ARC1_YEAST
ID ARC1_YEAST Reviewed; 376 AA.
AC P46672; D6VU41;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=tRNA-aminoacylation cofactor ARC1;
DE AltName: Full=Acyl-RNA-complex protein 1;
DE AltName: Full=GU4 nucleic-binding protein 1;
DE Short=G4p1 protein;
DE AltName: Full=P42;
DE AltName: Full=tRNA-interacting factor ARC1;
GN Name=ARC1; Synonyms=G4P1; OrderedLocusNames=YGL105W; ORFNames=G3085;
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], AND PROTEIN SEQUENCE OF 53-75 AND
RP 102-123.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7657649; DOI=10.1074/jbc.270.35.20692;
RA Frantz J.D., Gilbert W.;
RT "A novel yeast gene product, G4p1, with a specific affinity for quadruplex
RT nucleic acids.";
RL J. Biol. Chem. 270:20692-20697(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TRNA-BINDING, INTERACTION WITH
RP GUS1 AND MES1, AND SUBCELLULAR LOCATION.
RC STRAIN=JU4.2XJR26.19B;
RX PubMed=8895587; DOI=10.1002/j.1460-2075.1996.tb00927.x;
RA Simos G., Segref A., Fasiolo F., Hellmuth K., Shevshenko A., Mann M.,
RA Hurt E.C.;
RT "The yeast protein Arc1p binds to tRNA and functions as a cofactor for the
RT methionyl- and glutamyl-tRNA synthetases.";
RL EMBO J. 15:5437-5448(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9046090;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA Paoluzi S., Minenkova O., Castagnoli L.;
RT "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT the left arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:85-91(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP FUNCTION, TRNA BINDING, AND INTERACTION WITH GUS1 AND MES1.
RX PubMed=9659920; DOI=10.1016/s1097-2765(00)80024-6;
RA Simos G., Sauer A., Fasiolo F., Hurt E.C.;
RT "A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA
RT synthetases.";
RL Mol. Cell 1:235-242(1998).
RN [8]
RP SUBUNIT, INTERACTION WITH GUS1 AND MES1, AND SUBCELLULAR LOCATION.
RX PubMed=11726524; DOI=10.1093/emboj/20.23.6889;
RA Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.;
RT "The intracellular location of two aminoacyl-tRNA synthetases depends on
RT complex formation with Arc1p.";
RL EMBO J. 20:6889-6898(2001).
RN [9]
RP FUNCTION, TRNA-BINDING, AND INTERACTION WITH GUS1 AND MES1.
RX PubMed=11069915; DOI=10.1074/jbc.m008682200;
RA Deinert K., Fasiolo F., Hurt E.C., Simos G.;
RT "Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes
RT its interaction with the cognate tRNAs.";
RL J. Biol. Chem. 276:6000-6008(2001).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15710377; DOI=10.1016/j.febslet.2004.11.112;
RA Galani K., Hurt E., Simos G.;
RT "The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an
RT Xpo1p-dependent mechanism.";
RL FEBS Lett. 579:969-975(2005).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17131041; DOI=10.1007/s11010-006-9367-4;
RA Golinelli-Cohen M.P., Mirande M.;
RT "Arc1p is required for cytoplasmic confinement of synthetases and tRNA.";
RL Mol. Cell. Biochem. 300:47-59(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-122, AND INTERACTION WITH GUS1.
RX PubMed=17139087; DOI=10.1107/s0907444906039850;
RA Simader H., Hothorn M., Suck D.;
RT "Structures of the interacting domains from yeast glutamyl-tRNA synthetase
RT and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel
RT function for an old fold.";
RL Acta Crystallogr. D 62:1510-1519(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-122 IN COMPLEXES WITH GUS1 AND
RP MES1, AND MUTAGENESIS OF ALA-26 AND ARG-100.
RX PubMed=16914447; DOI=10.1093/nar/gkl560;
RA Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D.;
RT "Structural basis of yeast aminoacyl-tRNA synthetase complex formation
RT revealed by crystal structures of two binary sub-complexes.";
RL Nucleic Acids Res. 34:3968-3979(2006).
CC -!- FUNCTION: Binds to tRNA and functions as a cofactor for the methionyl-
CC tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a
CC complex with MetRS and GluRS and increases their affinity for cognate
CC tRNAs due to the presence of a tRNA binding domain in its middle and C-
CC terminal part. Binds specifically G4 quadruplex nucleic acid structures
CC (these are four-stranded right-handed helices, stabilized by guanine
CC base quartets). Also required for cytoplasmic confinement of the
CC synthetases and tRNA. {ECO:0000269|PubMed:11069915,
CC ECO:0000269|PubMed:17131041, ECO:0000269|PubMed:8895587,
CC ECO:0000269|PubMed:9659920}.
CC -!- SUBUNIT: Component of a yeast aminoacyl-tRNA synthase (aaRS) complex
CC formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and
CC the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex.
CC Interacts (via N-ter) with MES1 (via N-ter) and GUS1 (via N-ter). Can
CC also form a stable binary complex with either MES1 or GUS1 that is
CC functional in terms of aminoacylation. {ECO:0000269|PubMed:11069915,
CC ECO:0000269|PubMed:11726524, ECO:0000269|PubMed:17139087,
CC ECO:0000269|PubMed:8895587, ECO:0000269|PubMed:9659920}.
