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Protein

tRNA-aminoacylation cofactor ARC1

Gene

ARC1

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

Functioni

Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.4 Publications

GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • phosphatidylinositol-3,5-bisphosphate binding Source: SGD
  • phosphatidylinositol-3-phosphate binding Source: SGD
  • tRNA binding Source: SGD

GO - Biological processi

  • positive regulation of ligase activity Source: SGD
  • tRNA aminoacylation for protein translation Source: SGD
Complete GO annotation...

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30604-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-aminoacylation cofactor ARC1
Alternative name(s):
Acyl-RNA-complex protein 1
GU4 nucleic-binding protein 1
Short name:
G4p1 protein
P42
tRNA-interacting factor ARC1
Gene namesi
Name:ARC1
Synonyms:G4P1
Ordered Locus Names:YGL105W
ORF Names:G3085
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL105W.
SGDiS000003073. ARC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • methionyl glutamyl tRNA synthetase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261A → R: Abolishes interaction with MES1. 1 Publication
Mutagenesisi100 – 1001R → A: Abolishes interaction with GUS1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376tRNA-aminoacylation cofactor ARC1PRO_0000087409Add
BLAST

Proteomic databases

MaxQBiP46672.
TopDownProteomicsiP46672.

Interactioni

Subunit structurei

Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with MES1 (via N-ter) and GUS1 (via N-ter). Can also form a stable binary complex with either MES1 or GUS1 that is functional in terms of aminoacylation.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GUS1P466557EBI-7224,EBI-18665
MES1P009587EBI-7224,EBI-18762

Protein-protein interaction databases

BioGridi33145. 183 interactions.
DIPiDIP-2210N.
IntActiP46672. 7 interactions.
MINTiMINT-705320.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Helixi12 – 154Combined sources
Helixi22 – 3615Combined sources
Helixi41 – 433Combined sources
Helixi44 – 5310Combined sources
Helixi65 – 8319Combined sources
Helixi88 – 947Combined sources
Helixi96 – 10813Combined sources
Turni113 – 1153Combined sources
Helixi206 – 2083Combined sources
Beta strandi211 – 22111Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi242 – 2476Combined sources
Turni249 – 2513Combined sources
Helixi254 – 2574Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi305 – 3084Combined sources
Helixi322 – 3243Combined sources
Helixi326 – 3305Combined sources
Helixi331 – 3333Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi341 – 3455Combined sources
Beta strandi354 – 3596Combined sources
Beta strandi374 – 3763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQTX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-122[»]
2HRKX-ray2.05B1-122[»]
2HSMX-ray3.00B1-122[»]
2HSNX-ray2.20B1-122[»]
4R1JX-ray1.40A201-376[»]
ProteinModelPortaliP46672.
SMRiP46672. Positions 1-121, 203-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46672.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini205 – 307103tRNA-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 4625Interaction with methionyl-tRNA synthetase MES1Add
BLAST
Regioni52 – 6110Interaction with glutamyl-tRNA synthetase GUS1
Regioni91 – 12131Interaction with glutamyl-tRNA synthetase GUS1Add
BLAST

Sequence similaritiesi

Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00790000123080.
HOGENOMiHOG000167473.
InParanoidiP46672.
KOiK15437.
OMAiAMVLCGS.
OrthoDBiEOG71ZPBR.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]
PfamiPF01588. tRNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLVTKFES LIISKYPVSF TKEQSAQAAQ WESVLKSGQI QPHLDQLNLV
60 70 80 90 100
LRDNTFIVST LYPTSTDVHV FEVALPLIKD LVASSKDVKS TYTTYRHILR
110 120 130 140 150
WIDYMQNLLE VSSTDKLEIN HDLDLPHEVI EKKKKAPAGG AADAAAKADE
160 170 180 190 200
DVSKKAKKQD HPRGKPDEET LKKLREEAKA KKAAKKAANA KQQQEQQNKA
210 220 230 240 250
PEKPKPSAID FRVGFIQKAI KHPDADSLYV STIDVGDEEG PRTVCSGLVK
260 270 280 290 300
HFPLDAMQER YVVVVCNLKP VNMRGIKSTA MVLCGSNDDK VEFVEPPKDS
310 320 330 340 350
KAGDKVFFEG FGDEAPMKQL NPKKKIWEHL QPHFTTNDGL EVIFKDEEEK
360 370
DHPVRKLTNA KGESFKVASI ANAQVR
Length:376
Mass (Da):42,084
Last modified:October 1, 1996 - v2
Checksum:iB0CD64AD564900C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 14913PAGGA…AAKAD → LRVALLMLQQGS in AAC49072 (PubMed:7657649).CuratedAdd
BLAST
Sequence conflicti181 – 1822KK → LL in AAC49072 (PubMed:7657649).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31348 Genomic DNA. Translation: AAC49072.1.
X97644 Genomic DNA. Translation: CAA66247.1.
Z72627 Genomic DNA. Translation: CAA96812.1.
X95481 Genomic DNA. Translation: CAA64750.1.
AY558498 Genomic DNA. Translation: AAS56824.1.
BK006941 Genomic DNA. Translation: DAA08002.1.
PIRiS64113.
RefSeqiNP_011410.1. NM_001180970.1.

