ID A4X649_SALTO Unreviewed; 861 AA.
AC A4X649;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 29-MAY-2013, entry version 51.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
GN Name=pheT; OrderedLocusNames=Strop_1887;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micromonosporineae; Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S.,
RA Udwary D.W., Richardson P.;
RT "Complete sequence of Salinispora tropica CNB-440.";
RL Submitted (APR-2007) 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; CP000667; ABP54349.1; -; Genomic_DNA.
DR RefSeq; YP_001158727.1; NC_009380.1.
DR ProteinModelPortal; A4X649; -.
DR STRING; 369723.Strop_1887; -.
DR EnsemblBacteria; ABP54349; ABP54349; Strop_1887.
DR GeneID; 5058346; -.
DR KEGG; stp:Strop_1887; -.
DR PATRIC; 23442778; VBISalTro43511_1935.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000292086; -.
DR KO; K01890; -.
DR OMA; MKFSEQW; -.
DR ProtClustDB; PRK00629; -.
DR BioCyc; STRO369723:GI49-1917-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 DOMAIN 42 158 tRNA-binding (By similarity).
FT DOMAIN 423 515 B5 (By similarity).
FT DOMAIN 766 859 FDX-ACB (By similarity).
FT METAL 493 493 Magnesium (By similarity).
FT METAL 499 499 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 502 502 Magnesium (By similarity).
FT METAL 503 503 Magnesium (By similarity).
SQ SEQUENCE 861 AA; 90614 MW; D24952831E534A91 CRC64;
MRVSVSWLRE YVDLPAHLTP ADLEQSLVGL GLEVESIVDL AGTVTGPLVV GEVREIEELT
GFKKPIRFCR VDVGDANGTG ELQEIVCGAR NFAVGDRVVV ILPGGVLPGN FAIGARRTYG
RNSRGMICSA KELGLGDDHA GIIVLPGSSP AKPGDDARPV VGLDDVVVEV ELTPDRGYQM
SVRGIARELS HAFGVPFRDP GLASAPAGTE APAYPVEVRD PVGCDRFAAR MVRGVNPAAP
SPAWMVQRLT TAGIRSLSLP VDITNYVMLE LGQPMHAFDA DRITGSLVVR RAVAGEQLTT
LDGVVRTLVA EDMVISDAGL PNPNPAAGAD AGAPISLAAV MGGESSEVVA ETSNVLFEAA
HWDPVMVGRT ARRHRLFSAA AKRWERGVDP ALPLVAIDRA VRLLVEHGGG ATGAEILDID
HRTSPVPVVM PADLPSRRVG VAYPADRVAA LLTEIGCTVA AGPDQLTADP GEVGVAAGGA
VSFVVTPPTW RPDLTDPADL VEEVVRLDGY DRVPAVLPVA PAGRGLTWQQ RRRRAVARML
ADRGYVEVLC SPFVAVELAD QLGLPAGDAR RRAVRLANPL SEEEPALRTT LLGPLLGVLR
RNLGRGQRDL ALYEIGTVFH PRTEAGTPPR MGVEHRPSDA ELAAADAVLP EQPQHVAVVL
AGEVEPGGWW GEGRPAGWAD AVEAARTVLA AAGIPEDRVT VRAVEHAPWH PGRCAQLVVD
GVTVGYAGEL HPAVIAGLEL PRRTAAMELD LDAVPAAPVR QAPVISSFPP ALIDVALVVD
VDVPVAQVQG ALVEGAGELL ESVRLFDVYA GEQLGAGRRS LAYKLTFRAP DRTLTVEEAV
AARDAAVAAV AERFGATLRG V
//
