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Protein

Arginine--tRNA ligase, cytoplasmic

Gene

YDR341C

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.By similarity

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

GO - Molecular functioni

  • arginine-tRNA ligase activity Source: SGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • arginyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29896-MONOMER.
BRENDAi6.1.1.19. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Ordered Locus Names:YDR341C
ORF Names:D9651.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR341c.
EuPathDBiFungiDB:YDR341C.
SGDiS000002749. YDR341C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 607606Arginine--tRNA ligase, cytoplasmicPRO_0000151664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei15 – 151Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ05506.
PaxDbiQ05506.
PeptideAtlasiQ05506.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi32398. 56 interactions.
DIPiDIP-5046N.
IntActiQ05506. 1 interaction.
MINTiMINT-482020.

Structurei

Secondary structure

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311Combined sources
Helixi19 – 224Combined sources
Turni27 – 293Combined sources
Helixi31 – 4717Combined sources
Helixi51 – 544Combined sources
Helixi55 – 573Combined sources
Helixi64 – 663Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 764Combined sources
Helixi83 – 9210Combined sources
Turni97 – 993Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi109 – 1146Combined sources
Helixi116 – 13015Combined sources
Helixi131 – 1333Combined sources
Beta strandi144 – 1485Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 17816Combined sources
Beta strandi182 – 1909Combined sources
Helixi194 – 20613Combined sources
Helixi209 – 2146Combined sources
Helixi216 – 23318Combined sources
Beta strandi235 – 2384Combined sources
Turni240 – 2423Combined sources
Beta strandi243 – 2453Combined sources
Helixi246 – 25712Combined sources
Helixi260 – 28324Combined sources
Beta strandi289 – 2935Combined sources
Helixi294 – 2963Combined sources
Helixi299 – 31113Combined sources
Beta strandi315 – 3184Combined sources
Beta strandi321 – 3255Combined sources
Helixi326 – 3283Combined sources
Turni331 – 3333Combined sources
Beta strandi335 – 3395Combined sources
Turni341 – 3433Combined sources
Helixi347 – 36216Combined sources
Beta strandi365 – 3706Combined sources
Helixi373 – 3753Combined sources
Helixi376 – 38813Combined sources
Helixi392 – 3965Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi405 – 4073Combined sources
Turni410 – 4134Combined sources
Helixi418 – 43417Combined sources
Helixi437 – 4404Combined sources
Helixi446 – 46318Combined sources
Helixi475 – 4795Combined sources
Beta strandi482 – 4854Combined sources
Helixi486 – 50217Combined sources
Turni503 – 5053Combined sources
Helixi508 – 5114Combined sources
Helixi516 – 5183Combined sources
Helixi522 – 53110Combined sources
Helixi534 – 54411Combined sources
Helixi547 – 56721Combined sources
Helixi575 – 59925Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS2X-ray2.75A1-607[»]
1F7UX-ray2.20A1-607[»]
1F7VX-ray2.90A1-607[»]
ProteinModelPortaliQ05506.
SMRiQ05506. Positions 2-607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05506.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi151 – 16212"HIGH" regionAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0018.
GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247211.
InParanoidiQ05506.
KOiK01887.
OMAiDFQGNTG.
OrthoDBiEOG7NKKV8.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05506-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTANMISQ LKKLSIAEPA VAKDSHPDVN IVDLMRNYIS QELSKISGVD
60 70 80 90 100
SSLIFPALEW TNTMERGDLL IPIPRLRIKG ANPKDLAVQW AEKFPCGDFL
110 120 130 140 150
EKVEANGPFI QFFFNPQFLA KLVIPDILTR KEDYGSCKLV ENKKVIIEFS
160 170 180 190 200
SPNIAKPFHA GHLRSTIIGG FLANLYEKLG WEVIRMNYLG DWGKQFGLLA
210 220 230 240 250
VGFERYGNEE ALVKDPIHHL FDVYVRINKD IEEEGDSIPL EQSTNGKARE
260 270 280 290 300
YFKRMEDGDE EALKIWKRFR EFSIEKYIDT YARLNIKYDV YSGESQVSKE
310 320 330 340 350
SMLKAIDLFK EKGLTHEDKG AVLIDLTKFN KKLGKAIVQK SDGTTLYLTR
360 370 380 390 400
DVGAAMDRYE KYHFDKMIYV IASQQDLHAA QFFEILKQMG FEWAKDLQHV
410 420 430 440 450
NFGMVQGMST RKGTVVFLDN ILEETKEKMH EVMKKNENKY AQIEHPEEVA
460 470 480 490 500
DLVGISAVMI QDMQGKRINN YEFKWERMLS FEGDTGPYLQ YAHSRLRSVE
510 520 530 540 550
RNASGITQEK WINADFSLLK EPAAKLLIRL LGQYPDVLRN AIKTHEPTTV
560 570 580 590 600
VTYLFKLTHQ VSSCYDVLWV AGQTEELATA RLALYGAARQ VLYNGMRLLG

LTPVERM
Length:607
Mass (Da):69,525
Last modified:November 1, 1996 - v1
Checksum:i8349ABC0E30E50F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51032 Genomic DNA. Translation: AAB64777.1.
BK006938 Genomic DNA. Translation: DAA12182.1.
PIRiS70106.
RefSeqiNP_010628.3. NM_001180649.3.

Genome annotation databases

EnsemblFungiiYDR341C; YDR341C; YDR341C.
GeneIDi851942.
KEGGisce:YDR341C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51032 Genomic DNA. Translation: AAB64777.1.
BK006938 Genomic DNA. Translation: DAA12182.1.
PIRiS70106.
RefSeqiNP_010628.3. NM_001180649.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS2X-ray2.75A1-607[»]
1F7UX-ray2.20A1-607[»]
1F7VX-ray2.90A1-607[»]
ProteinModelPortaliQ05506.
SMRiQ05506. Positions 2-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32398. 56 interactions.
DIPiDIP-5046N.
IntActiQ05506. 1 interaction.
MINTiMINT-482020.

Proteomic databases

MaxQBiQ05506.
PaxDbiQ05506.
PeptideAtlasiQ05506.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR341C; YDR341C; YDR341C.
GeneIDi851942.
KEGGisce:YDR341C.

Organism-specific databases

CYGDiYDR341c.
EuPathDBiFungiDB:YDR341C.
SGDiS000002749. YDR341C.

Phylogenomic databases

eggNOGiCOG0018.
GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247211.
InParanoidiQ05506.
KOiK01887.
OMAiDFQGNTG.
OrthoDBiEOG7NKKV8.

Enzyme and pathway databases

BioCyciYEAST:G3O-29896-MONOMER.
BRENDAi6.1.1.19. 984.

Miscellaneous databases

EvolutionaryTraceiQ05506.
NextBioi970021.
PROiQ05506.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "L-arginine recognition by yeast arginyl-tRNA synthetase."
    Cavarelli J., Delagoutte B., Eriani G., Gangloff J., Moras D.
    EMBO J. 17:5438-5448(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

Entry informationi

Entry nameiSYRC_YEAST
AccessioniPrimary (citable) accession number: Q05506
Secondary accession number(s): D6VSX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 20600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.