ID Z9JH57_9GAMM Unreviewed; 562 AA.
AC Z9JH57;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123,
GN ECO:0000313|EMBL:EWS77353.1};
GN ORFNames=AF72_11335 {ECO:0000313|EMBL:EWS77353.1};
OS Xylella taiwanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=1444770 {ECO:0000313|EMBL:EWS77353.1, ECO:0000313|Proteomes:UP000020406};
RN [1] {ECO:0000313|EMBL:EWS77353.1, ECO:0000313|Proteomes:UP000020406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLS229 {ECO:0000313|EMBL:EWS77353.1,
RC ECO:0000313|Proteomes:UP000020406};
RX PubMed=24652975;
RA Su C.C., Deng W.L., Jan F.J., Chang C.J., Huang H., Chen J.;
RT "Draft Genome Sequence of Xylella fastidiosa Pear Leaf Scorch Strain in
RT Taiwan.";
RL Genome Announc. 2:e00166-14(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 ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWS77353.1}.
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DR EMBL; JDSQ01000022; EWS77353.1; -; Genomic_DNA.
DR RefSeq; WP_038272360.1; NZ_JDSQ01000022.1.
DR AlphaFoldDB; Z9JH57; -.
DR STRING; 1444770.AF72_11335; -.
DR GeneID; 69681889; -.
DR KEGG; xtw:AB672_00645; -.
DR PATRIC; fig|1444770.3.peg.2677; -.
DR eggNOG; COG0018; Bacteria.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000020406; Unassembled WGS sequence.
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; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 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|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}.
FT DOMAIN 3..92
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 441..562
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 129..139
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 562 AA; 62571 MW; F71C84995192C412 CRC64;
MKAQLRALIC QGIEALRSNG TLPSHTLPPD FVIERPKTRK HGDFATNAAM LLSKATRSNP
LLLAQALVAA LPTRAEIARV EIAGPGFINF HLHPVAYQRE TINVLKQGSD YGRNLSGKGR
TVGVEYVSAN PTGPLHVGHG RAAAIGDCLA RLLEANGWNV KREFYYNDAG VQIENLVRSV
QARARGLKPG DTQWPTDAYN GEYIADIAKA YLVGDSVNMA GTVITGTKNV DDTAAIHHFA
VNYLRNEQNQ DLAAFKVDFD LYFLESSLYK DGKVEETVQK LIDSGHTYED GGALWLKSTD
FGDDKDRVMR KSDGSYTYFV PDVAYHLSKW QRGYERAITE LGADHHGSLA RVHAGLQALE
IGIPPGWPEY VLHQMVTVMR GGEEVKLSKR SGSYVTLRDL IEETSTDATR WFLIARKPDS
QLTFDIDLAR QRSNDNPVFY VQYAHARVCS LLYQAHEKHL NYDQTSGIDS LNQLSDNTSL
WLMTEISRYP EIVEIAGELL EPHLIAQYLR ELAHAFHTWY HNIPVLVEDA AERNAKLTLA
CATRQVLANG LNLLGVSTPE KM
//
