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 29-MAY-2013, entry version 55.
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.
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; 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 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:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA: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_bac.
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; SSF56037; B3_4; 1.
DR SUPFAM; SSF54991; Fdx_AntiC_bd; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF46955; Putativ_DNA_bind; 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
//
