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 01-MAY-2013, entry version 53.
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 JMP134 / LMG 1197) (Alcaligenes
OS eutrophus) (Ralstonia eutropha).
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 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: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 1 815 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
//
