SYRM_YEAST
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 03-AUG-2022, entry version 178.
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; 12.
DR DIP; DIP-1452N; -.
DR IntAct; P38714; 2.
DR MINT; P38714; -.
DR STRING; 4932.YHR091C; -.
DR MaxQB; P38714; -.
DR PaxDb; P38714; -.
DR PRIDE; P38714; -.
DR EnsemblFungi; YHR091C_mRNA; YHR091C; YHR091C.
DR GeneID; 856491; -.
DR KEGG; sce:YHR091C; -.
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; EPHAINI; -.
DR BioCyc; YEAST:G3O-31138-MON; -.
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; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 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
