(data stored in ACNUC7421 zone)

SWISSPROT: C1AR21_RHOOB

ID   C1AR21_RHOOB            Unreviewed;       330 AA.
AC   C1AR21;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   SubName: Full=Oxidoreductase FAD-binding subunit {ECO:0000313|EMBL:BAH48498.1};
GN   OrderedLocusNames=ROP_02510 {ECO:0000313|EMBL:BAH48498.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48498.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48498.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48498.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011115; BAH48498.1; -; Genomic_DNA.
DR   RefSeq; WP_012687506.1; NC_012522.1.
DR   STRING; 632772.ROP_02510; -.
DR   EnsemblBacteria; BAH48498; BAH48498; ROP_02510.
DR   KEGG; rop:ROP_02510; -.
DR   PATRIC; fig|632772.20.peg.290; -.
DR   eggNOG; ENOG4105DIP; Bacteria.
DR   eggNOG; COG1319; LUCA.
DR   HOGENOM; HOG000244727; -.
DR   KO; K11178; -.
DR   OMA; AFTYERA; -.
DR   OrthoDB; POG091H0E2Y; -.
DR   BioCyc; ROPA632772:GH0Q-250-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; C1AR21.
DR   SWISS-2DPAGE; C1AR21.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212}.
FT   DOMAIN        1    222       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   330 AA;  35135 MW;  B96F9ED57CA7DC13 CRC64;
     MIPFDYERAS DVDSAVATVT ADPGASYLAG GTNLVDHMKL GVARPHLLVD VSRLPLDDVE
     ALPGGGLRIG AAVRNSDLAA HEVVRARYPM LSRALLSGAS GQLRNLATTA GNLLQRTRCV
     YFQDVTTPCN KREPGTGCSA LGGYVRYHAI LGASEHCVAV HPSDMAVAMT ALDAVVVVRT
     ADGERRIPLR EFYVLPGDRP DRDTVLGHGD LVTAVELPAP PAGNRSTYRK VRDRASFAFA
     VTSVAAELTV DDRSITSARV ALGGVAHRPW RATRAEEVLL GSPPTENTFT AAAEAELAAA
     QPLPGTEFKV VLTRRVLVSV LRSLAEEARR
//

If you have problems or comments...

PBIL Back to PBIL home page