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SYFB_BLOFL
ID   SYFB_BLOFL              Reviewed;         803 AA.
AC   Q7VR66;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Bfl356;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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}.
CC   -!- CAUTION: Lacks 2 conserved residues that bind magnesium; the aspartate
CC       residue in position 464 is replaced by an asparagine and the glutamate
CC       residue in position 467 is replaced by a serine residue. {ECO:0000305}.
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DR   EMBL; BX248583; CAD83423.1; -; Genomic_DNA.
DR   RefSeq; WP_011126631.1; NC_005061.1.
DR   AlphaFoldDB; Q7VR66; -.
DR   SMR; Q7VR66; -.
DR   STRING; 203907.Bfl356; -.
DR   EnsemblBacteria; CAD83423; CAD83423; Bfl356.
DR   KEGG; bfl:Bfl356; -.
DR   eggNOG; COG0072; Bacteria.
DR   HOGENOM; CLU_016891_0_0_6; -.
DR   OMA; ISYNWLK; -.
DR   OrthoDB; 53568at2; -.
DR   Proteomes; UP000002192; 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; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_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   PANTHER; PTHR10947; PTHR10947; 1.
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   SUPFAM; SSF55681; SSF55681; 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; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN           1..803
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000232797"
FT   DOMAIN          40..150
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          405..480
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          710..803
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         468
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ   SEQUENCE   803 AA;  91364 MW;  8C1228871DDA5C55 CRC64;
     MKFSESWIRE WVNPPIDHDQ LIDQFTLAGL NVEESRKLNS NKFYGIVIAK IIECQVHPSL
     ADTWIMTVNS GGGNIINIIT NNMNYNKNTK VVVANIGAIL PNGNIIKQIN IQGRKSEGVL
     CTFSMLGLNY YTQKGIIELP IDAPIGCNFY DYLHFNDNII DINITPNRGD CLSVIGLSRE
     IAAINQCKLK KINIKSNVPN ILDTIPIIIE TPHDCPKFLG KVLKNIDITI PTPLKIQEKL
     IRCGIQPINI ITDIANYVLL ELGQPVRIFD YEKIDKNIIY VRFSKPGETL TLSENNINIK
     LFSKTLVISD VRKPLAIAGV ITGNQSSVSC STHNIFLKVA FFNPLTIINQ YKLYNLYTSS
     VVRYEKGIDP DISELALNYA TSLLIKYCHG KAGPTINIIS HNHLPKIKII KLHRSKLNMI
     LGFYIPDQKI INILTNLGFQ VETQGHNWIV STPSWRFDIN IEENVISEII RIYGYNHIPK
     IPAKISLNQT VQCIPNQVIS LSKSKTVLIA RGYQEIITYS FVDPNIQKLL HPQCIPLTLM
     NPISTNMSVM RLSLWTGLIQ TMLYNQNRQH KNIKLFESGI CFIPKNSHSK QVSQQLRLSG
     IRSGLRHYEH WDIHTSLTDF YDIKGDVESI LYLFNKKNQN NNIHFKSCTY PALHPGQSAE
     IYLNDIFLGY VGVIHPMIQY KLRIHSNVLV FELIWDSIVN IKSQKIIDIS KFPKNYRDIS
     LIIPTHISAS SVIETCKKIG IINLTEVKLI DVYTGRNIPT NFKSLTIKLT LQSKTHTLKE
     QEIKEIIIIC TTTLKKHFNA IFR
 
 
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