ID   SYRM_YEAST              Reviewed;         643 AA.
AC   P38714; D3DL43;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Arginine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
DE   Flags: Precursor;
GN   Name=MSR1; OrderedLocusNames=YHR091C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24657 / D273-10B;
RA   Tzagoloff A.A., Shtanko A.;
RT   "Yeast MSR1 gene.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
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;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; L39019; AAA61486.1; -; Genomic_DNA.
DR   EMBL; U00060; AAB68931.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06787.1; -; Genomic_DNA.
DR   PIR; S46723; S46723.
DR   RefSeq; NP_011959.1; NM_001179221.1.
DR   AlphaFoldDB; P38714; -.
DR   SMR; P38714; -.
DR   BioGRID; 36526; 15.
DR   DIP; DIP-1452N; -.
DR   IntAct; P38714; 2.
DR   MINT; P38714; -.
DR   STRING; 4932.YHR091C; -.
DR   MaxQB; P38714; -.
DR   PaxDb; 4932-YHR091C; -.
DR   PeptideAtlas; P38714; -.
DR   EnsemblFungi; YHR091C_mRNA; YHR091C; YHR091C.
DR   GeneID; 856491; -.
DR   KEGG; sce:YHR091C; -.
DR   AGR; SGD:S000001133; -.
DR   SGD; S000001133; MSR1.
DR   VEuPathDB; FungiDB:YHR091C; -.
DR   eggNOG; KOG1195; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_6_2_1; -.
DR   InParanoid; P38714; -.
DR   OMA; VANRWAI; -.
DR   OrthoDB; 67085at2759; -.
DR   BioCyc; YEAST:G3O-31138-MONOMER; -.
DR   BioGRID-ORCS; 856491; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P38714; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38714; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; ISA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; ISA:SGD.
DR   GO; GO:0070144; P:mitochondrial arginyl-tRNA aminoacylation; IC:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
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   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; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..643
FT                   /note="Arginine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035799"
FT   MOTIF           188..198
FT                   /note="'HIGH' region"
FT   CONFLICT        499
FT                   /note="M -> T (in Ref. 1; AAA61486)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   643 AA;  73694 MW;  7C92C0EAD5A19E0E CRC64;
     MFGIVYLKNR SLLCKNPFSS YPRYGFMPSF DTQFSNQFRK LEINIGRKRY SSKTLNTKYT
     DQPEGPIYPL DVLRLDISKA LHDISGIDHS LILNALESTN SMDRGDLLLP LPKIKVADPV
     AVANRWAIEL STHGCIGKVC AKGPFLQFFL DQRYLIQSTV PNILLQKGKY GQKKSRHQKK
     VVVEFSSPNI AKPFHAGHLR STIIGGFLSN LYEAMGWSVT RMNYLGDWGR QFGLLAVGFK
     RYGDEKTLQK QPIQHLFDVY VKINMDLAKE EINGNSKCGI SGEARSFFKN LENGDENAIK
     IWNRFRSLSI HHYIQTYSRL NINFDIFSGE SQVSKESMNE ALDIFRKNNL VKEIDGALVI
     DLTQWSKRLG RVVVQKSDGT TLYLTRDVGA AIERKKNLHF DKMVYVISSQ QDLYMSQFFM
     ILKKMNFEWA KDLQHINFGM VQGMSTRKGN VVFLDTILDE ARDKALQIME NNKMKISQVD
     NPQRVADLIG VSAIIIQDMK SKRINNYEFN WNRMLSFEGD TGPYLQYTHS RLRSLERTSS
     DFTTDMLIHA DFSNLNEPQL VELVRLLAQY PDVLRRAFET QEPATIVTYL FKVCHQVSSC
     YKKIWVSGKP ADIAIPRLAV YSASRQVLHN AMSLLGLVPV DRM
//