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Database: UniProt
Entry: A0A101IWW0_9EURY
LinkDB: A0A101IWW0_9EURY
Original site: A0A101IWW0_9EURY 
ID   A0A101IWW0_9EURY        Unreviewed;       763 AA.
AC   A0A101IWW0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=PAS domain S-box {ECO:0000313|EMBL:KUL02802.1};
GN   ORFNames=XE11_1614 {ECO:0000313|EMBL:KUL02802.1};
OS   Methanomicrobiales archaeon 53_19.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=1641394 {ECO:0000313|EMBL:KUL02802.1, ECO:0000313|Proteomes:UP000054757};
RN   [1] {ECO:0000313|Proteomes:UP000054757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUL02802.1}.
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DR   EMBL; LGHF01000032; KUL02802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101IWW0; -.
DR   PATRIC; fig|1641394.3.peg.2023; -.
DR   Proteomes; UP000054757; Unassembled WGS sequence.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
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; 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; 3.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
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; 1.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   DOMAIN          10..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          141..211
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          214..266
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          302..372
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          422..500
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          558..751
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          264..298
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         60
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   763 AA;  86841 MW;  C20348F06EB6F6EC CRC64;
     MPNSVDSPIR ILYVDDEPEL LTLGTTFLET NGDFLVEGCQ SALDAVHLLK KDHYDAIISD
     FQMPKCDGIS LLTYLREKGD EMPFIILTGK GREEVVIEAL NNGADFYLEK GGDLKAQFAE
     LSNIIRYAVA RRRSEEALRE SEERYRNVVL DQTELICRFS ADGTVLFVND AYCRYFGVPC
     KEIVGSRFKP MIHPDDSGKV YRLFSSLSPE KPQASIDQRT IAPDGRILWQ RWNTRAIFGE
     DGSLREFQSV GQDITDLMER DLELKRANEE ILASYEELTA IEKELREQYD ELNTTETALL
     KSEALQRLIL QSLPDFLIRY DREGVYLDIL NYQEDLLILP KDEVIGRRVT EVISGGIGDR
     MIQAIRSALD RNELQTLEYT LPVPAGVCHF EARIVPYTEN EVIALIRDIT DKRMAEEAVI
     KSEKRYRSLF ESMHDGYALH RVRADPDDGD AVIHILDVNP SFEKLIGEPR DQVVGMLLTE
     VLPEADPHLF ERIAHTAETG ESEVFDICLN NPMRYVTVSV YSPGAGECAT LFQDITEKKR
     RDEETKQSLR EKELLLKEIH HRVKNNMQVI SSLLMLQKET ISDPEMRELF SQSESRVYSI
     ALVHEKLYQS ENLSRIEYGE YLSMMGEYIF SSRQVRAGTI ALDIHADGIY LSIDKAVPLS
     LITNELLTNS LKHAFPDGRK GTITICVEKK NNTLIYRFSD DGIGFPADID FENTRTLGMQ
     LIVSLVNQLL GTITLRREKG TAYEIVFPVD PGEYETVDSG TLE
//
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