(data stored in ACNUC7421 zone)

SWISSPROT: Q0SKM5_RHOJR

ID   Q0SKM5_RHOJR            Unreviewed;       228 AA.
AC   Q0SKM5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   SubName: Full=Phosphatidic acid phosphatase, type 2 {ECO:0000313|EMBL:ABG91911.1};
DE            EC=3.1.3.- {ECO:0000313|EMBL:ABG91911.1};
GN   OrderedLocusNames=RHA1_ro00075 {ECO:0000313|EMBL:ABG91911.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG91911.1, 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; ABG91911.1; -; Genomic_DNA.
DR   RefSeq; WP_011593404.1; NC_008268.1.
DR   ProteinModelPortal; Q0SKM5; -.
DR   STRING; 101510.RHA1_ro00075; -.
DR   PRIDE; Q0SKM5; -.
DR   EnsemblBacteria; ABG91911; ABG91911; RHA1_ro00075.
DR   GeneID; 4219498; -.
DR   KEGG; rha:RHA1_ro00075; -.
DR   PATRIC; fig|101510.16.peg.92; -.
DR   eggNOG; ENOG410841Q; Bacteria.
DR   eggNOG; COG0671; LUCA.
DR   HOGENOM; HOG000098132; -.
DR   OMA; LYLGYHW; -.
DR   OrthoDB; POG091H06SO; -.
DR   BioCyc; RJOS101510:GJJ1-75-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.144.10; -; 1.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   4: Predicted;
DR   PRODOM; Q0SKM5.
DR   SWISS-2DPAGE; Q0SKM5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Hydrolase {ECO:0000313|EMBL:ABG91911.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     54     79       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     86    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    149       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    161    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    186    204       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       86    201       acidPPc. {ECO:0000259|SMART:SM00014}.
SQ   SEQUENCE   228 AA;  23104 MW;  2C877528C41AEB42 CRC64;
     MPHTSIATAG LRVSALTLIL AVLCVQVRDG GPLTGADVPA TSWVVGHRSA TLDHVALLVT
     ALGSPVATVA LAVICGLALA WRRRSAIPAA VVVGTVGAAT AASTALKLVV ERSRPAVDLQ
     EVLETDYSFP SGHVTGTAAL LGVTAAILLG RRHLRVRVCG AAVAGCGVVI VAVTRVYLGV
     HWMSDVVAGA ILGAVFVTVG AATYERVHRP LVAVAPSKPL AVLDRVGG
//

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