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Database: UniProt/SWISS-PROT
Entry: SYFB_RHILO
LinkDB: SYFB_RHILO
Original site: SYFB_RHILO 
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   14-MAY-2014, entry version 69.
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; TWSFIAK; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   BioCyc; MLOT266835:GJ9L-3932-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    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
//
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