位置:首页 > 蛋白库 > SYR_CYAP4
SYR_CYAP4
ID   SYR_CYAP4               Reviewed;         585 AA.
AC   B8HSK8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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};
GN   OrderedLocusNames=Cyan7425_3671;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001344; ACL45991.1; -; Genomic_DNA.
DR   RefSeq; WP_012629049.1; NC_011884.1.
DR   AlphaFoldDB; B8HSK8; -.
DR   SMR; B8HSK8; -.
DR   STRING; 395961.Cyan7425_3671; -.
DR   EnsemblBacteria; ACL45991; ACL45991; Cyan7425_3671.
DR   KEGG; cyn:Cyan7425_3671; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
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; 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..585
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198892"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  65673 MW;  A03581ECE8D0B38B CRC64;
     MSSPLDHLKT QLQRAMVAAY GETLSGADPL LVNASHPKFG DYQSNAPLPL AKQLNQPPRT
     IASTIVDHLE VGEAWEPPTI AGPGFINFTL KTSYLASQLE LRLTDPRLGI SAVKLPLRVV
     VDFSSPNIAK EMHVGHLRST IIGDCLARIL EFLGHEVLRL NHVGDWGTQF GMLITYLREV
     CPEALTAPDA VDLGDLVAFY RQAKQRFDSD PDFQAIARQE VVRLQSGEPD SLHAWQLLCA
     QSRREFEKIY NLLDIKLTER GESFYNPLLP QVIQALDQTG LLVEDQGAKC VFLEGYTNKA
     GDPQPLIVQK SDGGYIYATT DLAALRYRIE QDQADWIIYV TDAGQSTHFA QVFQVAQRAG
     WIPNRIRLVH VPFGLVQGED GKKLKTRSGD TVRLQDLLDE AIDRARNDLV SRLEAEGRQE
     TPEFIDHVAQ VVGIGAVKYA DLSQNRTSNY VFSYDKMLSL QGNTAPYLIY AYVRVQGISR
     KGQIDLEQLT EQPTLSLQEE EEKLLARHLL QLEDVLAQVT EDLLPNRLCQ YLFELSQKFN
     QFYDRCPILQ AEEPLRNSRL GLAQLTARTL KLGLSLLGIQ VLERM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024