ID E8UQR0_THEBF Unreviewed; 792 AA.
AC E8UQR0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 18.
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=Thebr_0795;
OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389
OS / AKO-1) (Thermoanaerobacter finnii).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=509193;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL Submitted (JAN-2011) 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; CP002466; ADV79383.1; -; Genomic_DNA.
DR RefSeq; YP_004185766.1; NC_014964.1.
DR ProteinModelPortal; E8UQR0; -.
DR EnsemblBacteria; ADV79383; ADV79383; Thebr_0795.
DR GeneID; 10163052; -.
DR KEGG; tbo:Thebr_0795; -.
DR PATRIC; 47039535; VBITheBro57020_0817.
DR HOGENOM; HOG000292087; -.
DR KO; K01890; -.
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 37 150 tRNA-binding (By similarity).
FT DOMAIN 402 477 B5 (By similarity).
FT DOMAIN 699 792 FDX-ACB (By similarity).
FT METAL 455 455 Magnesium (By similarity).
FT METAL 461 461 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 464 464 Magnesium (By similarity).
FT METAL 465 465 Magnesium (By similarity).
SQ SEQUENCE 792 AA; 88484 MW; D24F4628544AD33B CRC64;
MSLSWLKEFV DIDEDAKAIA EGLTMSGSKV ETITSYGKEI SNVVVGKIIS LEKHPNADKL
LVGIVDVGTE KLQIVTGAQN IKVGDYIPVA LHGATLPGGV KIKRGKLRGI ESNGMMCSAE
ELGLDESLLP EYQRNGIFIL PPFPLGMDIN EALQLKDDVL EFEITPNRPD CLSMVGIARE
VAATFKKKFK MPVVEVNESE KQNPAKVTIE ATDLCFRYVA RVVKNVKIGP SPMWMQMRLL
KAGIRPINNV VDVTNYVMLE LGQPLHAFDL DKVENKHIIV RRAKEGEKLV TLDGKERTLD
SSMLVIADEK EAIGLAGVMG GENTEITDTT VNILIESANF KGSNIRHTSK KLGLRSEASS
RFEKGLDPEI TVLACERAAQ LMEKYCGGTV LKGLVDEYPK PIEKTVLTVN PHRINRFLGT
ELPTSQMIEI LESLEFKVLQ KGDDLEITVP HFRRDVTMEA DIAEEIARLF GYNNIQDSLM
KNAQTTLGAM TKEQELEEKI KEVLLVCGLN EIVTISFMGS KDLDKINVPL DSPLRKAVKI
INPLGEDQSL MRTTLLPFIL NVAYTNYSRK VQDFKVFEIS KVFMPKELPL KELPQEIKTI
AIGMYGKDVD FYSLKGVIEA LFEVMGIKGV EYVRAEDPSY HPGRSAKILL GDETLGIFGE
IHPDVLENYD IPVRVYGGEI NLDKVIQYAN VEKRYMPLPK YPAVERDIAV LVDRDIFVKD
VEKVILETGG KLIDKVELFD VYKGPNIPEG KKSVAFSIWY RSYERTLTDE EVNVIHNNIV
EALDKKLGAK LR
//
