(data stored in SCRATCH zone)

SWISSPROT: Q0SKE2_RHOJR

ID   Q0SKE2_RHOJR            Unreviewed;       551 AA.
AC   Q0SKE2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   SubName: Full=Probable metal-dependant glycoprotease {ECO:0000313|EMBL:ABG91994.1};
GN   OrderedLocusNames=RHA1_ro00158 {ECO:0000313|EMBL:ABG91994.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG91994.1, 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; ABG91994.1; -; Genomic_DNA.
DR   RefSeq; WP_011593475.1; NC_008268.1.
DR   ProteinModelPortal; Q0SKE2; -.
DR   STRING; 101510.RHA1_ro00158; -.
DR   PRIDE; Q0SKE2; -.
DR   EnsemblBacteria; ABG91994; ABG91994; RHA1_ro00158.
DR   GeneID; 4219366; -.
DR   KEGG; rha:RHA1_ro00158; -.
DR   PATRIC; fig|101510.16.peg.183; -.
DR   eggNOG; ENOG4105EFZ; Bacteria.
DR   eggNOG; COG1574; LUCA.
DR   HOGENOM; HOG000064644; -.
DR   OMA; WAAHEPQ; -.
DR   OrthoDB; POG091H0C1E; -.
DR   BioCyc; RJOS101510:GJJ1-158-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 2.30.40.10; -; 2.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 2.
PE   4: Predicted;
DR   PRODOM; Q0SKE2.
DR   SWISS-2DPAGE; Q0SKE2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Hydrolase {ECO:0000313|EMBL:ABG91994.1};
KW   Protease {ECO:0000313|EMBL:ABG91994.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN       52    546       Amidohydro_3. {ECO:0000259|Pfam:PF07969}.
SQ   SEQUENCE   551 AA;  58776 MW;  2FAA5B31B2BF0983 CRC64;
     MSAEPADLVF TGGSIATLDP ARSRATTVAV TGGRISAVGH DEVRELIGSR TEVVDLTGRL
     LLPGFQDAHI HPVVAGLEYA RCNLTGTSDA AGTLAAIRSY ADAHPELPWI VGGGWSMEAF
     DGGTPTAQLL DTVVRDRPVF LPNRDHHGAW ANTRALDLAG ITRDTPDPVG GRIERDADGL
     PTGMLQESAM ELVGCHTPQH TPDDRLKALL HAQQHLHSLG ITAWQDALLG DTSGISDVSD
     AYLSAAGDGS LTARVAGALW WDRDRGAEQI PDLLRRRSLL RVGRMRADTV KIMLDGVAES
     RTAAMISPYL DGCGCATAHS GTSFVDPDEL RGYVTELDAL GFQVHFHALG DRAVRDALDA
     VDAARTANGF RDTRPHLAHL QVVDPDDIPR FRALGVTANM QPLWAAHEPQ MDELTIPFLG
     DERSRRQYPF GSLLRSGATL AAGSDWPVSS ADPIHGIHVA VNRVLPGRDG QGRPVFLPEQ
     RIDLTAALTA YTAGSAYVNH LDDTGSIEVG KLADLVVLDR DPFTGTADEI GGSRAVLTYV
     GGNRVYSAPD A
//

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