Skip Header

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

60S ribosomal protein L9-A

Gene

RPL9A

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

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

Miscellaneous

Present with 52400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for uL6 in yeast.Curated

GO - Molecular functioni

  • RNA binding Source: GO_Central
  • rRNA binding Source: InterPro
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30641-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L9-A1 Publication
Alternative name(s):
L8
Large ribosomal subunit protein uL6-A1 Publication
RP24
YL11
Gene namesi
Name:RPL9A1 Publication
Synonyms:RPL8A, RPL9
Ordered Locus Names:YGL147C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL147C.
SGDiS000003115. RPL9A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001311111 – 19160S ribosomal protein L9-AAdd BLAST191

Proteomic databases

MaxQBiP05738.
PRIDEiP05738.

PTM databases

iPTMnetiP05738.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). uL6 lines the binding pocket for eukaryotic elongation factor 2 (eEF2) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi33105. 199 interactors.
DIPiDIP-4826N.
IntActiP05738. 10 interactors.
MINTiMINT-493534.

Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi17 – 21Combined sources5
Beta strandi24 – 29Combined sources6
Beta strandi32 – 37Combined sources6
Turni39 – 41Combined sources3
Beta strandi44 – 49Combined sources6
Beta strandi52 – 60Combined sources9
Helixi62 – 83Combined sources22
Beta strandi86 – 93Combined sources8
Beta strandi95 – 97Combined sources3
Beta strandi100 – 104Combined sources5
Beta strandi106 – 108Combined sources3
Beta strandi111 – 115Combined sources5
Helixi117 – 119Combined sources3
Beta strandi124 – 127Combined sources4
Beta strandi132 – 136Combined sources5
Beta strandi138 – 140Combined sources3
Beta strandi143 – 149Combined sources7
Helixi151 – 163Combined sources13
Beta strandi168 – 170Combined sources3
Turni172 – 174Combined sources3
Beta strandi178 – 189Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-H7-184[»]
3J16electron microscopy-F1-191[»]
3J6Xelectron microscopy6.10L91-191[»]
3J6Yelectron microscopy6.10L91-191[»]
3J77electron microscopy6.20L91-191[»]
3J78electron microscopy6.30L91-191[»]
3JCTelectron microscopy3.08H1-191[»]
4U3MX-ray3.00L9/l91-191[»]
4U3NX-ray3.20L9/l91-191[»]
4U3UX-ray2.90L9/l91-191[»]
4U4NX-ray3.10L9/l91-191[»]
4U4OX-ray3.60L9/l91-191[»]
4U4QX-ray3.00L9/l91-191[»]
4U4RX-ray2.80L9/l91-191[»]
4U4UX-ray3.00L9/l91-191[»]
4U4YX-ray3.20L9/l91-191[»]
4U4ZX-ray3.10L9/l91-191[»]
4U50X-ray3.20L9/l91-191[»]
4U51X-ray3.20L9/l91-191[»]
4U52X-ray3.00L9/l91-191[»]
4U53X-ray3.30L9/l91-191[»]
4U55X-ray3.20L9/l91-191[»]
4U56X-ray3.45L9/l91-191[»]
4U6FX-ray3.10L9/l91-191[»]
4V4Belectron microscopy11.70BH1-191[»]
4V6Ielectron microscopy8.80BF1-191[»]
4V7Felectron microscopy8.70F1-191[»]
4V7RX-ray4.00BI/DI1-191[»]
4V88X-ray3.00BH/DH1-191[»]
4V8Telectron microscopy8.10H1-191[»]
4V8Yelectron microscopy4.30BH1-191[»]
4V8Zelectron microscopy6.60BH1-191[»]
4V91electron microscopy3.70H1-191[»]
5APNelectron microscopy3.91H1-191[»]
5APOelectron microscopy3.41H1-191[»]
5DATX-ray3.15L9/l91-191[»]
5DC3X-ray3.25L9/l91-191[»]
5DGEX-ray3.45L9/l91-191[»]
5DGFX-ray3.30L9/l91-191[»]
5DGVX-ray3.10L9/l91-191[»]
5FCIX-ray3.40L9/l91-191[»]
5FCJX-ray3.10L9/l91-191[»]
5GAKelectron microscopy3.88L1-191[»]
5H4Pelectron microscopy3.07H1-191[»]
5I4LX-ray3.10L9/l91-191[»]
5JCSelectron microscopy9.50H1-191[»]
5JUOelectron microscopy4.00M1-191[»]
5JUPelectron microscopy3.50M1-191[»]
5JUSelectron microscopy4.20M1-191[»]
5JUTelectron microscopy4.00M1-191[»]
5JUUelectron microscopy4.00M1-191[»]
5LYBX-ray3.25L9/l91-191[»]
5M1Jelectron microscopy3.30H51-191[»]
5MC6electron microscopy3.80AD1-191[»]
5T62electron microscopy3.30K1-191[»]
5T6Relectron microscopy4.50K1-191[»]
5TGAX-ray3.30L9/l91-191[»]
5TGMX-ray3.50L9/l91-191[»]
ProteinModelPortaliP05738.
SMRiP05738.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05738.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000039905.
InParanoidiP05738.
KOiK02940.
OMAiIYIVKKP.
OrthoDBiEOG092C4TE3.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
InterProiView protein in InterPro
IPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiView protein in Pfam
PF00347. Ribosomal_L6. 2 hits.
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
PROSITEiView protein in PROSITE
PS00700. RIBOSOMAL_L6_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P05738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYIQTEQQI EVPEGVTVSI KSRIVKVVGP RGTLTKNLKH IDVTFTKVNN
60 70 80 90 100
QLIKVAVHNG GRKHVAALRT VKSLVDNMIT GVTKGYKYKM RYVYAHFPIN
110 120 130 140 150
VNIVEKDGAK FIEVRNFLGD KKIRNVPVRD GVTIEFSTNV KDEIVLSGNS
160 170 180 190
VEDVSQNAAD LQQICRVRNK DIRKFLDGIY VSHKGFITED L
Length:191
Mass (Da):21,569
Last modified:December 1, 1992 - v2
Checksum:iCAA342FCDD061175
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60190 Genomic DNA. Translation: CAA42746.1.
X99960 Genomic DNA. Translation: CAA68215.1.
Z72669 Genomic DNA. Translation: CAA96859.1.
BK006941 Genomic DNA. Translation: DAA07963.1.
PIRiS19077. R5BYL9.
RefSeqiNP_011368.3. NM_001181012.3.

