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Database: UniProt
Entry: Q6MMJ1
LinkDB: Q6MMJ1
Original site: Q6MMJ1 
ID   SYFB_BDEBA              Reviewed;         813 AA.
AC   Q6MMJ1;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   19-FEB-2014, entry version 65.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   Name=pheT; OrderedLocusNames=Bd1638;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529
OS   / HD100).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F.,
RA   Sockett R.E., Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 B5 domain.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; BX842650; CAE79513.1; -; Genomic_DNA.
DR   RefSeq; NP_968520.1; NC_005363.1.
DR   ProteinModelPortal; Q6MMJ1; -.
DR   STRING; 264462.Bd1638; -.
DR   EnsemblBacteria; CAE79513; CAE79513; Bd1638.
DR   GeneID; 2735391; -.
DR   KEGG; bba:Bd1638; -.
DR   PATRIC; 21077820; VBIBdeBac73187_1486.
DR   eggNOG; COG0072; -.
DR   HOGENOM; HOG000292085; -.
DR   KO; K01890; -.
DR   OMA; MKFSEQW; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.56.20; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR   InterPro; IPR005121; PheS_beta_Fdx_antiC-bd.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF56037; SSF56037; 1.
DR   TIGRFAMs; TIGR00472; pheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN         1    813       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000126848.
FT   DOMAIN       42    151       tRNA-binding.
FT   DOMAIN      405    480       B5.
FT   DOMAIN      720    813       FDX-ACB.
FT   METAL       458    458       Magnesium (By similarity).
FT   METAL       464    464       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       467    467       Magnesium (By similarity).
FT   METAL       468    468       Magnesium (By similarity).
SQ   SEQUENCE   813 AA;  89251 MW;  43825873FDA49446 CRC64;
     MKISLKWLHD YVDVTEFFQK PEVLAEALTR GGLEVEEITN RAKDFNHVVI GHILEKDKHP
     NADKLSLCRV STGEGVVHQI VCGAQNHKAG DRVIVALPGA VLPGNFAIKK SAVRGVDSAG
     MLCSLKELGL ATESEGIAIL PADAPVGKAY AEYGGYDDVT FELKVTANRA DCLSHFGLAR
     EVSTLFGKEL KVPSSELKTN GKSSKSEIAL DVKAFDLCPR YAGRFLKGVK VGPSPAWLKA
     RLESVGMNSI NNIVDVTNYV MLELGQPLHA FDAAFINGKK IIVDRAVAGE KFITLDGTEI
     ALNGAELTIR DVNHPVCLAG VVGGKNSGVS DSTTEVFLEA AYFLPMSARK TSRSHGIDTD
     SSYRFARGVD PDGTLRGLNR AAALILEVAG GEAYADHHDF YPNPVKKAPV DITIKTVSDR
     LGYEAEEHKF VDFMKRLGCE INKKGETFTV LPPTFRFDIE QDMDLVEEYA RLNGYEHIPE
     ALPALAAAPS FQDKTFMLNR TTSELLRGEG FQQAVNFAFV GSKAQKAFLG SLEALKATGL
     AATEKEIRIL NPLNEEMDVM RSSLSFGLFK NLNHNFHSGN MQGRLFEIGS TFFVKDDGSF
     AEGSRAGMAI WGRASNLWNK SLDYPVVYEL KAAVEVLLKS LNISSYTWVT PANKSEVPEF
     LHQGQFAQLL VEGKKVGFIG TLHPLLLEDN KIRVPAALAE LDLDQLYKGQ PRPYRIQSVS
     KFPIVERDFA FVMPKALKVG DVLKDIRKAG AGLLLNVDVF DLYEGEKMEA GKKSVAIRIW
     LQDKNATLQE TQINETTTKI LESLKKNFDL SVR
//
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