ID A0A2I0NTK7_9EURY Unreviewed; 645 AA.
AC A0A2I0NTK7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CVV35_00895 {ECO:0000313|EMBL:PKL57307.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013822 {ECO:0000313|EMBL:PKL57307.1, ECO:0000313|Proteomes:UP000233331};
RN [1] {ECO:0000313|EMBL:PKL57307.1, ECO:0000313|Proteomes:UP000233331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-6 {ECO:0000313|EMBL:PKL57307.1};
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 -!- 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:PKL57307.1}.
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DR EMBL; PGYH01000005; PKL57307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0NTK7; -.
DR Proteomes; UP000233331; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; 3.
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; 2.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 46..119
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 252..304
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 305..383
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 378..430
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 539..637
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 288..315
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 645 AA; 72874 MW; 9A203F645935CD66 CRC64;
MKQLEHLQRT LQPLLEQLPA EEQKEVAAAL AGMESGIASL TADYDHIQRY RRVFENTSTA
IIVLEADCTI SLANTQFERL AGYPKSEIEG KKRWIEFIVP EDLTRMKGQH HLRREREERA
ETQYEFRLLS RSGEIHDIFA NIDMVPGTTE SIAILLDITE QKKAEEIIRQ TEAQLTNAMD
IAQLVKWEED VEAQTFTFND QFYSLYGTTA TREGGNVMPM ERYAREFVHP DDLHLVAEVM
ARTTQGAVPE VQQVEHRILC RDGTVRHIIA RIKCVKDADG KPVKVYGANQ DITERKRMEE
ELQKKNAELQ TIIDNIPDLA WLTDANSRFI AVNKKFSDVV GVGPKNLIGN TCGLCFGTEA
AEIFEEETRK VMASREQAVA EESFIDVGSS KPIFETIRSP ILDRSGKVIG TVGIARDITQ
RKKTEEAVRL ANKKLNLLSS ITRHDVLNQL TVVLGYLRMA EEQATDPILC DYLEKMDKAG
EIARRQIEFT KEYQEIGVQL PRWQDVRSTI VQATEDLDPG EVTLSIDIQG VEVFADPLLE
KVFYNMAENA LRHGGKLTKI EFSAEDSDRC LRIVCEDDGA GVPESEKQNI FERKYFKHTG
FGLFLAKEVL AITGLSIRET GVPGEGARFE LLVPAGMYRS SGRQS
//