SYR_UREPA
ID SYR_UREPA Reviewed; 550 AA.
AC Q9PQL3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=UU278;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30687.1; -; Genomic_DNA.
DR RefSeq; WP_006688892.1; NC_002162.1.
DR AlphaFoldDB; Q9PQL3; -.
DR SMR; Q9PQL3; -.
DR STRING; 273119.UU278; -.
DR PRIDE; Q9PQL3; -.
DR EnsemblBacteria; AAF30687; AAF30687; UU278.
DR GeneID; 29672519; -.
DR KEGG; uur:UU278; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000423; 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; 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.
PE 3: Inferred from homology;
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_0000151631"
FT MOTIF 123..133
FT /note="'HIGH' region"
SQ SEQUENCE 550 AA; 63662 MW; 0400D6105A17A69B CRC64;
MITQKISEEL NKALAKMGIH DTQETKILVD KTKNIKFGDF YTNIAMILSK KNNKSSLEIA
KEIANNFEQD LFLEVNLQPP GFLNFKLKAK DHENLLKQIY YEKDRFGQFS KKNITYNIEY
VSANPTGYLH IAHAANAIYG DILANLLKIY GYDVETEYWI NDAGNQIDKL AMSVLVRYLQ
LQNINIQLPA DAYHGQEIHL VAQTLYQTYK NQFINVRLNE KYEIDDDIAN QEIKNFAVKY
LLNEIKNDLA SINTFIDTYT SENWIRNSGR ILEVLSKIKP YTYTLDGALW LKTTTFGDDK
DRVLIKSDGS YTYFTPDIAY HDYKFNKTNT TKLIDVWGTD HLGYIARLKA AMNALGYDPN
NLEIVCAQVM KLVKNNQEFK LSKRSGQSLT IKDLVEIIGK DALRWFLGSS SMNSHVIIDV
DIALSKNNNN PLYYVQYAHA RANQVLNKQV YELDFKTDLL TETRERELLN QLHFYKQTIA
NAANNREPHR ISNYLYDLAQ IFHNYYANVK INNDNNKVLS AQRYTLVWCV KQVLANGLAI
MKITPYDQMY