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Protein

60S ribosomal protein L37-A

Gene

RPL37A

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 the 23S rRNA.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191ZincBy similarity
Metal bindingi22 – 221ZincBy similarity
Metal bindingi34 – 341ZincBy similarity
Metal bindingi37 – 371ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 3719C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: GO_Central
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • cytoplasmic translation Source: SGD
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32308-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L37-A
Alternative name(s):
L43
YL35
YP55
Gene namesi
Name:RPL37A
Synonyms:RPL35A
Ordered Locus Names:YLR185W
ORF Names:L9470.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR185W.
SGDiS000004175. RPL37A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
  • preribosome, large subunit precursor Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 888760S ribosomal protein L37-APRO_0000139722Add
BLAST

Proteomic databases

MaxQBiP49166.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi31455. 76 interactions.
DIPiDIP-2135N.
IntActiP49166. 1 interaction.
MINTiMINT-8285347.

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Beta strandi15 – 173Combined sources
Turni20 – 223Combined sources
Beta strandi24 – 285Combined sources
Turni29 – 324Combined sources
Turni35 – 373Combined sources
Beta strandi41 – 433Combined sources
Helixi48 – 503Combined sources
Helixi51 – 577Combined sources
Helixi67 – 693Combined sources
Helixi70 – 756Combined sources
Turni76 – 783Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-Z2-53[»]
3J6Xelectron microscopy6.10771-88[»]
3J6Yelectron microscopy6.10771-88[»]
3J77electron microscopy6.20871-88[»]
3J78electron microscopy6.30871-88[»]
3JCTelectron microscopy3.08j1-88[»]
4U3MX-ray3.00O7/o72-88[»]
4U3NX-ray3.20O7/o72-88[»]
4U3UX-ray2.90O7/o72-88[»]
4U4NX-ray3.10O7/o72-88[»]
4U4OX-ray3.60O7/o72-88[»]
4U4QX-ray3.00O7/o72-88[»]
4U4RX-ray2.80O7/o72-88[»]
4U4UX-ray3.00O7/o72-88[»]
4U4YX-ray3.20O7/o72-88[»]
4U4ZX-ray3.10O7/o72-88[»]
4U50X-ray3.20O7/o72-88[»]
4U51X-ray3.20O7/o72-88[»]
4U52X-ray3.00O7/o72-88[»]
4U53X-ray3.30O7/o72-88[»]
4U55X-ray3.20O7/o72-88[»]
4U56X-ray3.45O7/o72-88[»]
4U6FX-ray3.10O7/o72-88[»]
4V4Belectron microscopy11.70BY2-88[»]
4V6Ielectron microscopy8.80Bl1-88[»]
4V7Felectron microscopy8.70h1-88[»]
4V7RX-ray4.00Bd/Dd1-88[»]
4V88X-ray3.00Bj/Dj1-88[»]
4V8Telectron microscopy8.10j1-88[»]
4V8Yelectron microscopy4.30Bj2-88[»]
4V8Zelectron microscopy6.60Bj2-88[»]
4V91electron microscopy3.70j1-88[»]
5APNelectron microscopy3.91j1-88[»]
5APOelectron microscopy3.41j1-88[»]
5DC3X-ray3.25O7/o72-88[»]
5FCIX-ray3.40O7/o72-88[»]
5FCJX-ray3.10O7/o72-88[»]
5FL8electron microscopy9.50j1-88[»]
5GAKelectron microscopy3.88l1-88[»]
5I4LX-ray3.10O7/o72-88[»]
ProteinModelPortaliP49166.
SMRiP49166. Positions 2-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49166.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L37e family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 3719C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000005254.
HOGENOMiHOG000111076.
InParanoidiP49166.
KOiK02922.
OMAiHIQKHEC.
OrthoDBiEOG092C5XPX.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00547. Ribosomal_L37e. 1 hit.
InterProiIPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01907. Ribosomal_L37e. 1 hit.
[Graphical view]
ProDomiPD005132. Ribosomal_L37e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01077. RIBOSOMAL_L37E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGTPSFGK RHNKSHTLCN RCGRRSFHVQ KKTCSSCGYP AAKTRSYNWG
60 70 80
AKAKRRHTTG TGRMRYLKHV SRRFKNGFQT GSASKASA
Length:88
Mass (Da):9,850
Last modified:January 23, 2007 - v2
Checksum:i274D249361EBE5E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731R → RR AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17246 Genomic DNA. Translation: AAB67458.1.
BK006945 Genomic DNA. Translation: DAA09504.1.
PIRiS51430.
RefSeqiNP_013286.1. NM_001182072.1.

