ID A0A0Q0W3T1_9EURY Unreviewed; 737 AA.
AC A0A0Q0W3T1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APR55_07680 {ECO:0000313|EMBL:KQC11471.1};
OS Methanolinea sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanolinea.
OX NCBI_TaxID=1735327 {ECO:0000313|EMBL:KQC11471.1, ECO:0000313|Proteomes:UP000050878};
RN [1] {ECO:0000313|EMBL:KQC11471.1, ECO:0000313|Proteomes:UP000050878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC11471.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQC11471.1}.
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DR EMBL; LKUF01000005; KQC11471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0W3T1; -.
DR Proteomes; UP000050878; Unassembled WGS sequence.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 3..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 134..205
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 208..259
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 256..326
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 328..378
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 377..421
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 465..519
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 530..727
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 737 AA; 83495 MW; 11D104216FB20EFB CRC64;
MYSILYVDDE PAFLDIAGLY LKRSGDLQVD TSASAKQALK MLHAKKYDAI ISDYQMPVMN
GIDLLKRLRE SGDSIPFIIF TGRSREEIVI QALNEGADFY LQKGADAKPQ FVELEHKVKQ
AIERRRTEKA LRESEIRFRE LARLLPQIVF ECDVDLNLTF VNEPAFRLMG YTPADLYSGI
NVLDAIDPSQ HHRLKENMYR LVRGEPVTHQ EYTMVRRDGS TFPSLMYASP IFKENRNVGF
RGVVVDIGPT RQKDDYRKIL VQLLDNAPEA ISVHDFDGNF LYVNQKAIDI HGYSRGEYLS
LNLHSLDAPG TREKIAERMR ILEEKGETSF EVEHIRKDGS VVPLLVKAKY ADWGGKKVIL
SIATDMSDRK GTEVRNREAE TRATIDSFPI PSFVIDNDHR IIIWNRALAE LSGIPADAVI
GTRQHWRAFY RTERDCLADL LADNRIGDIE ELYSGKWAPS KLIPDAYEVT DFFPYIGENG
RWLYFTAAII RGSDGQSIGV AETLEDITER IAAEEALSQT NKKLNLLSNI TRHDILNQIT
VLMGAAALLR EEALSSRDRM EFLDKIDTST SIIRRHIEFT REYQDIGIDS PTWQALDRII
ARTLDQFDLS HIDLDLDLPG VEIYADPLLE KVFYNLIHNS LVHGQNVTRI SIQADENPYG
LAVRVSDNGS GIAHEKKEEI FKRGFGKNTG FGLFLAREIL DITGIGIREI GIEGEGACFE
LSVPRAGFRR CNGNDVS
//
