ID K7G7N3_PELSI Unreviewed; 661 AA.
AC K7G7N3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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|Ensembl:ENSPSIP00000016294.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000016294.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000016294.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AGCU01037648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01037649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01037650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01037651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01037652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01037653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7G7N3; -.
DR STRING; 13735.ENSPSIP00000016294; -.
DR Ensembl; ENSPSIT00000016370.1; ENSPSIP00000016294.1; ENSPSIG00000014393.1.
DR eggNOG; KOG4426; Eukaryota.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; CLU_006406_5_1_1; -.
DR OMA; CKSMLAW; -.
DR TreeFam; TF106111; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; 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:Ensembl.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267}.
FT DOMAIN 77..166
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 535..661
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 40..67
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 464..498
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 661 AA; 75808 MW; 25DEA1C4D7F32A48 CRC64;
ILVSVSVCQN KSFQEKEIKI LVAEIDRLKN FGCLETSPSL EGLRDENAKL KYRRKVLQKS
LQEERNKSTK SMININSRLQ EIFGDAIKAA YPDLEKPPLA VTPSQQPKFG DYQCNSAMSI
TKMLSKTNEQ KVSPREIAEN ISRHIPDNEY IAKVEIAGPG FINVHLRKDF VSKQLSSLLV
NGVQPPAIEN RKKVVVDFSS PNIAKEMHVG HLRSTIIGDS MCRLFEFVGY DVLRLNHLGD
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKRRF DTEEEFKKRA YQCVVLLQSK
NPDFIKAWKL ICDVSRKEFQ KIYDCLDITL IERGESYYQD RMKDIVQEFE EKGNTFFNDD
GRKIVFVPGC SVPLTIMKSD GGYTYDTSDL AALKQRLFEE NADIIVYVVD SGQSVHLQTV
FAAGQMIGWY DPTVTRVVHA AFGVVLGEDK KKFKTRSGDT VRLIDLLEEG LKRSMDKLKD
KERDKVLTEE ELKAAQTSVA FGCIKYADLS HNRMNDYIFS FDKMLDDRGN TAAYLLYAFT
RIRSIARLAN IDEEMLQKAA RETEILLDHE KEWKLGKCIL RFPEILQKIL DDLLLHTLCD
YLYELATTFT EFYDNCYCVE KDRQTGMIMK VNMWRMLLCE ATAAIMAKGF DILGIKPVQK
M
//