CC -!- INTERACTION:
CC P46672; P46655: GUS1; NbExp=7; IntAct=EBI-7224, EBI-18665;
CC P46672; P00958: MES1; NbExp=7; IntAct=EBI-7224, EBI-18762;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11726524,
CC ECO:0000269|PubMed:15710377, ECO:0000269|PubMed:17131041,
CC ECO:0000269|PubMed:8895587}. Note=Largely excluded from the nucleus.
CC -!- MISCELLANEOUS: Present with 57700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tRNA-aminoacylation cofactor ARC1 family.
CC {ECO:0000305}.
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DR EMBL; U31348; AAC49072.1; -; Genomic_DNA.
DR EMBL; X97644; CAA66247.1; -; Genomic_DNA.
DR EMBL; Z72627; CAA96812.1; -; Genomic_DNA.
DR EMBL; X95481; CAA64750.1; -; Genomic_DNA.
DR EMBL; AY558498; AAS56824.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08002.1; -; Genomic_DNA.
DR PIR; S64113; S64113.
DR RefSeq; NP_011410.1; NM_001180970.1.
DR PDB; 2HQT; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-122.
DR PDB; 2HRK; X-ray; 2.05 A; B=1-122.
DR PDB; 2HSM; X-ray; 3.00 A; B=1-122.
DR PDB; 2HSN; X-ray; 2.20 A; B=1-122.
DR PDB; 4R1J; X-ray; 1.40 A; A=201-376.
DR PDBsum; 2HQT; -.
DR PDBsum; 2HRK; -.
DR PDBsum; 2HSM; -.
DR PDBsum; 2HSN; -.
DR PDBsum; 4R1J; -.
DR AlphaFoldDB; P46672; -.
DR SMR; P46672; -.
DR BioGRID; 33145; 228.
DR ComplexPortal; CPX-1947; Methionyl glutamyl tRNA synthetase complex.
DR DIP; DIP-2210N; -.
DR IntAct; P46672; 14.
DR MINT; P46672; -.
DR STRING; 4932.YGL105W; -.
DR iPTMnet; P46672; -.
DR MaxQB; P46672; -.
DR PaxDb; P46672; -.
DR PRIDE; P46672; -.
DR TopDownProteomics; P46672; -.
DR EnsemblFungi; YGL105W_mRNA; YGL105W; YGL105W.
DR GeneID; 852773; -.
DR KEGG; sce:YGL105W; -.
DR SGD; S000003073; ARC1.
DR VEuPathDB; FungiDB:YGL105W; -.
DR eggNOG; KOG2241; Eukaryota.
DR GeneTree; ENSGT00940000154950; -.
DR HOGENOM; CLU_009710_6_6_1; -.
DR InParanoid; P46672; -.
DR OMA; HFPLEAM; -.
DR BioCyc; YEAST:G3O-30604-MON; -.
DR EvolutionaryTrace; P46672; -.
DR PRO; PR:P46672; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46672; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IMP:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IMP:SGD.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IC:ComplexPortal.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IC:ComplexPortal.
DR GO; GO:0051351; P:positive regulation of ligase activity; IDA:SGD.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..376
FT /note="tRNA-aminoacylation cofactor ARC1"
FT /id="PRO_0000087409"
FT DOMAIN 205..307
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 22..46
FT /note="Interaction with methionyl-tRNA synthetase MES1"
FT REGION 52..61
FT /note="Interaction with glutamyl-tRNA synthetase GUS1"
FT REGION 91..121
FT /note="Interaction with glutamyl-tRNA synthetase GUS1"
FT REGION 133..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 26
FT /note="A->R: Abolishes interaction with MES1."
FT /evidence="ECO:0000269|PubMed:16914447"
FT MUTAGEN 100
FT /note="R->A: Abolishes interaction with GUS1."
FT /evidence="ECO:0000269|PubMed:16914447"
FT CONFLICT 137..149
FT /note="PAGGAADAAAKAD -> LRVALLMLQQGS (in Ref. 1; AAC49072)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="KK -> LL (in Ref. 1; AAC49072)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:2HRK"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 65..83
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:2HQT"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2HQT"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:4R1J"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4R1J"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4R1J"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4R1J"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:4R1J"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:4R1J"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:4R1J"
SQ SEQUENCE 376 AA; 42084 MW; B0CD64AD564900C7 CRC64;
MSDLVTKFES LIISKYPVSF TKEQSAQAAQ WESVLKSGQI QPHLDQLNLV LRDNTFIVST
LYPTSTDVHV FEVALPLIKD LVASSKDVKS TYTTYRHILR WIDYMQNLLE VSSTDKLEIN
HDLDLPHEVI EKKKKAPAGG AADAAAKADE DVSKKAKKQD HPRGKPDEET LKKLREEAKA
KKAAKKAANA KQQQEQQNKA PEKPKPSAID FRVGFIQKAI KHPDADSLYV STIDVGDEEG
PRTVCSGLVK HFPLDAMQER YVVVVCNLKP VNMRGIKSTA MVLCGSNDDK VEFVEPPKDS
KAGDKVFFEG FGDEAPMKQL NPKKKIWEHL QPHFTTNDGL EVIFKDEEEK DHPVRKLTNA
KGESFKVASI ANAQVR
