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Database: UniProt
Entry: A0A2I0P4L9_9EURY
LinkDB: A0A2I0P4L9_9EURY
Original site: A0A2I0P4L9_9EURY 
ID   A0A2I0P4L9_9EURY        Unreviewed;       620 AA.
AC   A0A2I0P4L9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CVV31_12660 {ECO:0000313|EMBL:PKL61186.1};
OS   Methanomicrobiales archaeon HGW-Methanomicrobiales-2.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=2013818 {ECO:0000313|EMBL:PKL61186.1, ECO:0000313|Proteomes:UP000233573};
RN   [1] {ECO:0000313|EMBL:PKL61186.1, ECO:0000313|Proteomes:UP000233573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGW-Methanomicrobiales-2 {ECO:0000313|EMBL:PKL61186.1};
RX   PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA   Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA   Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT   "Potential for microbial H2 and metal transformations associated with novel
RT   bacteria and archaea in deep terrestrial subsurface sediments.";
RL   ISME J. 11:1915-1929(2017).
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:PKL61186.1}.
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DR   EMBL; PGYL01000043; PKL61186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0P4L9; -.
DR   Proteomes; UP000233573; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          402..618
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   620 AA;  69472 MW;  E746FFF63706A750 CRC64;
     MAPYTMKGPL LPLLERDFQE PGKFLVAGTS GIAVLAALLV EPPGTNLILW LLLFIPAVTA
     GYLYYERGLV AATVLGLACL GITALRAYPH PAIFLPFVAM VALASLASTV GHSTRERARQ
     REAMGQGPGG AFLLRRETRT IADANQDFAE LLGYAQEDLR EMPASRLWLY ADDRERFFFL
     AKPGEGSTII ETQFVGRDGG THWFVLWGRC IDDAVISCRV SDITRYKETE AALNAEHRRL
     FSVLDPPPAY VTLQREDHTF RFANRAFRET FGNPEGRTCY EVQQGSRRPC RPCRGTLVFT
     LKSPQRWEWD HMNGNTYEVH AYPFTDTDGS NLMLQLGIDI TQRVQAEEAL KGFAGNLQVK
     NRELEVLRSQ LCVVNQDLDA MVRERTADVE KLLTQKDEFI SQLGHDLKTP LTPLVALMPG
     LLQREQDPEL RRLLEIAGHN VTYMKDLVQK TLQLARMNSL YIELDLEPLN LRTELDNTLR
     NYTVPLKAKA IVLDNNIPPG ITVRADRVLL GEIFNNLIAN AVKYTENATG TIAIDAARRQ
     DVVIVSVRDT GIGMTRDQLE RAFIEFYKAD ASRHDLDSPG LGLTICRRIV ERHGGRIWAE
     SDGEGMGSTI IFSLEAIDEP
//
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