ID SYFB_CORDI Reviewed; 836 AA.
AC Q6NHH1;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 66.
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=DIP1166;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L.,
RA Whitehead S., Barrell B.G., Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium
RT diphtheriae NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248357; CAE49686.1; -; Genomic_DNA.
DR RefSeq; NP_939523.1; NC_002935.2.
DR ProteinModelPortal; Q6NHH1; -.
DR STRING; 257309.DIP1166; -.
DR DNASU; 2648566; -.
DR EnsemblBacteria; CAE49686; CAE49686; DIP1166.
DR GeneID; 2648566; -.
DR KEGG; cdi:DIP1166; -.
DR PATRIC; 21483519; VBICorDip47633_1148.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000292086; -.
DR KO; K01890; -.
DR OMA; MKFSEQW; -.
DR ProtClustDB; PRK00629; -.
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 1 836 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000126873.
FT DOMAIN 44 160 tRNA-binding.
FT DOMAIN 420 495 B5.
FT DOMAIN 742 835 FDX-ACB.
FT METAL 473 473 Magnesium (By similarity).
FT METAL 479 479 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 482 482 Magnesium (By similarity).
FT METAL 483 483 Magnesium (By similarity).
SQ SEQUENCE 836 AA; 89783 MW; 1E0EF6FDA17AB650 CRC64;
MLISQNWVTE LLGRSNPDWK VSPAELDSGY VRVGFETEGY SAIPETTGPL VIGRVETIEE
LEGFKKPIRH CFVNVGDANG TGELQSIVCG ARNFQEGSYV VVSLPGAVLP GNFAISARET
YGRMSAGMIC SAAELGLSDK QNSGIITLPN EIAEPGTDAR SIVGLDDTVF DVNITPDRGY
ALSARGLTRE LASAFNLKFV DPAVDLNVAG VDTSDVPESS GELIKVDLRP ETQARRFGVR
KVSGIDPKAP TPFWMQRELM LSGQRCVNAA TDVTNFVMLL LGQPMHAFDA NLIKGGLVVR
NALEGESFET LDHVKRTLSA EDVVISDDTG IQSLAGVMGG TTSEISDETT DVFFEAANWH
PITTARTSRR HKLSTEASRR FERGVDPEII EVALDVACAL LVSIAGGSVE SARTLIGSAP
SMPQIRMKTS RPAELAGVAY SDATVIARLK EVGCAVEVDG DDLLVTPPTW RPDMTMSADL
VEEVLRLEGL EDIPTIVPLA PVGSGLSPAQ LRRRAIGHAL AYSGYAEILP TPFIRNDTFD
VWGLAADDER RSVVTVQNPL DAEYGVLATT LLPSMLEAVT RNVSRGQTSV NLFGLQQVSF
KRGSGISPML DVRQRPSDNE VAELLNSLPV QPLHVATVGA GFMELEGPWG HGRTYSFADA
IESARVVARA AGVELNVENV EMLPWHPGRC AALKAGDHIV GYAGELHPQI VEALNLPART
CAMELDVSAL PLKESFPAPV LSAFPVLHQD LALVVDESVP AESVRKVIED AAGELLEKVE
LFDVYRSEAL GAEKKSLAFS LEFRAQDRTL TDDECSEGRL AAAGRAAELF GATMRA
//
