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Protein

U6 snRNA-associated Sm-like protein LSm5

Gene

lsm5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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. LSm5 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-SPO-430039. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
U6 snRNA-associated Sm-like protein LSm5
Gene namesi
Name:lsm5
ORF Names:SPBC20F10.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC20F10.09.
PomBaseiSPBC20F10.09. lsm5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8080U6 snRNA-associated Sm-like protein LSm5PRO_0000317307Add
BLAST

Proteomic databases

MaxQBiO42978.

Interactioni

Subunit structurei

LSm subunits form a heteromer with a doughnut shape.By similarity

Protein-protein interaction databases

BioGridi277246. 8 interactions.
MINTiMINT-4674402.

Structurei

Secondary structure

1
80
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 137Combined sources
Turni14 – 163Combined sources
Beta strandi17 – 3620Combined sources
Beta strandi42 – 5110Combined sources
Turni52 – 543Combined sources
Beta strandi57 – 659Combined sources
Beta strandi70 – 756Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SWNX-ray2.50A/D/P/S1-80[»]
4EMKX-ray2.30A1-80[»]
ProteinModelPortaliO42978.
SMRiO42978. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO42978.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

HOGENOMiHOG000223547.
InParanoidiO42978.
KOiK12624.
OMAiSRIWIAM.
OrthoDBiEOG7PZSB0.
PhylomeDBiO42978.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

O42978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMTILPLEL IDKCIGSNLW VIMKSEREFA GTLVGFDDYV NIVLKDVTEY
60 70 80
DTVTGVTEKH SEMLLNGNGM CMLIPGGKPE
Length:80
Mass (Da):8,853
Last modified:May 1, 1999 - v2
Checksum:i8F9576156A97F54C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16849.2.
PIRiT39880.
RefSeqiNP_596373.1. NM_001022294.2.

Genome annotation databases

EnsemblFungiiSPBC20F10.09.1; SPBC20F10.09.1:pep; SPBC20F10.09.
GeneIDi2540723.
KEGGispo:SPBC20F10.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16849.2.
PIRiT39880.
RefSeqiNP_596373.1. NM_001022294.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SWNX-ray2.50A/D/P/S1-80[»]
4EMKX-ray2.30A1-80[»]
ProteinModelPortaliO42978.
SMRiO42978. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277246. 8 interactions.
MINTiMINT-4674402.

Proteomic databases

MaxQBiO42978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC20F10.09.1; SPBC20F10.09.1:pep; SPBC20F10.09.
GeneIDi2540723.
KEGGispo:SPBC20F10.09.

Organism-specific databases

EuPathDBiFungiDB:SPBC20F10.09.
PomBaseiSPBC20F10.09. lsm5.

Phylogenomic databases

HOGENOMiHOG000223547.
InParanoidiO42978.
KOiK12624.
OMAiSRIWIAM.
OrthoDBiEOG7PZSB0.
PhylomeDBiO42978.

Enzyme and pathway databases

ReactomeiR-SPO-430039. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

EvolutionaryTraceiO42978.
NextBioi20801845.
PROiO42978.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLSM5_SCHPO
AccessioniPrimary (citable) accession number: O42978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.