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Database: UniProt
Entry: Q6NHH1
LinkDB: Q6NHH1
Original site: Q6NHH1 
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   19-FEB-2014, entry version 72.
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   OrthoDB; EOG6CCH1J; -.
DR   ProtClustDB; PRK00629; -.
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    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
//
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