(data stored in SCRATCH zone)

SWISSPROT: Q0SK67_RHOJR

ID   Q0SK67_RHOJR            Unreviewed;       855 AA.
AC   Q0SK67;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   SubName: Full=Probable non-ribosomal peptide synthetase {ECO:0000313|EMBL:ABG92069.1};
GN   OrderedLocusNames=RHA1_ro00233 {ECO:0000313|EMBL:ABG92069.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92069.1, 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).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000256|SAAS:SAAS00542384}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00258}.
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DR   EMBL; CP000431; ABG92069.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0SK67; -.
DR   STRING; 101510.RHA1_ro00233; -.
DR   PRIDE; Q0SK67; -.
DR   EnsemblBacteria; ABG92069; ABG92069; RHA1_ro00233.
DR   KEGG; rha:RHA1_ro00233; -.
DR   eggNOG; ENOG4105UWE; Bacteria.
DR   eggNOG; ENOG410XPD8; LUCA.
DR   HOGENOM; HOG000229993; -.
DR   OMA; IVHWKEV; -.
DR   OrthoDB; POG091H088I; -.
DR   BioCyc; RJOS101510:GJJ1-233-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0SK67.
DR   SWISS-2DPAGE; Q0SK67.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Ligase {ECO:0000256|SAAS:SAAS00542462};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN      776    846       Carrier. {ECO:0000259|PROSITE:PS50075}.
SQ   SEQUENCE   855 AA;  91633 MW;  EDD254E04D616898 CRC64;
     MQYLDQVADL VVVADRRDLD TASLTLVCDV LVGVRDADTV TANPVGRHRH GRALGGWSAE
     VLRSSHPLVA AREDMTATVA AAAAVVTGRR DDLSVVTVPV WRVDRTRPPR MLGGFENWVD
     LAFHTSLDRT LAELAEEVKC SRQQEVSWES VKIGEMRSTA TGVLGTVTRD TGREYLPCQT
     APFPLTLVPV ADTGGHATLE VYADPVSVDA DTAARFGQWV ARVVNGLRDP SPRRRRVFGA
     AVAPVGAGVR APVSGGRIED LVVRQAHERP DAVAVTHGRR TLTYRALEEQ SAWMARGLHD
     RGVGPGDRVG ICVDRSVDLV VTMLAVLRSG AAFVPMDVRH PPDRLAYTAR DAGVRLVVTE
     LQGEARWAGV PAVTPAELPG SVSGPGEVDW AVGGDGAPAY VVYTSGSTGR PKGVVIPHRA
     VPALMSATAT EFAPTPGDTW SMFHSPAFDF SVWEIWGSLS TGGRLVIVPY WISRSPVEFH
     TLLADERVSV LSQTPSAFVL LAAADRDLEP LSALRLVVFG GETLDPRVVL PWLDRYPESR
     CRLVNMFGTT ETTVHVTAHT VTRRDALTGS RTVGKPLPGW EMAVADEFGD PLPNGLTGEI
     YVGGAGVALG YLDRAGLTAC RFVAAPGGSR WYRTGDRGRI CDDGTLEHLG RLDTQVQIRG
     FRVELDEVRS VLLDDPVVTA AAVVPSGRPE DPAGIALDAY VVPGGSAAAG GTETVAAIRE
     RAARFLPEHM VPRSITLVDA LPLTINGKID VARLPAPAPR SLPHNVVEPQ DGGPLTDAGT
     AHMLTDIWES VLGVPVSLDD NLFELGGNSL CAIKADSMMR RLGLPALPMR ELYRHPSIRG
     ICGTLARLYL PRPDR
//

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