Genome annotation databases

EnsemblFungiiYLR185W; YLR185W; YLR185W.
GeneIDi850882.
KEGGisce:YLR185W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17246 Genomic DNA. Translation: AAB67458.1.
BK006945 Genomic DNA. Translation: DAA09504.1.
PIRiS51430.
RefSeqiNP_013286.1. NM_001182072.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-Z2-53[»]
3J6Xelectron microscopy6.10771-88[»]
3J6Yelectron microscopy6.10771-88[»]
3J77electron microscopy6.20871-88[»]
3J78electron microscopy6.30871-88[»]
3JCTelectron microscopy3.08j1-88[»]
4U3MX-ray3.00O7/o72-88[»]
4U3NX-ray3.20O7/o72-88[»]
4U3UX-ray2.90O7/o72-88[»]
4U4NX-ray3.10O7/o72-88[»]
4U4OX-ray3.60O7/o72-88[»]
4U4QX-ray3.00O7/o72-88[»]
4U4RX-ray2.80O7/o72-88[»]
4U4UX-ray3.00O7/o72-88[»]
4U4YX-ray3.20O7/o72-88[»]
4U4ZX-ray3.10O7/o72-88[»]
4U50X-ray3.20O7/o72-88[»]
4U51X-ray3.20O7/o72-88[»]
4U52X-ray3.00O7/o72-88[»]
4U53X-ray3.30O7/o72-88[»]
4U55X-ray3.20O7/o72-88[»]
4U56X-ray3.45O7/o72-88[»]
4U6FX-ray3.10O7/o72-88[»]
4V4Belectron microscopy11.70BY2-88[»]
4V6Ielectron microscopy8.80Bl1-88[»]
4V7Felectron microscopy8.70h1-88[»]
4V7RX-ray4.00Bd/Dd1-88[»]
4V88X-ray3.00Bj/Dj1-88[»]
4V8Telectron microscopy8.10j1-88[»]
4V8Yelectron microscopy4.30Bj2-88[»]
4V8Zelectron microscopy6.60Bj2-88[»]
4V91electron microscopy3.70j1-88[»]
5APNelectron microscopy3.91j1-88[»]
5APOelectron microscopy3.41j1-88[»]
5DC3X-ray3.25O7/o72-88[»]
5FCIX-ray3.40O7/o72-88[»]
5FCJX-ray3.10O7/o72-88[»]
5FL8electron microscopy9.50j1-88[»]
5GAKelectron microscopy3.88l1-88[»]
5I4LX-ray3.10O7/o72-88[»]
ProteinModelPortaliP49166.
SMRiP49166. Positions 2-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31455. 76 interactions.
DIPiDIP-2135N.
IntActiP49166. 1 interaction.
MINTiMINT-8285347.

Proteomic databases

MaxQBiP49166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR185W; YLR185W; YLR185W.
GeneIDi850882.
KEGGisce:YLR185W.

Organism-specific databases

EuPathDBiFungiDB:YLR185W.
SGDiS000004175. RPL37A.

Phylogenomic databases

GeneTreeiENSGT00390000005254.
HOGENOMiHOG000111076.
InParanoidiP49166.
KOiK02922.
OMAiHIQKHEC.
OrthoDBiEOG092C5XPX.

Enzyme and pathway databases

BioCyciYEAST:G3O-32308-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP49166.
PROiP49166.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00547. Ribosomal_L37e. 1 hit.
InterProiIPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01907. Ribosomal_L37e. 1 hit.
[Graphical view]
ProDomiPD005132. Ribosomal_L37e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01077. RIBOSOMAL_L37E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL37A_YEAST
AccessioniPrimary (citable) accession number: P49166
Secondary accession number(s): D6VYI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 129 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 21800 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for L37 in yeast.

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.