Genome annotation databases

EnsemblFungiiYGL105W; YGL105W; YGL105W.
GeneIDi852773.
KEGGisce:YGL105W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31348 Genomic DNA. Translation: AAC49072.1.
X97644 Genomic DNA. Translation: CAA66247.1.
Z72627 Genomic DNA. Translation: CAA96812.1.
X95481 Genomic DNA. Translation: CAA64750.1.
AY558498 Genomic DNA. Translation: AAS56824.1.
BK006941 Genomic DNA. Translation: DAA08002.1.
PIRiS64113.
RefSeqiNP_011410.1. NM_001180970.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQTX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-122[»]
2HRKX-ray2.05B1-122[»]
2HSMX-ray3.00B1-122[»]
2HSNX-ray2.20B1-122[»]
4R1JX-ray1.40A201-376[»]
ProteinModelPortaliP46672.
SMRiP46672. Positions 1-121, 203-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33145. 183 interactions.
DIPiDIP-2210N.
IntActiP46672. 7 interactions.
MINTiMINT-705320.

Proteomic databases

MaxQBiP46672.
TopDownProteomicsiP46672.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL105W; YGL105W; YGL105W.
GeneIDi852773.
KEGGisce:YGL105W.

Organism-specific databases

EuPathDBiFungiDB:YGL105W.
SGDiS000003073. ARC1.

Phylogenomic databases

GeneTreeiENSGT00790000123080.
HOGENOMiHOG000167473.
InParanoidiP46672.
KOiK15437.
OMAiAMVLCGS.
OrthoDBiEOG71ZPBR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30604-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP46672.
PROiP46672.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]
PfamiPF01588. tRNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel yeast gene product, G4p1, with a specific affinity for quadruplex nucleic acids."
    Frantz J.D., Gilbert W.
    J. Biol. Chem. 270:20692-20697(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-75 AND 102-123.
    Strain: ATCC 204508 / S288c.
  2. "The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases."
    Simos G., Segref A., Fasiolo F., Hellmuth K., Shevshenko A., Mann M., Hurt E.C.
    EMBO J. 15:5437-5448(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TRNA-BINDING, INTERACTION WITH GUS1 AND MES1, SUBCELLULAR LOCATION.
    Strain: JU4.2XJR26.19B.
  3. "The genes encoding the transcription factor yTAFII60, the G4p1 protein and a putative glucose transporter are contained in a 12.3 kb DNA fragment on the left arm of Saccharomyces cerevisiae chromosome VII."
    Paoluzi S., Minenkova O., Castagnoli L.
    Yeast 13:85-91(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases."
    Simos G., Sauer A., Fasiolo F., Hurt E.C.
    Mol. Cell 1:235-242(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TRNA BINDING, INTERACTION WITH GUS1 AND MES1.
  8. "The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p."
    Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.
    EMBO J. 20:6889-6898(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH GUS1 AND MES1, SUBCELLULAR LOCATION.
  9. "Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs."
    Deinert K., Fasiolo F., Hurt E.C., Simos G.
    J. Biol. Chem. 276:6000-6008(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TRNA-BINDING, INTERACTION WITH GUS1 AND MES1.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism."
    Galani K., Hurt E., Simos G.
    FEBS Lett. 579:969-975(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Arc1p is required for cytoplasmic confinement of synthetases and tRNA."
    Golinelli-Cohen M.P., Mirande M.
    Mol. Cell. Biochem. 300:47-59(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold."
    Simader H., Hothorn M., Suck D.
    Acta Crystallogr. D 62:1510-1519(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-122, INTERACTION WITH GUS1.
  14. "Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes."
    Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D.
    Nucleic Acids Res. 34:3968-3979(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-122 IN COMPLEXES WITH GUS1 AND MES1, MUTAGENESIS OF ALA-26 AND ARG-100.

Entry informationi

Entry nameiARC1_YEAST
AccessioniPrimary (citable) accession number: P46672
Secondary accession number(s): D6VU41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 57700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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 one 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.