ID SYFB_RHILO Reviewed; 802 AA.
AC Q98CQ1;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 01-MAY-2013, entry version 64.
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=mll5053;
OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB51570.1; -; Genomic_DNA.
DR RefSeq; NP_105784.1; NC_002678.2.
DR ProteinModelPortal; Q98CQ1; -.
DR STRING; 266835.mll5053; -.
DR EnsemblBacteria; BAB51570; BAB51570; BAB51570.
DR GeneID; 1228445; -.
DR KEGG; mlo:mll5053; -.
DR PATRIC; 22482220; VBIMesLot2464_3992.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000292085; -.
DR KO; K01890; -.
DR OMA; MKFSEQW; -.
DR ProtClustDB; PRK00629; -.
DR BioCyc; MLOT266835:GJ9L-3932-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 1 802 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000126936.
FT DOMAIN 38 149 tRNA-binding.
FT DOMAIN 399 474 B5.
FT DOMAIN 708 801 FDX-ACB.
FT METAL 452 452 Magnesium (By similarity).
FT METAL 458 458 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 461 461 Magnesium (By similarity).
FT METAL 462 462 Magnesium (By similarity).
SQ SEQUENCE 802 AA; 85169 MW; 32C01501A34D5241 CRC64;
MKFTLSWLKD HLETDASLDE IVERLTSIGL EVEHVDDKSS LKPFVIAKVL TAVQHPDADR
LRVLTVDTGD GKSPVQVVCG APNARAGLIG AFAAPGTYVP GIDVTLTVGK IRGVESHGMM
CSERELELSD EHNGIIDLPA DAPVGTSFAS YAHLDDPVIE INLTPNRPDA TSVYGIARDL
AASGLGTLKS AAVEKIPGKG ETPVKVVIEA PELCPGFALR LVRGVKNGPS PKWLQQRLIA
IGLRPISALV DITNYVTFDR GRPLHVFDAR KVAGNLVVRR AHDGEKVMAL DGREYTLTPD
MCAIADDNGV ESIAGVMGGE HSGCDENTTD VLIESALWDP ITTARTGRTL GIITDARYRF
ERGVDPEFMV PGVELATRLV LDLCGGEPAE TEVVGYAGHK PKIVSFPISE VTRLTGIEVP
KEESLDILSR LGFKPQGSSE VVDVALPSWR PDVDGKADLV EEVMRIHGVD NIAPQPLGAH
DAVNSKILTT LQVRTRTAKR ALAVRGMMEA VTWSFIPAKH AELFGGGQTA LKLANPIAAD
MSDMRPSLLP GLIAAAQRNA DKGIGDVALF EVSGTYEGDG ADQQRRVAAG VRRGTAKLDG
SGRSWAGNSG PVGVFDAKAD AIAALEACGA PVERLQIEAG GPAWYHPGRS GTIKLGPKTV
LGTFGEFHPK TMEGLDVSGP LCGFEVFVDA VPEPKAKPTK TKPKLELSAF QAVKRDFAFV
VDKAVEAGTL VRAALAADKK LITAVSVFDI FEGASLGADK KSIAIEVSIQ PVEKTLTDED
FEALAKRVVE NVGKQTGGVL RG
//
