ID M0NL62_9EURY Unreviewed; 685 AA.
AC M0NL62;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=PAS/PAC sensor signal transduction histidine kinase {ECO:0000313|EMBL:EMA58526.1};
GN ORFNames=C470_12088 {ECO:0000313|EMBL:EMA58526.1};
OS Halorubrum litoreum JCM 13561.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227483 {ECO:0000313|EMBL:EMA58526.1, ECO:0000313|Proteomes:UP000011581};
RN [1] {ECO:0000313|EMBL:EMA58526.1, ECO:0000313|Proteomes:UP000011581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13561 {ECO:0000313|EMBL:EMA58526.1,
RC ECO:0000313|Proteomes:UP000011581};
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 -!- 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:EMA58526.1}.
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DR EMBL; AOJF01000052; EMA58526.1; -; Genomic_DNA.
DR RefSeq; WP_008367513.1; NZ_AOJF01000052.1.
DR AlphaFoldDB; M0NL62; -.
DR PATRIC; fig|1227483.3.peg.2402; -.
DR Proteomes; UP000011581; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR031621; HisKA_7TM.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF16927; HisKA_7TM; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EMA58526.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EMA58526.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 349..419
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 475..681
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 685 AA; 74341 MW; 505F03F4F5F474AA CRC64;
MAWQATPYTV PLLVAAAASF AFAAYAVGNR SRGGRVLLWS FVGVAGTAGV WSLAYAAQLS
ASSLGATLFF NRFVWLGSAG LAVAWPAFVL SYVDRTAWLD RRRFALFWVV PAAVVVPVWT
VGVDPLFYLD PVLVDAGGFR ILEYAPTPAL LGFVGYTYAV NLFTFAVLGY AAVTRDGVFR
RQAAVLFVAG VAPLALGAAG IAGLVGPEDG LVDFTPIAFS GTSALLAWVV FRYRLLDVSP
IAREAVFANL SDGVVVCDAD GRVVDNNDPA EALFPDANVG VHADEAFADV PTVADAVTEE
PADDEFRVTV DGGGAPRFLT VDVHDITGPG TTRGGTVLLF RDVTERETLQ RRYRALIEKS
PNVIAVCGED GLLRYVSPSI ERLIGHKANE VEGRPVIDLV HPEDRREAQR AFERAFDSAE
PQSLTHRIAC ADGSWRRFET VIERLFADTR EVVITATDVT DARRYEQRLQ VLNRVLRHDL
KNDTNVIGGY ADLLRDHVDE EGDPYLDIID RKVRTLTHLS DQAREIDVAL HSDAGRTEID
LAALVERLCE SLESSFPHAT VTATVPESAV VSADELLESA VRNVLENAVV HNDGDDPHVE
ATVVADGDGD RFRLDVADDG PGIPPVERTV FSEARETALE HASGLGLWLV HWIVTESGGD
LEIDTREPTG TVVRMWLPRA AEESE
//
