(data stored in SCRATCH zone)

SWISSPROT: Q0SKQ1_RHOJR

ID   Q0SKQ1_RHOJR            Unreviewed;       573 AA.
AC   Q0SKQ1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   SubName: Full=Sensor kinase, two-component system {ECO:0000313|EMBL:ABG91885.1};
GN   OrderedLocusNames=RHA1_ro00049 {ECO:0000313|EMBL:ABG91885.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG91885.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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DR   EMBL; CP000431; ABG91885.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0SKQ1; -.
DR   STRING; 101510.RHA1_ro00049; -.
DR   PRIDE; Q0SKQ1; -.
DR   EnsemblBacteria; ABG91885; ABG91885; RHA1_ro00049.
DR   KEGG; rha:RHA1_ro00049; -.
DR   eggNOG; ENOG4107EFD; Bacteria.
DR   eggNOG; COG2203; LUCA.
DR   eggNOG; COG4585; LUCA.
DR   HOGENOM; HOG000245055; -.
DR   OMA; NCKKHAG; -.
DR   OrthoDB; POG091H03PP; -.
DR   BioCyc; RJOS101510:GJJ1-49-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0070483; P:detection of hypoxia; IEA:InterPro.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR027035; DosT/DevS.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF_dom-like.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR43336:SF2; PTHR43336:SF2; 1.
DR   Pfam; PF13185; GAF_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55781; SSF55781; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   4: Predicted;
DR   PRODOM; Q0SKQ1.
DR   SWISS-2DPAGE; Q0SKQ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Kinase {ECO:0000313|EMBL:ABG91885.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000313|EMBL:ABG91885.1}.
FT   DOMAIN       58    205       GAF. {ECO:0000259|SMART:SM00065}.
FT   DOMAIN      226    375       GAF. {ECO:0000259|SMART:SM00065}.
FT   DOMAIN      485    573       HATPase_c. {ECO:0000259|SMART:SM00387}.
SQ   SEQUENCE   573 AA;  61622 MW;  A0763FE4B019BF50 CRC64;
     MTRQPDAGDR GPLLGSLSEL RLRELLAEVQ ERIEQIVDAR DHVDGLLEAM LAVTSGLDLD
     NTLHTIVHAA INLVDARYGA LGVLGPGGGL SEFVFEGIDE ETRERIGDLP RGRGVLGFLI
     TNPKPVRLDD LSHHSASVGF PAEHPPMKTF LGVPIQIRDE VFGNLYLTEK ANGSQFTEDD
     EVLLRALAAA AGIAIENARL YEESRTRQAW LEATREIATE LLAGSETAEV LQVIADDALA
     LTGADSAFLA VPDDPDIPSD EVTELVVTAS AGTVSDRIIG RTIPVDKSTS GEAFRERTPL
     RVTALAFDPG FETGTRFGPA LALPLRAAQS VTGVLVTLRH VDALPFTDDQ LALMSGFADQ
     AAVALQLANS QRRMRELDVL SDRDRIARDL HDHVIQRLFA VGLSLQSTLQ RAKAPIVKQR
     LEQSIDDLHD IVRDIRTAIF DLHGGSGGMT QFRRRLHEIV AETTADSGLR TTVHMSGPLS
     VIDAALADHA EAVLREALSN AVRHAGADTV TVSISVYDDL AIEVADDGKG FVENVVTSGL
     ENLAARAREV NGHFAIDTTP GGGTTLRWTA PLP
//

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