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SYR_CAUSK
ID   SYR_CAUSK               Reviewed;         613 AA.
AC   B0T019;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Caul_4389;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000927; ABZ73509.1; -; Genomic_DNA.
DR   RefSeq; WP_012288386.1; NC_010338.1.
DR   AlphaFoldDB; B0T019; -.
DR   SMR; B0T019; -.
DR   STRING; 366602.Caul_4389; -.
DR   EnsemblBacteria; ABZ73509; ABZ73509; Caul_4389.
DR   KEGG; cak:Caul_4389; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_5; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
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   CDD; cd00671; ArgRS_core; 1.
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; 2.
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   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..613
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000076207"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   613 AA;  67521 MW;  5B3EFD61B385698C CRC64;
     MSDLKRSLSE AAAAAFQAAG LSPDFGRVTA SDRPDLADFQ CNGALAAAKS AKRNPREIAV
     QVVDVLKADP RLASVEIAGV GFINMRVSTD ALSIRANEIA ADPRAGAEPL AHPRRVLVDY
     AGPNVAKPMH VGHLRASIIG ESVKRLYRFR GDDVVGDAHF GDWGFQMGLL ISAIMEEDAF
     IRALLERLVE APREFSKADE DKVMSEFAQR VTLDDLDRLY PAASARQKED PEFKEKARKA
     TAELQNGRFG YRLLWRHFVN ISRVALEREF HALGVDFDLW KGESDVQDLI APMVRQLEVK
     GLLVDDQGAR IVRVARPGET KKKKLPDGSV VEVESPDPLL VVSSEGSAMY GTTDLATILD
     RRKSFDPHLI LYCVDQRQAD HFEQVFRAAY LAGYAEPGSL EHIGFGTMNG SDGKPFKTRA
     GGVLKLHDLI EMAREKARER LREAGLGAEL SQEAFEETAH KVGIAALKFA DLQNFRGTSY
     VFDLDRFTSF EGKTGPYLLY QSVRIKSILR KAAEQKVVSG AIIVGEPAER DLTLLLDAFE
     GALSEAYDKK APNFIAEHAY KLAQTFSKFY AACPILSADN DATRASRLAL AETTLKQLEL
     ALDLLGIEAP ERM
 
 
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