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Database: UniProt
Entry: Q3JT07
LinkDB: Q3JT07
Original site: Q3JT07 
ID   SYFB_BURP1              Reviewed;         810 AA.
AC   Q3JT07;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   19-FEB-2014, entry version 59.
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=BURPS1710b_1896;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000124; ABA48741.1; -; Genomic_DNA.
DR   RefSeq; YP_333296.1; NC_007434.1.
DR   ProteinModelPortal; Q3JT07; -.
DR   STRING; 320372.BURPS1710b_1896; -.
DR   EnsemblBacteria; ABA48741; ABA48741; BURPS1710b_1896.
DR   GeneID; 3689438; -.
DR   KEGG; bpm:BURPS1710b_1896; -.
DR   PATRIC; 19236198; VBIBurPse115837_1977.
DR   eggNOG; COG0072; -.
DR   HOGENOM; HOG000292085; -.
DR   KO; K01890; -.
DR   OMA; MKFSEQW; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   ProtClustDB; PRK00629; -.
DR   BioCyc; BPSE320372:GBYB-1896-MONOMER; -.
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    810       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000232049.
FT   DOMAIN       39    154       tRNA-binding.
FT   DOMAIN      405    480       B5.
FT   DOMAIN      707    809       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   810 AA;  88647 MW;  34B6F7DA6389542C CRC64;
     MQFPESWLRT FVDPQLTTDE LSHALTMAGL EVESLRPAAP PTEKIVVGRV LEVVKHPDAD
     KLNVCQVDAG TGATLQIVCG APNVAPGIKV PVALVGAKLP PAEEGGAPFA IKLSKLRGVE
     SQGMLCSARE LKLSEDHSGL MILPEGTPVG QDIREALNLD DTVFEIKLTP NKADCLSVFG
     IARETAAITG APLAAPDIRP VLAELTETLP VKISAPDLCG RFSGRVIRGV NARAKTPHWM
     VERLERAGQR SVSALVDISN YVMFELGRPS HVFDLDKIHG GIDVRWGKRG ESLKLLNGNT
     IELDETVGVI SDGAQVESLA GIMGGDSTAV TLDTTNIYLE AAFWWPDSIR GRARKYNFST
     DAAHRFERGV DYSTTVEHVE RITQLILDIC GGQAGPVDDQ IVNLPQRAPV SMRASRANRI
     IGVEIGEDEI AQIFTRLGLA FERDGDVFRV TPPPHRFDIE IEEDLIEEVA RIYGFEKIPA
     RPPVAKSEMR ATDETRRSVH AIRHALAARD YAETVNFSFV DAEWERDFAG NDNPVRLLNP
     IASQLSVMRT TLFGSLVGVL RHNLNRRAER VRVFEAGRVF VADPSVKAGE LAVEGYAQPK
     RIGALAYGPV VEEQWGTATR QVDYFDVKGD LEALLAPVPA RFVKAEHPAL HPGRSARIEV
     DGHAVGWIGE LHPRLMQKYE LPHAPVMFEI DTDALVARAL PAPSEVSKFP PVRRDIAVVV
     DQKVEVQALF DEMKKALADD ACKFVQRVAL FDEFRAKSNT SGGLSAHEKS LAFRVTLQDA
     AGTLQDETVD QAIQTLVDRM ARVYGARLRG
//
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