SYRC_SCHPO
ID SYRC_SCHPO Reviewed; 618 AA.
AC O74781; P78751;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable arginine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=mrs1; Synonyms=rrs1; ORFNames=SPBC25B2.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-476.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC attachment of specific amino acids to cognate tRNAs during protein
CC synthesis. {ECO:0000250}.
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: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21267.1; -; Genomic_DNA.
DR EMBL; D89099; BAA13762.1; -; mRNA.
DR PIR; T39985; T39985.
DR PIR; T42007; T42007.
DR RefSeq; NP_596077.1; NM_001021989.2.
DR AlphaFoldDB; O74781; -.
DR SMR; O74781; -.
DR STRING; 4896.SPBC25B2.09c.1; -.
DR iPTMnet; O74781; -.
DR MaxQB; O74781; -.
DR PaxDb; O74781; -.
DR PRIDE; O74781; -.
DR EnsemblFungi; SPBC25B2.09c.1; SPBC25B2.09c.1:pep; SPBC25B2.09c.
DR GeneID; 2540548; -.
DR KEGG; spo:SPBC25B2.09c; -.
DR PomBase; SPBC25B2.09c; mrs1.
DR VEuPathDB; FungiDB:SPBC25B2.09c; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_6_2_1; -.
DR InParanoid; O74781; -.
DR OMA; YEFKWER; -.
DR PhylomeDB; O74781; -.
DR PRO; PR:O74781; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0070144; P:mitochondrial arginyl-tRNA aminoacylation; ISO:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..618
FT /note="Probable arginine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000151663"
FT REGION 60..61
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT REGION 104..109
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT REGION 496..510
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT MOTIF 149..160
FT /note="'HIGH' region"
FT BINDING 146..151
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT BINDING 160
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT BINDING 359
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT BINDING 363
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT BINDING 387
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT CONFLICT 359
FT /note="Y -> S (in Ref. 2; BAA13762)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="M -> T (in Ref. 2; BAA13762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 70689 MW; 69BDECEA3B2853F5 CRC64;
MATSVDQISK SLSTLGLQDL PVFREADIHH NPVDVYRSYI SSELSKINGV DVSLIYPALE
TSISKDSADL NLPVPRLRVK GKPQELAQKW AEAFPKDLVE VTANGIFLRF NFNGPSLTKL
ILPIIWEQRE NYGRNESGSG KVAVIEFSSP NIAKPFHAGH LRSTIIGSFL ANLHESQGWK
VHRVNYLGDW GKQFGLLAIG YKKYGDEDQL KSNPIRHLYD VYVKVNADAT EEDEKIQKDK
AEAESKGLPY TPPLSLHDKA REFFKRMEDG DEESLKVWAR FRDLSITKLK DTYDRLNIHY
DEYDGESQVS LELMNKMVDE LRSLNLIEED GGALLIDLSK HDKKLGKAIV QKRDGTTLYL
TRDIGTAYKR YEKYKFDKSI YVVSSQQDMY FSQLFKIFEL MGFDWAKKCV HINYGLVQGM
STRKGKAVFL DDIMEVAKEE MHKVMQKNEE KYAQVENPEE VADIVGKTAI RIQDSTGKRI
NNYAFDWSRM TSFEGDTGPY LQYAHSRLSS VRRNVNYTDE EIMGANLELL TEPDAYDLVR
LLGQYPDVLK NAFRFQETST VVTYLFKLTH AVSKLYDILW VRGRERDIQL ARLALFGAAK
QVLNNGMTLL GLTPLERM
