位置:首页 > 蛋白库 > SYR_PROMA
SYR_PROMA
ID   SYR_PROMA               Reviewed;         603 AA.
AC   Q7VE03;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Pro_0212;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99258.1; -; Genomic_DNA.
DR   RefSeq; NP_874606.1; NC_005042.1.
DR   RefSeq; WP_011124367.1; NC_005042.1.
DR   AlphaFoldDB; Q7VE03; -.
DR   SMR; Q7VE03; -.
DR   STRING; 167539.Pro_0212; -.
DR   PRIDE; Q7VE03; -.
DR   EnsemblBacteria; AAP99258; AAP99258; Pro_0212.
DR   GeneID; 54199571; -.
DR   KEGG; pma:Pro_0212; -.
DR   PATRIC; fig|167539.5.peg.219; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000001420; 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   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; Reference proteome.
FT   CHAIN           1..603
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151589"
FT   MOTIF           143..153
FT                   /note="'HIGH' region"
SQ   SEQUENCE   603 AA;  67957 MW;  47480307399C3839 CRC64;
     MYNIYKSLNQ QVQRALNTAF PEAASQVKES GDFLNPQLVA ATKPEFGDFQ INGALALARI
     IKKSPRQIAE ILIKQLESNE VFKAICLPPE IAGPGFINLT LQNTCLINEI TSRLNDDLLG
     VPLVNDDEIT KKLKPVIVDF SSPNIAKEMH VGHLRSTIIG DSIARILNYR GYKVIRLNHV
     GDWGTQFGML ITHLKEVAPK ALTTANVINL GNLVEFYKKA KQRFDEDEYF QQCSRNEVVN
     LQRGNKESLK AWELLCEQSR KEFNKIYDRL KIEISERGES FYNPFLQGVI DDLTRSGLLV
     EDDGAKCVFL NGINGKDGNP LPLIIQKADG GFNYATTDLA AIRYRLKDQP DGDGAGRIIY
     VTDSGQANHF AGVFQVAKRA KWLPSSSRIE HVPFGLVQGE DGKKLKTRSG ETVRLKDLLD
     EAISRAKLDI ERRLNEENRK ESQAFIEKVS NTIGIAAVKY ADLSQNRITN YQFSFDRMLA
     LQGNTAPYLL YAVVRIAGIN RKGGDLHSSV NKLNFSEPQE WRLIRELLKF DEVIIAVEEE
     LLPNRLCNYL FELSQVFNRF YDQIPVLKAE EPSRSCRLAL CQLTGDTLKK GLNLLGISTL
     ERM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024