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SYFB_BORT9
ID   SYFB_BORT9              Reviewed;         564 AA.
AC   A1QZU9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=BT0514;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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_00284};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284}.
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DR   EMBL; CP000049; AAX17841.1; -; Genomic_DNA.
DR   RefSeq; WP_011772459.1; NC_008710.1.
DR   AlphaFoldDB; A1QZU9; -.
DR   SMR; A1QZU9; -.
DR   STRING; 314724.BT0514; -.
DR   KEGG; btu:BT0514; -.
DR   eggNOG; COG0072; Bacteria.
DR   HOGENOM; CLU_020279_3_0_12; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 53568at2; -.
DR   Proteomes; UP000001205; 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:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947; PTHR10947; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00471; pheT_arch; 1.
DR   PROSITE; PS51483; B5; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..564
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_1000199335"
FT   DOMAIN          286..362
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT   BINDING         350
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
SQ   SEQUENCE   564 AA;  64351 MW;  23CCF94A3188227E CRC64;
     MPKVEIYKSI LLEKIGKILT KSELVSVLEM AKAEICEFDT VNDKIKIEFN DTNRPDLWSC
     AGLARQIKTY LFGHLPLFKF FSMADNLQEF YGEILVSPEV FSIRPFIFGF LAKGVICNER
     MLETLIQLQE KLCHNYGQKR KRVAMGMYSS DLIEFPLSYT ACNSDYRFIP LGMDREMSIE
     EINRVHSKGI EYSTILASFN KYPLLLDDKD KVLSYPPVIN SHDIGALKVG DTDLFIEVTG
     TNLEATLLSL SVTACDLHDM GFEILPVKTI FPNETLFGKE IICPYYFQNM LEVNVDNVNK
     MLGSNFTANN MCLDLKKLGI SAYFKELDKF YVIPPVYRND FLHEVDVIEE IMIGMGLDSF
     KPELPKDFTL GRLSQIEEFS RKIKNLMIGM GFQEMIYNYL GSRTDFIEKM NIEGDDFLSV
     ANPMTEGYEY IRGSIVSDLL KSESISSNFP YPHKIFEIGK VALKDLNSVD GTITYDNLAF
     LMADKEFSFN EINSLVSSLF YYLNIEFKLR ESSKSLYIDG RGVDILINDT VLGGFGEVSP
     YILRNFGIMV PCCVLEINLN KLLN
 
 
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