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Database: UniProt
Entry: W8GFR7_9MOLU
LinkDB: W8GFR7_9MOLU
Original site: W8GFR7_9MOLU 
ID   W8GFR7_9MOLU            Unreviewed;       550 AA.
AC   W8GFR7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   Name=argS {ECO:0000313|EMBL:AHK22629.1};
GN   ORFNames=X271_00529 {ECO:0000313|EMBL:AHK22629.1};
OS   Candidatus Hepatoplasma crinochetorum Av.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Hepatoplasma.
OX   NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22629.1, ECO:0000313|Proteomes:UP000019450};
RN   [1] {ECO:0000313|EMBL:AHK22629.1, ECO:0000313|Proteomes:UP000019450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Av {ECO:0000313|EMBL:AHK22629.1,
RC   ECO:0000313|Proteomes:UP000019450};
RX   PubMed=24482531; DOI=10.1093/gbe/evu020;
RA   Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT   "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage of
RT   Mollicutes Associated with Noninsect Arthropods.";
RL   Genome Biol. Evol. 6:407-415(2014).
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:0000256|ARBA:ARBA00001766};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; CP006932; AHK22629.1; -; Genomic_DNA.
DR   AlphaFoldDB; W8GFR7; -.
DR   STRING; 1427984.X271_00529; -.
DR   KEGG; hcr:X271_00529; -.
DR   PATRIC; fig|1427984.3.peg.508; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_14; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000019450; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363038};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019450}.
FT   DOMAIN          3..86
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          430..550
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   550 AA;  64256 MW;  FAC20BCBE506DBBB CRC64;
     MKDKIILYLK KYLDLNKFSH FTEKIIILNS KSKNFGDFNT NLAIIIAKKN NKDPLIIANE
     IKEYLLKVSL FKDITITKPG FINFFINEKE IIKYALSYFD KNYHDKFNTL QKLKINYEFV
     SANPTGYLHL GHARHAIIGE TTVMILKYVG HDVIREYYIN DAGVQIDNLA HSIYNHALIK
     LNIKKSDQDN SQYNGYEIID YASYLAKNHQ DLFIDKNKEQ AIIKIKKLAV DHFLEEIKKD
     LKALNVANYD IFTSDKKLIE DKKVDKILAK FQKSKYYYKK DDAIWIKTSA FGDPKDRVLI
     KKDLTYTYMV ADFANHVKKY QGGYDLMIDL WGADHHGYEA RIKAGLEILG YDSNKLKIDY
     ITLVKLLENG QEFKMSKRKG TAIRIREILD LIDVPAFKFS ILAKAKSQMH SIDIAKVNKK
     DINNNIYWYI QYANSRINQL LNKVEAKTIA NLKLKNDYFY LGKEQAEQNL LLKIIAFADQ
     ILQAANNREP LILINYLKEL AQAFHAYYNS CKIINKNKEI EEERLLLIIS LKNLFERIFN
     ILKIEPIKKM
//
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