ID A0A2D0T1L7_ICTPU Unreviewed; 659 AA.
AC A0A2D0T1L7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Arginine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00022171};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN Name=rars1 {ECO:0000313|RefSeq:XP_017348812.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017348812.1};
RN [1] {ECO:0000313|RefSeq:XP_017348812.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017348812.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017348812.1; XM_017493323.2.
DR AlphaFoldDB; A0A2D0T1L7; -.
DR STRING; 7998.ENSIPUP00000009119; -.
DR Ensembl; ENSIPUT00000009518; ENSIPUP00000009119; ENSIPUG00000006210.
DR GeneID; 108279246; -.
DR KEGG; ipu:108279246; -.
DR CTD; 5917; -.
DR OMA; CKSMLAW; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000221080; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 77..165
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 533..659
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 5..60
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 659 AA; 75512 MW; B22F0AB245A50B60 CRC64;
MADPLAEYTD RLQNQEKEIQ ALWSQVENLK KETDFSSPVL EELMEENVRL KYRLNVLKRC
IQEENSCNSK SMTNVNHRLQ EIFGHAISLA YPDLENPPLA VAPNQQPKFG DYQCNSAMAM
SQMMKGKGLK VNPREIAEKI SQNIPDNELI ERTEIAGPGF INVYLKKSFV SKLLSNLLLS
GVQPPALDKK KKVIIDFSSP NIAKEMHVGH LRSTIIGDSM CRLFEYLGHD VLRLNHVGDW
GTQFGMLIAH LQDKFPNYLS VSPPIGDLQA FYKESKKRFD EDEEFKKKAY QCVVRLQSKE
PDFIKAWNLI CDVSREEFQK VYDCLGIRIL ERGESFYQDM MTDVVKEFEE KGLVELDEGR
KIVFIPGQPI PLTVVKSDGG YTYDTSDLAA VRQRLFDEKG DILIYVTDSG QATHFQVVFA
AARAIGWYDP KVTRVEHAGF GVVLGEDKKK FKTRSGDTVR LMDLLEEGLK RSMDKLKEKE
RDKVLTAEEL IQAQRAVAFG CIKYADLSHN RINDYVFSFD KMLDDRGNTA AYLLYAFTRI
RSIARLANIE EAALRKAAET CEILLEHEKE WKLGKCILRF PEILQKIMED LLLHTLCDYL
YELATTFTEF YDSCYCVEKD RQTGEVVKVN MWRMLLCEAT AAVMAKAFDI LGLTPVQRM
//
