ID A0A1D3L0N8_9EURY Unreviewed; 991 AA.
AC A0A1D3L0N8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative sensor histidine kinase pdtaS {ECO:0000313|EMBL:SCG85222.1};
DE EC=2.7.13.3 {ECO:0000313|EMBL:SCG85222.1};
GN Name=pdtaS5 {ECO:0000313|EMBL:SCG85222.1};
GN ORFNames=MCBB_0649 {ECO:0000313|EMBL:SCG85222.1};
OS Methanobacterium congolense.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=118062 {ECO:0000313|EMBL:SCG85222.1, ECO:0000313|Proteomes:UP000094707};
RN [1] {ECO:0000313|EMBL:SCG85222.1, ECO:0000313|Proteomes:UP000094707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Buetzberg {ECO:0000313|EMBL:SCG85222.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT607756; SCG85222.1; -; Genomic_DNA.
DR RefSeq; WP_071906413.1; NZ_LT607756.1.
DR AlphaFoldDB; A0A1D3L0N8; -.
DR STRING; 118062.MCBB_0649; -.
DR GeneID; 30411504; -.
DR KEGG; mcub:MCBB_0649; -.
DR PATRIC; fig|129848.4.peg.657; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000094707; Chromosome I.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17534; REC_DC-like; 1.
DR Gene3D; 2.10.70.100; -; 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; 5.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF07568; HisKA_2; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 4.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SCG85222.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000094707};
KW Transferase {ECO:0000313|EMBL:SCG85222.1}.
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 131..205
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 209..259
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 267..337
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 339..389
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 469..521
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 522..594
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 597..648
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 731..783
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 794..986
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 991 AA; 114414 MW; EA06A31357A5E149 CRC64;
MVNKKILLVE DESIESLDIK RVLESFGYQV PYVASSSEEA VEKTIEIMPD LILMDIVLKG
DSNGIGAVSK IKDLNIPVIY LTAHSEESTI ERAKLTEPYG YIIKPYDPTE LKYAIELAIY
KNQTKKELKQ NEKRFRHILE NSLDVVYRRN LDSDEYDYLS PMIEQVLGYS TEEFISMPST
EVVELIHPHD RENVSNIFAN AFSGKTKTYN IEYRFKQKNG HYKWVNDFGS IVKDGDIMFL
IGSVYDITER KKGEERRKNG EKALRESEEK YRAMMNYSSD AIVLTDFEGN FVECNKNAEE
LFGYSQEELI KLNFRDIHPS EELEVVQTSF KKIIMDDMGT VDTLVLTKDN KKVPVAITGS
LIEYGDKTII QGMFRDITER KESEESLLNI NKALKKRDEE FKYFIDSAPV AIAMFDKRMR
YIAASLRWIE DYNLEGQELH GISHYDIFPE ITDEVKEVHK RALTGSIERA DDDKFVRADG
RVQYIRWEVH PWYLSSGDIG GIIIFSEDVS ERINAEKKFR DNEEKYRTLF ESNPDYTIIV
GLDGIILDFN VAAEQIIGIF KDELIGKHLM DLGILPKDEL DLLEEKFSLL VKHGEVAPFE
FRIIDKNGDI RWGETSLTLI MGENGPAYIL VIFNDITERK IAEKKLRSSQ IQLVNAMEMS
NLVNWEYDVA SDTFTFDHRF YDLYGTTVER EGSYLMSSEV YAREFVHPDD HDMVADETAK
AIETSDPDYV SMVEHRIIRR DGNIRHLVVR IAITKDSEGR TIKTHGTNQD ITELKEKEEE
IKKSLEEKEV LLREIHHRVK NNMQIISSLL NLQIQHVEDR EAENVLKESQ GRVKSMAMLH
EKLYQSPNFT NINFKEYIER LVFDIFYSYG IKTGSIESEL DIEDIKIGIE TAIPVGLIIN
ELVTNSIKYA FPKYNGTIKI EFKSSEEGLE LIVADDGIGL QKDIDPKNTE TLGLQLVNSL
TDQIDGNIEL DRSNGTKFKI TFKELDYKER L
//
