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Database: UniProt
Entry: Q3B4Z2
LinkDB: Q3B4Z2
Original site: Q3B4Z2 
ID   SYFB_PELLD              Reviewed;         804 AA.
AC   Q3B4Z2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-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=Plut_0711;
OS   Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM
OS   273)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-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; CP000096; ABB23589.1; -; Genomic_DNA.
DR   RefSeq; YP_374632.1; NC_007512.1.
DR   ProteinModelPortal; Q3B4Z2; -.
DR   STRING; 319225.Plut_0711; -.
DR   PRIDE; Q3B4Z2; -.
DR   EnsemblBacteria; ABB23589; ABB23589; Plut_0711.
DR   GeneID; 3745839; -.
DR   KEGG; plt:Plut_0711; -.
DR   PATRIC; 21378944; VBIChlLut1287_0744.
DR   eggNOG; COG0072; -.
DR   HOGENOM; HOG000292087; -.
DR   KO; K01890; -.
DR   OMA; MKFSEQW; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   ProtClustDB; PRK00629; -.
DR   BioCyc; PLUT319225:GHDM-726-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    804       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000232073.
FT   DOMAIN       40    153       tRNA-binding.
FT   DOMAIN      400    476       B5.
FT   DOMAIN      710    802       FDX-ACB.
FT   METAL       454    454       Magnesium (By similarity).
FT   METAL       460    460       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       463    463       Magnesium (By similarity).
FT   METAL       464    464       Magnesium (By similarity).
SQ   SEQUENCE   804 AA;  86445 MW;  790D346B82474775 CRC64;
     MKISVNWLKD FLPSFSPDIT SLVEKLTFLG LEVEDVESTP LPDLRVVVGR VQSVALHPDA
     DRLRICMVDT GLEEPLQIVC GAPNVAEGML VPVATEGSRL TMQDGTSFVI KPSKIRGQRS
     FGMICAADEL GLSADHSGVM ELDSSYAVGE PFARYLDSDT VLDIAVTPNR PDVLSHLGIA
     RELGSAPDAI LFPEEAPLEF SADSPLVQVM DSGACPLYVG VIIRGVTVGP SPRWLSARLE
     SIGLRPKNNI VDITNFILHA LGQPLHAFDL QKLKGGRVIV RSDFSGSFTT LGAEQCTVEP
     GMPVICDTQM PVALAGVMGG LDSAVGEGTV DILLEAACFA PSAVRRSARK AGISSDSSYR
     FERGIDIRNV LPAARAAVAL ILETAGGTVG EATLQGDPSP ALLVLPFRPR RANELLGTAI
     ETDAMQAMLA RIGFRTLALD EGVMQVEVPS CRIDVLQEID LIEEVARLHG YDNIEASGRL
     AATYPASRTR PGYFPDFLRG VAVGLDFREV LTNPLIRREE AAPFGDGLVS VLNPISEGLE
     VLRPGLVPGM LKVIAHNIRH GNRDMRLFEV AHGFSVADPS GAAEQGPLGA YCEKEWLVLA
     LTGNRYPRSW NQPPDRVDFY DAVGAAEMLL GKLNLLDKSA VNIYNENTVS IDLELTEGKK
     KRSQRAGRAM RLDSALLSQF GIEQDVFTVE LDVSVLEMLY SPDVVYDPPS KFPAVQRDLS
     FILPGTVPVQ SLVGLVRSSD PLIRDVSVFD VFERGSGGGG ERSVGLSISI ADHSGTLQEG
     RISEILRTVG VNAESKLGAV IRQV
//
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