ID W5PU06_SHEEP Unreviewed; 578 AA.
AC W5PU06;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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|Ensembl:ENSOARP00000013937.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000013937.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000013937.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000013937.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000013937.1}
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; AMGL01107380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01107381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01107382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004011336.1; XM_004011287.3.
DR AlphaFoldDB; W5PU06; -.
DR SMR; W5PU06; -.
DR STRING; 9940.ENSOARP00000013937; -.
DR PaxDb; 9940-ENSOARP00000013937; -.
DR Ensembl; ENSOART00000014143.1; ENSOARP00000013937.1; ENSOARG00000013003.1.
DR GeneID; 101112906; -.
DR KEGG; oas:101112906; -.
DR CTD; 57038; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_6_2_1; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000002356; Chromosome 8.
DR Bgee; ENSOARG00000013003; Expressed in fallopian tube and 55 other cell types or tissues.
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 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:UP000002356}.
FT DOMAIN 463..578
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 578 AA; 65702 MW; CEA42CE5C1D7B658 CRC64;
MACGFRRSIA SQLSRVLDLP PENLIKSISA VPISRKEEVA DFQLSVDSLL ENNNDHSRPD
IQIQAMRLAE KLKCDTVVSE ISTGQGTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
GLPQKRIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY LGDWGMQFGL
LGTGFQLFGY EEKLQSSPLQ HLFEVYVQVN KEAADDKNVA QSAHEFFQRL ELGDMQALAL
WQKFRDLSIE EYMRIYKRLG VHFDEYSGES FYREKSQEVL KLLDSKGLLQ KTLKGTAVVD
LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMEKYNFD KMIYVTDKGQ KKHFQQVFQM
LQIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI RLRMLQNMAS IKTTKELENP
QETAEQVGLA ALIIQDFRGF LLSDYQFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
YLNDFNIACL QEPQSVSILQ HLLRFDEVLY RSSQDLQPRH IVSYLLTLSH LAAVAHRTLH
IRNSPPEVAG ARLHLFRAVR SVLANGMKLL GITPVCRM
//
