Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P46655

- SYEC_YEAST

UniProt

P46655 - SYEC_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate--tRNA ligase, cytoplasmic

Gene

GUS1

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

Functioni

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).2 Publications

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151ATPBy similarity
Binding sitei241 – 2411GlutamateBy similarity
Binding sitei400 – 4001GlutamateBy similarity
Binding sitei403 – 4031ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi437 – 4415ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-tRNA ligase activity Source: SGD

GO - Biological processi

  1. glutamyl-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-30716-MONOMER.
BRENDAi6.1.1.17. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase, cytoplasmic (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
(c)ERS
Short name:
GluRS
P85
Gene namesi
Name:GUS1
Ordered Locus Names:YGL245W
ORF Names:G0583, HRB724
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL245w.
SGDiS000003214. GUS1.

Subcellular locationi

Cytoplasm. Mitochondrion
Note: Largely excluded from the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. methionyl glutamyl tRNA synthetase complex Source: SGD
  3. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481R → A: Abolishes interaction with ARC1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Glutamate--tRNA ligase, cytoplasmicPRO_0000119739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46655.
PaxDbiP46655.
PeptideAtlasiP46655.

Expressioni

Gene expression databases

GenevestigatoriP46655.

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 ARC1 (via N-ter). Can also form a stable binary complex with ARC1 that is functional in terms of aminoacylation. ARC1 increases the affinity for cognate tRNAs due to the presence of a tRNA binding domain in the middle and C-terminal part of ARC1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARC1P466727EBI-18665,EBI-7224

Protein-protein interaction databases

BioGridi32995. 114 interactions.
DIPiDIP-2212N.
IntActiP46655. 25 interactions.
MINTiMINT-491904.
STRINGi4932.YGL245W.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi16 – 2813Combined sources
Beta strandi32 – 387Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 484Combined sources
Helixi55 – 628Combined sources
Turni63 – 664Combined sources
Helixi72 – 8413Combined sources
Turni85 – 873Combined sources
Helixi91 – 10414Combined sources
Turni105 – 1073Combined sources
Helixi119 – 13012Combined sources
Helixi134 – 1407Combined sources
Helixi144 – 15411Combined sources
Helixi157 – 1604Combined sources
Helixi162 – 17716Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HRAX-ray1.90A/B1-191[»]
2HRKX-ray2.05A1-191[»]
2HSMX-ray3.00A1-191[»]
ProteinModelPortaliP46655.
SMRiP46655. Positions 1-180, 193-692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46655.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 11510Interaction with ARC1
Regioni141 – 15717Interaction with ARC1Add
BLAST
Regioni205 – 2073Glutamate bindingBy similarity
Regioni382 – 3865Glutamate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi210 – 21910"HIGH" region
Motifi437 – 4415"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00550000074815.
HOGENOMiHOG000259234.
InParanoidiP46655.
KOiK01885.
OMAiTDRNPQY.
OrthoDBiEOG7MKWFN.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46655-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD
60 70 80 90 100
ATEDVFNKIT SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET
110 120 130 140 150
LDSQLNLRTF ILGGLKYSAA DVACWGALRS NGMCGSIIKN KVDVNVSRWY
160 170 180 190 200
TLLEMDPIFG EAHDFLSKSL LELKKSANVG KKKETHKANF EIDLPDAKMG
210 220 230 240 250
EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF DDTNPSKEKE
260 270 280 290 300
EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT
310 320 330 340 350
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK
360 370 380 390 400
ALNKTLRDPV IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR
410 420 430 440 450
TIEYRDRNAQ YDWMLQALRL RKVHIWDFAR INFVRTLLSK RKLQWMVDKD
460 470 480 490 500
LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV LSQGPSRNVI NLEWNLIWAF
510 520 530 540 550
NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH KKNPAVGEKK
560 570 580 590 600
VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG
610 620 630 640 650
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE
660 670 680 690 700
FHTDAIADLN VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS

VNKYGAKK
Length:708
Mass (Da):80,843
Last modified:September 5, 2006 - v3
Checksum:iEADAD430A2D98974
GO

