ID H1YXJ5_9EURY Unreviewed; 984 AA.
AC H1YXJ5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Metlim_0842 {ECO:0000313|EMBL:EHQ34964.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ34964.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ34964.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ34964.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) 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};
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DR EMBL; CM001436; EHQ34964.1; -; Genomic_DNA.
DR RefSeq; WP_004076678.1; NZ_CM001436.1.
DR AlphaFoldDB; H1YXJ5; -.
DR STRING; 937775.Metlim_0842; -.
DR PATRIC; fig|937775.9.peg.975; -.
DR HOGENOM; CLU_000445_114_58_2; -.
DR InParanoid; H1YXJ5; -.
DR OrthoDB; 230688at2157; -.
DR Proteomes; UP000005741; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 5.
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; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
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 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; 5.
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; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000005741}.
FT DOMAIN 3..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 134..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 207..259
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 260..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 333..385
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 385..456
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 459..511
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 511..566
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 585..637
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 638..711
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 715..767
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 984 AA; 112870 MW; 5B6E9D5AB073654A CRC64;
MIRILHVDDE KSLIDLTKIY LEKKGEFRVT SASSVSEALK ILESDCFDVI LSDYEMPHID
GIEFLKTLKA GGDPTPFIIF SGRGREDVLI EAINNGADFY LQKGGKPTAQ FAELKNMIFQ
AYSRKKAEIE LKKSEERYRA VVESQTELIC RFLPDGTIGF VNDAFCRYYG LDSQKIVGEI
FVPNIPDSEQ NAIRSHLKSL TPENPFDSIE HRIILPDGSV RWQQWNDTAI FDERGNISEY
QSVGRDMTDQ KLMEEWLQEK VNYVQALMYT IPAPVFYRDV NGVYHDCNKA FEELVGLPRS
EIVGKNIHDF FNKDLAEWYA KMDREIIDSP HLQQYEYQIN NSMGEILDVL FSKTARYRAD
GTVDGIVGVI VDISDRKKME KSINEEINFI QALKDTIPAP FFFRDEYGIY HDCNKAFEEL
VGLSRDEIIG KDIHHFFNKD FADFYAERDR EILNNPHLQQ YEYRINNSDG EIFDVMFSKT
AKLRADGTVD GIVGVILDIS QRKNVERDLK REINFIQALK DTIPAPVFYR DINGIYHDCN
KAFEELVGLS KEEILGRNIH DFFNDDLADL YSVRDKEIID NPHLQQYEHK INNSEGEIID
VMFSKTALHN PDGSVAGIVG VILDISRRTR MEEALRGNEE MMRTLADYTY DWESWVGPDS
SYIYISPSCE RITGYKPEEF MADPMAIMND IVHPDDLEML IDHYSGIDEN NTDVAHFDFR
IILPDGGLKW ISHYCQPVYH EDGTWAGRRE TKRDITQRKL AEEQLSIANS KLNLLSNVTR
HDVLNQVTAV LGYLELIREF SGRDDDVSEM VSKIEILMNT IQHQLLFTKD YQEIGITTPV
WQDLDSCIWD VSYLLDLNDS EVFVDVGSYE ILADNLLKKV FYNFAENSLR HGGGKLTEIR
FTTEEENGFL KIIYEDNGGG ILYADKDKIM LKGFGKNTGY GLFLSHNVLS MTGMSLRECG
VPGEGVRFEI TVPAGNYRVK SSGT
//
