位置:首页 > 蛋白库 > SYR_FLAJ1
SYR_FLAJ1
ID   SYR_FLAJ1               Reviewed;         592 AA.
AC   A5FND6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=Fjoh_0251;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000685; ABQ03287.1; -; Genomic_DNA.
DR   RefSeq; WP_012022357.1; NZ_MUGZ01000005.1.
DR   AlphaFoldDB; A5FND6; -.
DR   SMR; A5FND6; -.
DR   STRING; 376686.Fjoh_0251; -.
DR   EnsemblBacteria; ABQ03287; ABQ03287; Fjoh_0251.
DR   KEGG; fjo:Fjoh_0251; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_10; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..592
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076215"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   592 AA;  67140 MW;  ECCEE9EBDB971A24 CRC64;
     MSLSQILTPS IQKAIQVLFD VSVDKIEFQT TRKEFEGDIT MVIFPLLKVI KSNPAELGNK
     IGTYLVENVS EVARFNVVSG FLNIVISDSY YVDFFNGIKD QKQFGFLSPN PEEKAVMVEY
     SSPNTNKPLH LGHVRNNLLG YSVAEILKAS GKKVYKTQII NDRGIHICKS MLAWEKFGNG
     ETPESSDLKG DKLVGKYYVE FDKAYKTEIN QLIETGKTEE EAKKQAPIII EAQEMLKKWE
     AGDEQVIALW KKMNQWVYDG FATTYTNLGV NFDKYYYESN TYLLGKDVVQ VGLDKGVFEK
     DPDGSVWIDL TDEGLDRKIV LRSDGTAVYM TQDIGTAIQR VKDMPDVGGM VYTVGNEQDY
     HFKVLFLILK KLGFDWASSL YHLSYGMVDL PSGKMKSREG TVVDADDLMQ DMTDTAKQIA
     EDLGKLDSYS ADEKAKLYKT IGLGALKYYI LKVDPKKRIL FNPEESVDFA GNTGPFIQYT
     YARIQSIIRK ADFDFSNKIE IEELHEKEKE LVKQIELFPE VIQNAAQNHS PALIANYTYD
     LVKEYNSFYQ SVHILGEADL TKKIFRVQLS QKVAEVIKSA FSLLGIEVPE RM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024