Genome annotation databases

EnsemblFungiiYGL147C; YGL147C; YGL147C.
GeneIDi852730.
KEGGisce:YGL147C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60190 Genomic DNA. Translation: CAA42746.1.
X99960 Genomic DNA. Translation: CAA68215.1.
Z72669 Genomic DNA. Translation: CAA96859.1.
BK006941 Genomic DNA. Translation: DAA07963.1.
PIRiS19077. R5BYL9.
RefSeqiNP_011368.3. NM_001181012.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-H7-184[»]
3J16electron microscopy-F1-191[»]
3J6Xelectron microscopy6.10L91-191[»]
3J6Yelectron microscopy6.10L91-191[»]
3J77electron microscopy6.20L91-191[»]
3J78electron microscopy6.30L91-191[»]
3JCTelectron microscopy3.08H1-191[»]
4U3MX-ray3.00L9/l91-191[»]
4U3NX-ray3.20L9/l91-191[»]
4U3UX-ray2.90L9/l91-191[»]
4U4NX-ray3.10L9/l91-191[»]
4U4OX-ray3.60L9/l91-191[»]
4U4QX-ray3.00L9/l91-191[»]
4U4RX-ray2.80L9/l91-191[»]
4U4UX-ray3.00L9/l91-191[»]
4U4YX-ray3.20L9/l91-191[»]
4U4ZX-ray3.10L9/l91-191[»]
4U50X-ray3.20L9/l91-191[»]
4U51X-ray3.20L9/l91-191[»]
4U52X-ray3.00L9/l91-191[»]
4U53X-ray3.30L9/l91-191[»]
4U55X-ray3.20L9/l91-191[»]
4U56X-ray3.45L9/l91-191[»]
4U6FX-ray3.10L9/l91-191[»]
4V4Belectron microscopy11.70BH1-191[»]
4V6Ielectron microscopy8.80BF1-191[»]
4V7Felectron microscopy8.70F1-191[»]
4V7RX-ray4.00BI/DI1-191[»]
4V88X-ray3.00BH/DH1-191[»]
4V8Telectron microscopy8.10H1-191[»]
4V8Yelectron microscopy4.30BH1-191[»]
4V8Zelectron microscopy6.60BH1-191[»]
4V91electron microscopy3.70H1-191[»]
5APNelectron microscopy3.91H1-191[»]
5APOelectron microscopy3.41H1-191[»]
5DATX-ray3.15L9/l91-191[»]
5DC3X-ray3.25L9/l91-191[»]
5DGEX-ray3.45L9/l91-191[»]
5DGFX-ray3.30L9/l91-191[»]
5DGVX-ray3.10L9/l91-191[»]
5FCIX-ray3.40L9/l91-191[»]
5FCJX-ray3.10L9/l91-191[»]
5GAKelectron microscopy3.88L1-191[»]
5H4Pelectron microscopy3.07H1-191[»]
5I4LX-ray3.10L9/l91-191[»]
5JCSelectron microscopy9.50H1-191[»]
5JUOelectron microscopy4.00M1-191[»]
5JUPelectron microscopy3.50M1-191[»]
5JUSelectron microscopy4.20M1-191[»]
5JUTelectron microscopy4.00M1-191[»]
5JUUelectron microscopy4.00M1-191[»]
5LYBX-ray3.25L9/l91-191[»]
5M1Jelectron microscopy3.30H51-191[»]
5MC6electron microscopy3.80AD1-191[»]
5T62electron microscopy3.30K1-191[»]
5T6Relectron microscopy4.50K1-191[»]
5TGAX-ray3.30L9/l91-191[»]
5TGMX-ray3.50L9/l91-191[»]
ProteinModelPortaliP05738.
SMRiP05738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33105. 199 interactors.
DIPiDIP-4826N.
IntActiP05738. 10 interactors.
MINTiMINT-493534.

PTM databases

iPTMnetiP05738.

Proteomic databases

MaxQBiP05738.
PRIDEiP05738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL147C; YGL147C; YGL147C.
GeneIDi852730.
KEGGisce:YGL147C.

Organism-specific databases

EuPathDBiFungiDB:YGL147C.
SGDiS000003115. RPL9A.

Phylogenomic databases

HOGENOMiHOG000039905.
InParanoidiP05738.
KOiK02940.
OMAiIYIVKKP.
OrthoDBiEOG092C4TE3.

Enzyme and pathway databases

BioCyciYEAST:G3O-30641-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP05738.
PROiPR:P05738.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
InterProiView protein in InterPro
IPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiView protein in Pfam
PF00347. Ribosomal_L6. 2 hits.
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
PROSITEiView protein in PROSITE
PS00700. RIBOSOMAL_L6_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL9A_YEAST
AccessioniPrimary (citable) accession number: P05738
Secondary accession number(s): D6VU02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 1, 1992
Last modified: April 12, 2017
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  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

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.