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Protein

60S ribosomal protein L33-A

Gene

RPL33A

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

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

There are 2 genes for eL33 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-34040-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L33-A1 Publication
Alternative name(s):
L37
Large ribosomal subunit protein eL33-A1 Publication
RP47
YL37
Gene namesi
Name:RPL33A1 Publication
Synonyms:RPL37A
Ordered Locus Names:YPL143W
ORF Names:LPI4W, P2625
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL143W.
SGDiS000006064. RPL33A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001928072 – 10760S ribosomal protein L33-AAdd BLAST106

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; partial1 Publication1
Cross-linki47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP05744.
PRIDEiP05744.
TopDownProteomicsiP05744.

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) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi36040. 106 interactors.
IntActiP05744. 15 interactors.
MINTiMINT-8285485.

Structurei

Secondary structure

1107
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 18Combined sources11
Beta strandi23 – 32Combined sources10
Helixi38 – 41Combined sources4
Turni42 – 46Combined sources5
Beta strandi48 – 54Combined sources7
Beta strandi59 – 61Combined sources3
Beta strandi63 – 74Combined sources12
Beta strandi76 – 79Combined sources4
Beta strandi81 – 87Combined sources7
Turni92 – 95Combined sources4
Beta strandi97 – 101Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10731-107[»]
3J6Yelectron microscopy6.10731-107[»]
3J77electron microscopy6.20831-107[»]
3J78electron microscopy6.30831-107[»]
3JCTelectron microscopy3.08f1-107[»]
4U3MX-ray3.00O3/o32-107[»]
4U3NX-ray3.20O3/o32-107[»]
4U3UX-ray2.90O3/o32-107[»]
4U4NX-ray3.10O3/o32-107[»]
4U4OX-ray3.60O3/o32-107[»]
4U4QX-ray3.00O3/o32-107[»]
4U4RX-ray2.80O3/o32-107[»]
4U4UX-ray3.00O3/o32-107[»]
4U4YX-ray3.20O3/o32-107[»]
4U4ZX-ray3.10O3/o32-107[»]
4U50X-ray3.20O3/o32-107[»]
4U51X-ray3.20O3/o32-107[»]
4U52X-ray3.00O3/o32-107[»]
4U53X-ray3.30O3/o32-107[»]
4U55X-ray3.20O3/o32-107[»]
4U56X-ray3.45O3/o32-107[»]
4U6FX-ray3.10O3/o32-107[»]
4V6Ielectron microscopy8.80Bj1-107[»]
4V7Felectron microscopy8.70e1-107[»]
4V88X-ray3.00Bf/Df1-107[»]
4V8Telectron microscopy8.10f1-107[»]
4V8Yelectron microscopy4.30Bf2-107[»]
4V8Zelectron microscopy6.60Bf2-107[»]
4V91electron microscopy3.70f1-107[»]
5APNelectron microscopy3.91f1-107[»]
5APOelectron microscopy3.41f1-107[»]
5DATX-ray3.15O3/o32-107[»]
5DC3X-ray3.25O3/o32-107[»]
5DGEX-ray3.45O3/o32-107[»]
5DGFX-ray3.30O3/o32-107[»]
5DGVX-ray3.10O3/o32-107[»]
5FCIX-ray3.40O3/o32-107[»]
5FCJX-ray3.10O3/o32-107[»]
5FL8electron microscopy9.50f1-107[»]
5GAKelectron microscopy3.88h1-107[»]
5H4Pelectron microscopy3.07f1-107[»]
5I4LX-ray3.10O3/o32-107[»]
5JCSelectron microscopy9.50f1-107[»]
5JUOelectron microscopy4.00KA1-107[»]
5JUPelectron microscopy3.50KA1-107[»]
5JUSelectron microscopy4.20KA1-107[»]
5JUTelectron microscopy4.00KA1-107[»]
5JUUelectron microscopy4.00KA1-107[»]
5LYBX-ray3.25O3/o32-107[»]
5M1Jelectron microscopy3.30f52-107[»]
5MC6electron microscopy3.80BK1-107[»]
5T62electron microscopy3.30s1-107[»]
5T6Relectron microscopy4.50s1-107[»]
5TGAX-ray3.30O3/o32-107[»]
5TGMX-ray3.50O3/o32-107[»]
ProteinModelPortaliP05744.
SMRiP05744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000195636.
InParanoidiP05744.
KOiK02917.
OMAiGERCAYV.
OrthoDBiEOG092C5MJS.

Family and domain databases

HAMAPiMF_00573. Ribosomal_L35Ae. 1 hit.
InterProiView protein in InterPro
IPR001780. Ribosomal_L35A.
IPR018266. Ribosomal_L35Ae_CS.
IPR009000. Transl_B-barrel.
PANTHERiPTHR10902. PTHR10902. 1 hit.
PfamiView protein in Pfam
PF01247. Ribosomal_L35Ae. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD012670. Ribosomal_L35Ae. 1 hit.
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiView protein in PROSITE
PS01105. RIBOSOMAL_L35AE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05744-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESHRLYVK GKHLSYQRSK RVNNPNVSLI KIEGVATPQD AQFYLGKRIA
60 70 80 90 100
YVYRASKEVR GSKIRVMWGK VTRTHGNSGV VRATFRNNLP AKTFGASVRI

FLYPSNI
Length:107
Mass (Da):12,154
Last modified:January 23, 2007 - v3
Checksum:i263E8389218B5027
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24N → D AA sequence (PubMed:18782943).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57969 Genomic DNA. Translation: CAA41035.1.
U43703 Genomic DNA. Translation: AAB68218.1.
Z73499 Genomic DNA. Translation: CAA97847.1.
BK006949 Genomic DNA. Translation: DAA11292.1.
PIRiS18431.
RefSeqiNP_015182.1. NM_001183957.1.