Sequence cautioni

The sequence AAA78905.1 differs from that shown. Reason: Frameshift at position 698.
The sequence AAA78905.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAA64142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAA89009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAA96964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091E → D in AAA78905. 1 PublicationCurated
Sequence conflicti473 – 4731V → A in AAA78905. 1 PublicationCurated
Sequence conflicti510 – 5101P → S in AAA78905. 1 PublicationCurated
Sequence conflicti546 – 5461V → M in AAA78905. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32265 Genomic DNA. Translation: AAA78905.1. Sequence problems.
Z49149 Genomic DNA. Translation: CAA89009.1. Different initiation.
Z72767 Genomic DNA. Translation: CAA96964.1. Different initiation.
X94357 Genomic DNA. Translation: CAA64142.1. Different initiation.
BK006941 Genomic DNA. Translation: DAA07874.1.
PIRiS53934.
RefSeqiNP_011269.2. NM_001181111.1.

Genome annotation databases

EnsemblFungiiYGL245W; YGL245W; YGL245W.
GeneIDi852606.
KEGGisce:YGL245W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32265 Genomic DNA. Translation: AAA78905.1 . Sequence problems.
Z49149 Genomic DNA. Translation: CAA89009.1 . Different initiation.
Z72767 Genomic DNA. Translation: CAA96964.1 . Different initiation.
X94357 Genomic DNA. Translation: CAA64142.1 . Different initiation.
BK006941 Genomic DNA. Translation: DAA07874.1 .
PIRi S53934.
RefSeqi NP_011269.2. NM_001181111.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HRA X-ray 1.90 A/B 1-191 [» ]
2HRK X-ray 2.05 A 1-191 [» ]
2HSM X-ray 3.00 A 1-191 [» ]
ProteinModelPortali P46655.
SMRi P46655. Positions 1-180, 193-692.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32995. 114 interactions.
DIPi DIP-2212N.
IntActi P46655. 25 interactions.
MINTi MINT-491904.
STRINGi 4932.YGL245W.

Proteomic databases

MaxQBi P46655.
PaxDbi P46655.
PeptideAtlasi P46655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL245W ; YGL245W ; YGL245W .
GeneIDi 852606.
KEGGi sce:YGL245W.

Organism-specific databases

CYGDi YGL245w.
SGDi S000003214. GUS1.

Phylogenomic databases

eggNOGi COG0008.
GeneTreei ENSGT00550000074815.
HOGENOMi HOG000259234.
InParanoidi P46655.
KOi K01885.
OMAi TDRNPQY.
OrthoDBi EOG7MKWFN.

Enzyme and pathway databases

BioCyci YEAST:G3O-30716-MONOMER.
BRENDAi 6.1.1.17. 984.

Miscellaneous databases

EvolutionaryTracei P46655.
NextBioi 971793.

Gene expression databases

Genevestigatori P46655.

Family and domain databases

Gene3Di 1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence characterization of the gene encoding the yeast cytosolic glutamyl-tRNA synthetase."
    Frantz J.D., Gilbert W.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII, reveals the presence of eight open reading frames."
    Vandenbol M., Durand P., Portetelle D., Hilger F.
    Yeast 11:1519-1523(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae."
    Coissac E., Maillier E., Robineau S., Netter P.
    Yeast 12:1555-1562(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
    Strain: ATCC 96604 / S288c / FY1679.
  6. "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: INTERACTION WITH ARC1.
  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: INTERACTION WITH ARC1.
  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 ARC1, 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, CATALYTIC ACTIVITY.
  10. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "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 THR-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS."
    Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.
    Genes Dev. 23:1119-1130(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 1-191, INTERACTION WITH ARC1.
  17. "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 (3.0 ANGSTROMS) OF 1-191 IN COMPLEX WITH ARC1, MUTAGENESIS OF ARG-148.

Entry informationi

Entry nameiSYEC_YEAST
AccessioniPrimary (citable) accession number: P46655
Secondary accession number(s): D6VV90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 48700 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3