(data stored in SCRATCH zone)

SWISSPROT: Q13EI5_RHOPS

ID   Q13EI5_RHOPS            Unreviewed;       438 AA.
AC   Q13EI5;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   16-JAN-2019, entry version 72.
DE   SubName: Full=FolC bifunctional protein {ECO:0000313|EMBL:ABE37504.1};
GN   OrderedLocusNames=RPD_0264 {ECO:0000313|EMBL:ABE37504.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37504.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37504.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37504.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; CP000283; ABE37504.1; -; Genomic_DNA.
DR   RefSeq; WP_011500694.1; NC_007958.1.
DR   STRING; 316057.RPD_0264; -.
DR   EnsemblBacteria; ABE37504; ABE37504; RPD_0264.
DR   KEGG; rpd:RPD_0264; -.
DR   eggNOG; ENOG4105DPM; Bacteria.
DR   eggNOG; COG0285; LUCA.
DR   HOGENOM; HOG000019980; -.
DR   OMA; KCDYAVI; -.
DR   OrthoDB; 1232874at2; -.
DR   BioCyc; RPAL316057:RPD_RS01335-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR11136; PTHR11136; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01499; folC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EI5.
DR   SWISS-2DPAGE; Q13EI5.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001563};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT   DOMAIN       37    262       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      293    362       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
SQ   SEQUENCE   438 AA;  46803 MW;  2962E252D8EC32D3 CRC64;
     MFDLPKYGEG ICLARLAVLL DRLGVDRARL QRIAVAVCGS NGKGSTAAFT AGIGRAHGLR
     TGLFTSPHLY RFNERFQIDG APIPDDALRR LLERVTKAIA EVGEARGEQF GAFEAQFALA
     CLYFQDNACD FAVFEAGIGG RYDPVRLLGA RVSCVTSVDL EHVALLGHSI ELIASDKSDA
     CAAGGVIVYG ENCRPLRDHL AEYNRNREVA ALFIGDEIGI GSASIADARQ RFDLRIEDHT
     YVALETSLLG PFQVNNAAIA ASLFALWLRQ SGTDHDPARL DAAIRHGLRD ARWPGRLETI
     STEPLTVIDV GHTPDGIRQA LAGLRAAHGE SGWILVLGAS RDKNAAEIVA ALAPSFDAIV
     CSSAHHKGAP AEVIAEAARA ANPRAEIVTA ATVADAVGEA RMLAERLDAR IYVAGGLFLA
     IEFAAVTRGG RAEDLRFF
//

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