(data stored in ACNUC9435 zone)

SWISSPROT: SYFB_LISIN

ID   SYFB_LISIN              Reviewed;         802 AA.
AC   Q92CI6;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; OrderedLocusNames=lin1185;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC         L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC         Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
DR   EMBL; AL596167; CAC96416.1; -; Genomic_DNA.
DR   PIR; AH1580; AH1580.
DR   RefSeq; WP_010990817.1; NC_003212.1.
DR   SMR; Q92CI6; -.
DR   STRING; 272626.lin1185; -.
DR   PRIDE; Q92CI6; -.
DR   EnsemblBacteria; CAC96416; CAC96416; CAC96416.
DR   KEGG; lin:pheT.1; -.
DR   eggNOG; ENOG4105C6A; Bacteria.
DR   eggNOG; COG0072; LUCA.
DR   eggNOG; COG0073; LUCA.
DR   HOGENOM; HOG000292087; -.
DR   KO; K01890; -.
DR   OMA; ISYNWLK; -.
DR   OrthoDB; 53568at2; -.
DR   BioCyc; GCF_000195795:LIN_RS06045-MONOMER; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 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_sf.
DR   InterPro; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
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; IPR041616; PheRS_beta_core.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
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   Pfam; PF17759; tRNA_synthFbeta; 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   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;
DR   PRODOM; Q92CI6.
DR   SWISS-2DPAGE; Q92CI6.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..802
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126906"
FT   DOMAIN          40..155
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          409..484
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          709..802
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   METAL           462
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   METAL           468
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   METAL           471
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   METAL           472
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ   SEQUENCE   802 AA;  88192 MW;  D75802193964D7D0 CRC64;
     MLVSYNWVKE FFQDFPLTAE ELGEAITRTG IEIEGVEELS ASLKNVVVGE VLSCERHPDA
     EKLNKCLVQT DEEEPVQIIC GAPNVAAGQK VIVAKVGARL PGGLKIKRAK LRGEVSEGMI
     CSLAELGFES KVVPKAYADG IYVLPEHVET GVSAITLLGL DDAILDMAIT PNRADALSMN
     GVAHEVGAII HQKPAQPTEP DVSEKGKADD FISVEVENPT ETPYYAIKMV ENIEIKESPL
     WLQTKLMKAG IRPHNNVVDV TNYINLLYGQ PLHSFDYDKI GSKKIVVRSA KDQEEITTLD
     GEKRILQTGH TVITNGTEPI AIAGVMGGEF SEVTETTTTV ALEGAIFSSS SVGKASRELY
     LRTEASIRYD KGSDAWKVEK ALAHGGALIA ELSGGTLVGG VVEVDNREKA VNKIETSLTR
     INRILGTEIS LSEIETIFDR LGFVLEVKED TLIIEVPTRR WDITIEADIL EEVARIYGYD
     EIPVTLPATS TTGGLSDSQK ARRVMRAYLE GAGLNQALTY SLTSKKDATR LALSDEKTVA
     LSMPMSEEHS HLRTSIVPQL IRSASYNIAR KNMDVALYEM GTVFYATEGD NLPIEQEHLA
     GLITGNWHTA DWQKTPKPVD FFVLKGIVEG LVNKLGIEAE LHWKQIEKEE LHPGRTASIQ
     LEGKEIGYLG ALHPAVEASY DLKETYVFEI NVKALLDATK EKVVYHPIPR YPEMTRDLAL
     LVDKDTDHAT ISQVIKEHGG NLLVDIELFD IFEGESLGEN KKSLAYTLTF LDSERTLVEE
     DVQKATNKVV EALQAKLHAI IR
//

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