ID   A0A2Y9EJI8_PHYMC        Unreviewed;       578 AA.
AC   A0A2Y9EJI8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN   Name=RARS2 {ECO:0000313|RefSeq:XP_007104093.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007104093.1};
RN   [1] {ECO:0000313|RefSeq:XP_007104093.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007104093.1};
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_007104093.1; XM_007104031.3.
DR   AlphaFoldDB; A0A2Y9EJI8; -.
DR   STRING; 9755.ENSPCTP00005018605; -.
DR   Ensembl; ENSPCTT00005020494; ENSPCTP00005018605; ENSPCTG00005013228.
DR   GeneID; 102976487; -.
DR   KEGG; pcad:102976487; -.
DR   CTD; 57038; -.
DR   InParanoid; A0A2Y9EJI8; -.
DR   OrthoDB; 67085at2759; -.
DR   Proteomes; UP000248484; Chromosome 10.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
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; 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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
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   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:UP000248484}.
FT   DOMAIN          463..578
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   578 AA;  65599 MW;  EAFED0D6359FAE51 CRC64;
     MACGFRRSIA CQLSRVLDLP PESLIKSISA VPISRKEEVA DFQLSVDSLL ENNNDHSRPD
     IQLQTMRLAE KLKCDTVVSE ISTGPGTVNF KINRELLTKT VLQEVIEDGS KYGLKSELFS
     GLPQKKIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVTRVNY LGDWGMQFGL
     LGTGFQLFGY EEKLQSNPLQ HLFEVYVQVN KEAADDKNVA KSAHEFFQRL ELGDTQALAL
     WQKFRDLSIE EYIRIYKRLG VRFDEYSGES FYREKSQEVL KLLDSKGLLQ KTIKGTAVVD
     LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMDKYNFD KMIYVTDKGQ KKHFQQVFQM
     LQIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI RLRMLQNMAS IKTTRELENP
     QETAERVGLA ALIIQDLRGF LLSDYQFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
     YLNDFNTACL QEPQSVSILQ HLLRFDEVLY RSARDLQPRH IVSYLLTLSH LAAVAHKTLH
     IKNSPPEVAG ARLHLFRAVR SVLANGMKLL GITPVCRM
//