Genome annotation databases

EnsemblFungiiYPL143W; YPL143W; YPL143W.
GeneIDi855960.
KEGGisce:YPL143W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57969 Genomic DNA. Translation: CAA41035.1.
U43703 Genomic DNA. Translation: AAB68218.1.
Z73499 Genomic DNA. Translation: CAA97847.1.
BK006949 Genomic DNA. Translation: DAA11292.1.
PIRiS18431.
RefSeqiNP_015182.1. NM_001183957.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10731-107[»]
3J6Yelectron microscopy6.10731-107[»]
3J77electron microscopy6.20831-107[»]
3J78electron microscopy6.30831-107[»]
3JCTelectron microscopy3.08f1-107[»]
4U3MX-ray3.00O3/o32-107[»]
4U3NX-ray3.20O3/o32-107[»]
4U3UX-ray2.90O3/o32-107[»]
4U4NX-ray3.10O3/o32-107[»]
4U4OX-ray3.60O3/o32-107[»]
4U4QX-ray3.00O3/o32-107[»]
4U4RX-ray2.80O3/o32-107[»]
4U4UX-ray3.00O3/o32-107[»]
4U4YX-ray3.20O3/o32-107[»]
4U4ZX-ray3.10O3/o32-107[»]
4U50X-ray3.20O3/o32-107[»]
4U51X-ray3.20O3/o32-107[»]
4U52X-ray3.00O3/o32-107[»]
4U53X-ray3.30O3/o32-107[»]
4U55X-ray3.20O3/o32-107[»]
4U56X-ray3.45O3/o32-107[»]
4U6FX-ray3.10O3/o32-107[»]
4V6Ielectron microscopy8.80Bj1-107[»]
4V7Felectron microscopy8.70e1-107[»]
4V88X-ray3.00Bf/Df1-107[»]
4V8Telectron microscopy8.10f1-107[»]
4V8Yelectron microscopy4.30Bf2-107[»]
4V8Zelectron microscopy6.60Bf2-107[»]
4V91electron microscopy3.70f1-107[»]
5APNelectron microscopy3.91f1-107[»]
5APOelectron microscopy3.41f1-107[»]
5DATX-ray3.15O3/o32-107[»]
5DC3X-ray3.25O3/o32-107[»]
5DGEX-ray3.45O3/o32-107[»]
5DGFX-ray3.30O3/o32-107[»]
5DGVX-ray3.10O3/o32-107[»]
5FCIX-ray3.40O3/o32-107[»]
5FCJX-ray3.10O3/o32-107[»]
5FL8electron microscopy9.50f1-107[»]
5GAKelectron microscopy3.88h1-107[»]
5H4Pelectron microscopy3.07f1-107[»]
5I4LX-ray3.10O3/o32-107[»]
5JCSelectron microscopy9.50f1-107[»]
5JUOelectron microscopy4.00KA1-107[»]
5JUPelectron microscopy3.50KA1-107[»]
5JUSelectron microscopy4.20KA1-107[»]
5JUTelectron microscopy4.00KA1-107[»]
5JUUelectron microscopy4.00KA1-107[»]
5LYBX-ray3.25O3/o32-107[»]
5M1Jelectron microscopy3.30f52-107[»]
5MC6electron microscopy3.80BK1-107[»]
5T62electron microscopy3.30s1-107[»]
5T6Relectron microscopy4.50s1-107[»]
5TGAX-ray3.30O3/o32-107[»]
5TGMX-ray3.50O3/o32-107[»]
ProteinModelPortaliP05744.
SMRiP05744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36040. 106 interactors.
IntActiP05744. 15 interactors.
MINTiMINT-8285485.

Proteomic databases

MaxQBiP05744.
PRIDEiP05744.
TopDownProteomicsiP05744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL143W; YPL143W; YPL143W.
GeneIDi855960.
KEGGisce:YPL143W.

Organism-specific databases

EuPathDBiFungiDB:YPL143W.
SGDiS000006064. RPL33A.

Phylogenomic databases

HOGENOMiHOG000195636.
InParanoidiP05744.
KOiK02917.
OMAiGERCAYV.
OrthoDBiEOG092C5MJS.

Enzyme and pathway databases

BioCyciYEAST:G3O-34040-MONOMER.

Miscellaneous databases

PROiPR:P05744.

Family and domain databases

HAMAPiMF_00573. Ribosomal_L35Ae. 1 hit.
InterProiView protein in InterPro
IPR001780. Ribosomal_L35A.
IPR018266. Ribosomal_L35Ae_CS.
IPR009000. Transl_B-barrel.
PANTHERiPTHR10902. PTHR10902. 1 hit.
PfamiView protein in Pfam
PF01247. Ribosomal_L35Ae. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD012670. Ribosomal_L35Ae. 1 hit.
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiView protein in PROSITE
PS01105. RIBOSOMAL_L35AE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL33A_YEAST
AccessioniPrimary (citable) accession number: P05744
Secondary accession number(s): D6W3M6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 156 of the entry and version 3 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.