SYR_CORGL
ID SYR_CORGL Reviewed; 550 AA.
AC P35868; P41253;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=argS; OrderedLocusNames=Cgl1179, cg1333;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2082143; DOI=10.1111/j.1365-2958.1990.tb02030.x;
RA Marcel T., Archer J.A.C., Mengin-Lecreulx D., Sinskey A.J.;
RT "Nucleotide sequence and organization of the upstream region of the
RT Corynebacterium glutamicum lysA gene.";
RL Mol. Microbiol. 4:1819-1830(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8226683; DOI=10.1128/jb.175.22.7356-7362.1993;
RA Oguiza J.A., Malumbres M., Eriani G., Pisabarro A., Mateos L.M., Martin F.,
RA Martin J.F.;
RT "A gene encoding arginyl-tRNA synthetase is located in the upstream region
RT of the lysA gene in Brevibacterium lactofermentum: regulation of argS-lysA
RT cluster expression by arginine.";
RL J. Bacteriol. 175:7356-7362(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=8497194; DOI=10.1111/j.1365-2958.1993.tb01217.x;
RA Sharp P.M., Mitchell K.J.;
RT "Corynebacterium glutamicum arginyl-tRNA synthetase.";
RL Mol. Microbiol. 8:200-200(1993).
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by arginine and repressed by lysine.
CC {ECO:0000269|PubMed:8226683}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA38537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X54740; CAA38537.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z21501; CAA79710.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98572.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19883.1; -; Genomic_DNA.
DR PIR; A49936; A49936.
DR PIR; S12227; S12227.
DR RefSeq; NP_600405.1; NC_003450.3.
DR RefSeq; WP_011014179.1; NC_006958.1.
DR AlphaFoldDB; P35868; -.
DR SMR; P35868; -.
DR STRING; 196627.cg1333; -.
DR KEGG; cgb:cg1333; -.
DR KEGG; cgl:Cgl1179; -.
DR PATRIC; fig|196627.13.peg.1158; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_11; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000582; 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..550
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151554"
FT MOTIF 130..140
FT /note="'HIGH' region"
FT CONFLICT 355
FT /note="G -> D (in Ref. 2; CAA79710)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="I -> M (in Ref. 2; CAA79710)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="V -> A (in Ref. 2; CAA79710)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="H -> R (in Ref. 2; CAA79710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 59723 MW; 3AF724BDEE8DC4C1 CRC64;
MTPADLATLI KETAVEVLTS RELDTSVLPE QVVVERPRNP EHGDYATNIA LQVAKKVGQN
PRDLATWLAE ALAADDAIDS AEIAGPGFLN IRLAAAAQGE IVAKILAQGE TFGNSDHLSH
LDVNLEFVSA NPTGPIHLGG TRWAAVGDSL GRVLEASGAK VTREYYFNDH GRQIDRFALS
LLAAAKGEPT PEDGYGGEYI KEIAEAIVEK HPEALALEPA ATQELFRAEG VEMMFEHIKS
SLHEFGTDFD VYYHENSLFE SGAVDKAVQV LKDNGNLYEN EGAWWLRSTE FGDDKDRVVI
KSDGDAAYIA GDIAYVADKF SRGHNLNIYM LGADHHGYIA RLKAAAAALG YKPEGVEVLI
GQMVNLLRDG KAVRMSKRAG TVVTLDDLVE AIGIDAARYS LIRSSVDSSL DIDLGLWESQ
SSDNPVYYVQ YGHARLCSIA RKAETLGVTE EGADLSLLTH DREGDLIRTL GEFPAVVKAA
ADLREPHRIA RYAEELAGTF HRFYDSCHIL PKVDEDTAPI HTARLALAAA TRQTLANALH
LVGVSAPEKM
