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

U6 snRNA-associated Sm-like protein LSm7

Gene

LSM7

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 LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM7 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM7, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA.5 Publications

GO - Molecular functioni

GO - Biological processi

  • maturation of SSU-rRNA Source: SGD
  • mRNA splicing, via spliceosome Source: SGD
  • nuclear-transcribed mRNA catabolic process Source: SGD
  • tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, rRNA processing, tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33165-MONOMER.
ReactomeiR-SCE-430039. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
U6 snRNA-associated Sm-like protein LSm7
Gene namesi
Name:LSM7
Ordered Locus Names:YNL147W
ORF Names:N1202, N1780
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL147W.
SGDiS000005091. LSM7.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: GO_Central
  • cytoplasm Source: SGD
  • Lsm1-7-Pat1 complex Source: SGD
  • nucleolus Source: SGD
  • small nucleolar ribonucleoprotein complex Source: SGD
  • U12-type spliceosomal complex Source: GO_Central
  • U2-type prespliceosome Source: GO_Central
  • U4/U6 x U5 tri-snRNP complex Source: SGD
  • U6 snRNP Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95R → A: Slightly reduces affinity for poly-U RNA ends. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001255811 – 115U6 snRNA-associated Sm-like protein LSm7Add BLAST115

Proteomic databases

MaxQBiP53905.
PRIDEiP53905.

Interactioni

Subunit structurei

Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the spliceosome U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHH1P395173EBI-141,EBI-158
LSM2P382033EBI-141,EBI-180
LSM4P400703EBI-141,EBI-188
PAT1P256443EBI-141,EBI-204
PRP24P499603EBI-141,EBI-212
PRP4P200533EBI-141,EBI-219

Protein-protein interaction databases

BioGridi35681. 364 interactors.
DIPiDIP-1419N.
IntActiP53905. 26 interactors.
MINTiMINT-398907.

Structurei

Secondary structure

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 33Combined sources4
Beta strandi36 – 42Combined sources7
Turni43 – 45Combined sources3
Beta strandi47 – 55Combined sources9
Beta strandi61 – 69Combined sources9
Beta strandi86 – 94Combined sources9
Helixi96 – 98Combined sources3
Beta strandi99 – 105Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCMelectron microscopy3.80g1-115[»]
4C8QX-ray3.70G1-115[»]
4C92X-ray2.30G1-115[»]
4M75X-ray2.95F/M1-115[»]
4M77X-ray3.11F/M1-115[»]
4M78X-ray2.79F/M1-115[»]
4M7AX-ray2.78F/M1-115[»]
4M7DX-ray2.60F/M1-115[»]
5GANelectron microscopy3.6071-115[»]
ProteinModelPortaliP53905.
SMRiP53905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

GeneTreeiENSGT00510000047872.
HOGENOMiHOG000223548.
InParanoidiP53905.
KOiK12626.
OMAiKKFEGPK.
OrthoDBiEOG092C5VL3.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

P53905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHQQHSKSEN KPQQQRKKFE GPKREAILDL AKYKDSKIRV KLMGGKLVIG
60 70 80 90 100
VLKGYDQLMN LVLDDTVEYM SNPDDENNTE LISKNARKLG LTVIRGTILV
110
SLSSAEGSDV LYMQK
Length:115
Mass (Da):13,006
Last modified:June 26, 2007 - v2
Checksum:iEA1D019FC5D1B5C5
GO

Sequence cautioni

The sequence CAA86879 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAA96030 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46843 Genomic DNA. Translation: CAA86879.1. Sequence problems.
Z71423 Genomic DNA. Translation: CAA96030.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10401.1.
PIRiS55137.
RefSeqiNP_014252.2. NM_001182985.1.

Genome annotation databases

EnsemblFungiiYNL147W; YNL147W; YNL147W.
GeneIDi855575.
KEGGisce:YNL147W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46843 Genomic DNA. Translation: CAA86879.1. Sequence problems.
Z71423 Genomic DNA. Translation: CAA96030.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10401.1.
PIRiS55137.
RefSeqiNP_014252.2. NM_001182985.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCMelectron microscopy3.80g1-115[»]
4C8QX-ray3.70G1-115[»]
4C92X-ray2.30G1-115[»]
4M75X-ray2.95F/M1-115[»]
4M77X-ray3.11F/M1-115[»]
4M78X-ray2.79F/M1-115[»]
4M7AX-ray2.78F/M1-115[»]
4M7DX-ray2.60F/M1-115[»]
5GANelectron microscopy3.6071-115[»]
ProteinModelPortaliP53905.
SMRiP53905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35681. 364 interactors.
DIPiDIP-1419N.
IntActiP53905. 26 interactors.
MINTiMINT-398907.

Proteomic databases

MaxQBiP53905.
PRIDEiP53905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL147W; YNL147W; YNL147W.
GeneIDi855575.
KEGGisce:YNL147W.

Organism-specific databases

EuPathDBiFungiDB:YNL147W.
SGDiS000005091. LSM7.

Phylogenomic databases

GeneTreeiENSGT00510000047872.
HOGENOMiHOG000223548.
InParanoidiP53905.
KOiK12626.
OMAiKKFEGPK.
OrthoDBiEOG092C5VL3.

Enzyme and pathway databases

BioCyciYEAST:G3O-33165-MONOMER.
ReactomeiR-SCE-430039. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

PROiP53905.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLSM7_YEAST
AccessioniPrimary (citable) accession number: P53905
Secondary accession number(s): D6W135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 26, 2007
Last modified: November 2, 2016
This is version 142 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 3070 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.