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Database: UniProt
Entry: Q472N3
LinkDB: Q472N3
Original site: Q472N3 
ID   SYFB_CUPPJ              Reviewed;         815 AA.
AC   Q472N3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   19-FEB-2014, entry version 58.
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=Reut_A1280;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia
OS   eutropha (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
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.
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DR   EMBL; CP000090; AAZ60650.1; -; Genomic_DNA.
DR   RefSeq; YP_295494.1; NC_007347.1.
DR   ProteinModelPortal; Q472N3; -.
DR   STRING; 264198.Reut_A1280; -.
DR   EnsemblBacteria; AAZ60650; AAZ60650; Reut_A1280.
DR   GeneID; 3609271; -.
DR   KEGG; reu:Reut_A1280; -.
DR   PATRIC; 20228057; VBIRalEut24049_1898.
DR   eggNOG; COG0073; -.
DR   HOGENOM; HOG000292085; -.
DR   KO; K01890; -.
DR   OMA; MKFSEQW; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   ProtClustDB; PRK00629; -.
DR   BioCyc; CPIN264198:GIW3-1290-MONOMER; -.
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    815       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000232081.
FT   DOMAIN       40    155       tRNA-binding.
FT   DOMAIN      406    485       B5.
FT   DOMAIN      712    814       FDX-ACB.
FT   METAL       463    463       Magnesium (By similarity).
FT   METAL       469    469       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       472    472       Magnesium (By similarity).
FT   METAL       473    473       Magnesium (By similarity).
SQ   SEQUENCE   815 AA;  89706 MW;  0024894E7F4F5BE1 CRC64;
     MQFSESWLRT FANPEKISTD ALSHSLTMAG LEVEEVGPVA PPFDKIVVAH VLSTERHPNA
     DRLNVCQVDA GTGETLQIVC GAPNVKPGIK VPCALVGAVL PPAEAEGKPF EIKVGKLRGV
     ESYGMLCSAR ELKLSEDHGG LLVLPEDAPV GQNIREYLDL DDQVFIIKLT PNKADCLSIH
     GVAREVSALT GATLTLPDMK PVAVTIDDKL PVKVSAPDLC GRFSGRVIRG VNARAATPAW
     MVQRLERSGQ RSISAMVDIS NYVMLELGRP SHVFDLDKIH GGLDVRWGRK GEQIKLLNGN
     TIEVDEQVGV IADDKEIESL AGIMGGDSTA VTLDTTNIYL EAAFWWPSAI QGRARRYNFS
     TDAAHRFERG VDYATTVEHI ERITALILEI CGGQAGPVDD HIVNLPQRRP VSLRLARAER
     VLGIELSSAV VADVFQRLQL PFTRSQGADG EVFEVTPPSY RFDIEIEEDL IEEVARIYGF
     ERIAARPPVA ESEMRPTNEG RRSTHVVRHA LAARDYQEVI NFAFVEEKWE RDFAANDNPI
     RLLNPIASQL AVMRSSLIGG LLDKVRYNLN RKAARVRLFE VGRVFHRDAD VKDGGLTVAG
     YHQPMMAAGI AYGPAFEEQW GITTRNVDFF DVKGDVETLF YPRVARFEPV EHPALHPGRA
     ARMLIDGKPV GVVGEMHPRW LQEYELTQAP VLFELELDAL REAGLPTYAE ISKFPAAVRD
     LAVVVKQSVR VQDMLDSMRA ALDKQGCGRF CQSLVLFDEF RPKAASAAIG ADEKSLAFRV
     TLQDTGSTLQ DETVDSAVRC MVDALGEAFQ ARLRG
//
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