ID I7KP37_9LACO Unreviewed; 560 AA.
AC I7KP37;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=BN52_02380 {ECO:0000313|EMBL:CCI87099.1};
OS Lactobacillus gigeriorum DSM 23908 = CRBIP 24.85.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423751 {ECO:0000313|EMBL:CCI87099.1, ECO:0000313|Proteomes:UP000009326};
RN [1] {ECO:0000313|EMBL:CCI87099.1, ECO:0000313|Proteomes:UP000009326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.85T {ECO:0000313|Proteomes:UP000009326};
RA Cousin S., Ma L., Creno S., Clermont D., Loux V., Bizet C., Bouchier C.;
RT "Draft genome sequence of Lactobacillus gigeriorum CRBIP 24.85T, isolated
RT from chicken crop.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI87099.1}.
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DR EMBL; CAKC01000048; CCI87099.1; -; Genomic_DNA.
DR RefSeq; WP_008473224.1; NZ_CAKC01000048.1.
DR AlphaFoldDB; I7KP37; -.
DR STRING; 1423751.FC38_GL000286; -.
DR PATRIC; fig|1423751.3.peg.302; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000009326; 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; cd07956; Anticodon_Ia_Arg; 1.
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; 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.
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}; Cytoplasm {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 1..82
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 446..560
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 119..129
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 560 AA; 62991 MW; 1F02AB8E16CD1623 CRC64;
MDFKEKVVEL ILSKVDLPKE QVMGLIERPK NPKLGDYAFP CFVLAKSLHK NPVEIAAEVS
EGLASPEFAK ITAVGPYVNF AIDHQQLITD TLKTVLEKQQ TYGEQQLGQG NVPIDMSSPN
IAKPMSMGHL RSTVIGNSIA KIMKKVGYNP IKINYLGDYG TQFGKLIAAY KRWGSEEDVK
KDPIMNLFHY YVRFHEEAEK DPALDDEGRE WFKKLEDGDP EAVKLWQWFR EVSLADFNRI
YKELGVTFDS YNGEAFFNDK MQPVIDELKE KGLLHESRGA QVVDMGEGEN PAIIVKSDGT
SIYLTRDLAA AEWRMKEYGF VKMLYVVGGE QAQHFVELKT VLKKMGYDWA DEIHHIPFGL
ITQGGKKLST RKGNVVFLDQ VLKDAVSLAK EQIQAKNPNL EDQDQVAHDV GVGAVIFHDL
KNDRLDNFDF DLEEVVRFEG DTGPYVQYTN ARAQSILRKA KAMGKEVGTA RSLDDDWAFA
VAKDLADFPD TIKKASEKFE PSIIAKYALN LAKKFNKYYA NVKILTDDDQ ISERLALVEA
TSIVLTNALG LLGVNAPKEM
//
