKGFGG GAETGAGSRF GAETETGARS ADGGPVDETA NGDSESSPRV
SVSYPPNARA FTHPELDYAI AELVENAIEH AESTPRVRID VRATDEVIEV SIHDNCPPIP
VEERYVITDR WEMDDLRHTG GMGLWLVYWV ANRSGGDLNF DTHGDGNIVT LTVPNAKTDA
SVEGSREPGR SNRSETGGVE RADTRIRTDG SVPSAPDGGE DDDTDGAN
//