ID L0JWX9_9EURY Unreviewed; 1067 AA.
AC L0JWX9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=PAS domain S-box {ECO:0000313|EMBL:AGB36348.1};
GN ORFNames=Natoc_0486 {ECO:0000313|EMBL:AGB36348.1};
OS Natronococcus occultus SP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB36348.1, ECO:0000313|Proteomes:UP000010878};
RN [1] {ECO:0000313|EMBL:AGB36348.1, ECO:0000313|Proteomes:UP000010878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP4 {ECO:0000313|EMBL:AGB36348.1,
RC ECO:0000313|Proteomes:UP000010878};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA Klenk H.-P.;
RT "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CP003929; AGB36348.1; -; Genomic_DNA.
DR RefSeq; WP_015319804.1; NC_019974.1.
DR AlphaFoldDB; L0JWX9; -.
DR STRING; 694430.Natoc_0486; -.
DR GeneID; 14405514; -.
DR KEGG; nou:Natoc_0486; -.
DR eggNOG; arCOG02327; Archaea.
DR eggNOG; arCOG02330; Archaea.
DR eggNOG; arCOG02334; Archaea.
DR eggNOG; arCOG02367; Archaea.
DR eggNOG; arCOG02387; Archaea.
DR HOGENOM; CLU_010703_0_0_2; -.
DR OrthoDB; 327291at2157; -.
DR Proteomes; UP000010878; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 3.30.450.40; -; 2.
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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010878};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 155..226
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 433..503
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 507..558
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 717..773
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 847..1053
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 118..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 116982 MW; D707A91B07A72630 CRC64;
MGTATHVVCV GTPLPPNVED VLEDVTDAVT VAVAETAADC LAGLESADCV VATDAVPDTT
CPELCSQIAR RRPELPVVVF PATGSEELAG EVIAAGADGY VPRSQGLETL RSRLDGLIGD
GSNERHEDGA GRNAADDRDE SGDRAQCRDS SPNGGSSRLE LLVEQSPLAI VEWNREFEAA
SWNPAATELF GYAPAEALGE SAFDLVVAER DRTEVANHWE LLVEADLEES FRTVNRNVRA
DGTELTCEWI NTPLIEDGEV VRVLSFVRDV TDDLERANAL EALQETTRRL VGTSSPDEVA
EIIMEAIERV LDRSLAGVWF AAEDTDRLEL EATASRLADD SIARRPIDPG SGLLWEAYDR
GEPIVVDDAT TERLPYFLEY PLGNAVVYPL GDHGVVSVCS VAGRELEAAD VSLVQVLAAA
AETALDRTAR RRELERAKTI VEAVGDSIYA VDRDGRFVAV NDMLASVTGY DREALLGRHF
SSVLTDESVA RVRERVDEFE PGAADTATDE VTVSTRTGER IPCEATTRLL CRDGDPEGAV
GVVRDISDRK RMERELRDRR AKIESLHEVA SRLDDCDSPE EIYELVVETA EDVLNFDVCV
VDRIVGNSLE KVALSSQLDD ADYVERIDVE RGVAGRTYRE QRTYRIDDVD RCDDAMEDAN
AYSSILSAPV GDHGVFQAAA RERGAFDRHD EELVELLLSH AVDQLDQLES EEKLRSERDR
FAALFENVPD AVVSLRHCDG EPIIEAVNPA FERVFGYAEA ELVGEPLDEF VVPPGTSDTP
AERDPRVDEG TVVETEVRRR TADGFREFVL QLVPIELEES DGRSFGLYTD VTEQNRRRKR
LEILNRVLRH DLRNGMNVID GCAELLAESL EGTDAARVRT IRERSRDLTS LAEKSRTAEC
VLDRDANSRP VNAAALAERA ADRLEDVHPD VDLGRSLPTS APVIASADLR TAIYQLLENA
VEHHDGVPSV DLELRERPEE DLVVLSVVDD GPGIPPEERA LLSDDREITQ LRHASGLGLW
LANWVVSQAG GRLAFADNEP RGTVVRIELP RADPEAIGPA SDRSASE
//
