id: Q7S234
gene_symbol: NCU09880
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:367110
  label: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
description: NCU09880 is a canonical SmG protein that binds snRNA in the heptameric Sm ring. SmG-containing
  U1, U2, U4 and U5 small nuclear ribonucleoproteins assemble into the spliceosome and support pre-mRNA
  splicing. SmG also participates in the assembly intermediates that build these RNA-protein particles.
existing_annotations:
- term: &id001
    id: GO:0000387
    label: spliceosomal snRNP assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000104
  qualifier: involved_in
  supporting_entities:
  - UniRule:UR000481797
  review:
    summary: The SmG-specific domain identifies a canonical Sm-ring subunit.
    action: ACCEPT
    reason: The SmG-specific domain identifies a canonical Sm-ring subunit. Characterized yeast SmG participates
      in the U1, U2, U4 and U5 snRNP scaffolds, and mutational interactions establish its functional contribution
      to spliceosome assembly and pre-mRNA splicing.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
    - reference_id: PMID:27417296
      supporting_text: 'Tests of pairwise combinations of

        SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

        within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

        any two of the Sm subunits are lethal.'
- term:
    id: GO:0000398
    label: mRNA splicing, via spliceosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - PANTHER:PTN000058285
  - PomBase:SPBC4B4.05
  - SGD:S000002965
  - UniProtKB:P62308
  - UniProtKB:Q382A6
  review:
    summary: The SmG-specific domain identifies a canonical Sm-ring subunit.
    action: ACCEPT
    reason: The SmG-specific domain identifies a canonical Sm-ring subunit. Characterized yeast SmG participates
      in the U1, U2, U4 and U5 snRNP scaffolds, and mutational interactions establish its functional contribution
      to spliceosome assembly and pre-mRNA splicing.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
    - reference_id: PMID:27417296
      supporting_text: 'Tests of pairwise combinations of

        SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

        within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

        any two of the Sm subunits are lethal.'
- term: &id002
    id: GO:0000398
    label: mRNA splicing, via spliceosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  supporting_entities:
  - UniProtKB:P40204
  - sgd:YFL017W-A
  - InterPro:IPR034098
  - UniRule:UR000481797
  review:
    summary: The SmG-specific domain identifies a canonical Sm-ring subunit.
    action: ACCEPT
    reason: The SmG-specific domain identifies a canonical Sm-ring subunit. Characterized yeast SmG participates
      in the U1, U2, U4 and U5 snRNP scaffolds, and mutational interactions establish its functional contribution
      to spliceosome assembly and pre-mRNA splicing.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
    - reference_id: PMID:27417296
      supporting_text: 'Tests of pairwise combinations of

        SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

        within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

        any two of the Sm subunits are lethal.'
- term:
    id: GO:0003723
    label: RNA binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: contributes_to
  supporting_entities:
  - PANTHER:PTN000058283
  - SGD:S000005091
  review:
    summary: Canonical SmG contacts the snRNA Sm site within the heptameric ring.
    action: ACCEPT
    reason: Canonical SmG contacts the snRNA Sm site within the heptameric ring. Conserved RNA-contact
      mutagenesis in yeast supports RNA binding by the subunit in its normal complex context.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'Tests of pairwise combinations of

        SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

        within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

        any two of the Sm subunits are lethal.'
- term: &id003
    id: GO:0003723
    label: RNA binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  supporting_entities:
  - InterPro:IPR047575
  - UniRule:UR000481797
  - UniRule:UR001714480
  review:
    summary: Canonical SmG contacts the snRNA Sm site within the heptameric ring.
    action: ACCEPT
    reason: Canonical SmG contacts the snRNA Sm site within the heptameric ring. Conserved RNA-contact
      mutagenesis in yeast supports RNA binding by the subunit in its normal complex context.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'Tests of pairwise combinations of

        SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

        within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

        any two of the Sm subunits are lethal.'
- term: &id005
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  supporting_entities:
  - UniProtKB-SubCell:SL-0191
  review:
    summary: SmG-containing snRNPs function in nuclear pre-mRNA splicing.
    action: ACCEPT
    reason: SmG-containing snRNPs function in nuclear pre-mRNA splicing. The conserved SmG identity and
      characterized nuclear snRNP membership support nuclear localization; cytoplasmic assembly intermediates
      are compatible with this annotation.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term: &id004
    id: GO:0005681
    label: spliceosomal complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: part_of
  supporting_entities:
  - InterPro:IPR034098
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005682
    label: U5 snRNP
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - PomBase:SPBC4B4.05
  - SGD:S000002965
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005682
    label: U5 snRNP
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: part_of
  supporting_entities:
  - UniProtKB:O74966
  - PomBase:SPBC4B4.05.1:pep
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005685
    label: U1 snRNP
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - PomBase:SPBC4B4.05
  - RGD:9286705
  - SGD:S000002965
  - UniProtKB:P62308
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005685
    label: U1 snRNP
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: part_of
  supporting_entities:
  - UniProtKB:O74966
  - PomBase:SPBC4B4.05.1:pep
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005686
    label: U2 snRNP
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - PomBase:SPBC4B4.05
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005686
    label: U2 snRNP
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  supporting_entities:
  - UniProtKB:O74966
  - PomBase:SPBC4B4.05.1:pep
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005687
    label: U4 snRNP
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - SGD:S000002965
  - UniProtKB:P62308
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0005687
    label: U4 snRNP
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  supporting_entities:
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: part_of
  supporting_entities:
  - ARBA:ARBA00028902
  review:
    summary: Protein-containing complex is correct but uninformative for a canonical SmG subunit.
    action: MODIFY
    reason: Protein-containing complex is correct but uninformative for a canonical SmG subunit. Its supported
      role is in spliceosomal snRNPs and spliceosome complexes.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
    proposed_replacement_terms:
    - id: GO:0005681
      label: spliceosomal complex
- term:
    id: GO:0034719
    label: SMN-Sm protein complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - UniProtKB:P62308
  review:
    summary: SmG is a substrate subunit in the SMN-mediated Sm assembly intermediate.
    action: ACCEPT
    reason: SmG is a substrate subunit in the SMN-mediated Sm assembly intermediate. The human structure
      explicitly contains SmG in the SmD1/D2/F/E/G pentamer bound to Gemin2 and SMN. The curated ancestral
      assertion transfers this conserved assembly interaction, not a stable catalytic-spliceosome SMN
      membership.
    supported_by:
    - reference_id: PMID:21816274
      supporting_text: 'Here, we describe the 2.5 Å crystal structure of Gemin2 bound to SmD1/D2/F/E/G

        pentamer and SMN''s Gemin2-binding domain, a key assembly intermediate.'
- term:
    id: GO:0036261
    label: 7-methylguanosine cap hypermethylation
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  supporting_entities:
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: Cap hypermethylation is catalyzed by Tgs1 and is coupled to snRNP biogenesis, so a noncatalytic
      SmG contribution is plausible.
    action: UNDECIDED
    reason: Cap hypermethylation is catalyzed by Tgs1 and is coupled to snRNP biogenesis, so a noncatalytic
      SmG contribution is plausible. The retrieved experiments establish SmG-dependent ring assembly but
      do not resolve the specific SmG requirement for cap hypermethylation underlying this yeast-to-Neurospora
      transfer. This is not rejected merely because SmG lacks methyltransferase activity.
    supported_by:
    - reference_id: PMID:11983179
      supporting_text: 'Here,

        we show that yeast Tgs1p, an evolutionarily conserved protein carrying a

        signature of S-AdoMet methyltransferase, is essential for hypermethylation of

        the m(7)G caps of both snRNAs and snoRNAs.'
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0046540
    label: U4/U6 x U5 tri-snRNP complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  supporting_entities:
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0071004
    label: U2-type prespliceosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058284
  - SGD:S000002965
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0071004
    label: U2-type prespliceosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  supporting_entities:
  - UniProtKB:P40204
  - sgd:YFL017W-A
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0071011
    label: precatalytic spliceosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - UniProtKB:P62308
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0071013
    label: catalytic step 2 spliceosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058284
  - UniProtKB:P62308
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0071014
    label: post-mRNA release spliceosomal complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  supporting_entities:
  - UniProtKB:O74966
  - PomBase:SPBC4B4.05.1:pep
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
- term:
    id: GO:0097526
    label: spliceosomal tri-snRNP complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - PANTHER:PTN000058285
  - SGD:S000002965
  - UniProtKB:P62308
  review:
    summary: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog.
    action: ACCEPT
    reason: The SmG-specific subfamily distinguishes this protein from the related Lsm7 paralog. Canonical
      Sm rings scaffold U1, U2, U4 and U5 snRNPs and persist with their snRNAs through the relevant spliceosome
      intermediates, supporting these conserved memberships and the curator-established phylogenetic assignments.
    supported_by:
    - reference_id: PMID:27417296
      supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

        snRNPs that direct pre-mRNA splicing.'
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping,
    accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000104
  title: Electronic Gene Ontology annotations created by transferring manual GO annotations between related
    proteins based on shared sequence features
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl
    Compara
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:27417296
  title: Structure-function analysis and genetic interactions of the SmG, SmE, and SmF subunits of the
    yeast Sm protein ring.
  full_text_unavailable: false
- id: PMID:21816274
  title: Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP
    assembly.
  full_text_unavailable: true
- id: PMID:11983179
  title: Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase
    that is localized to the nucleolus.
  full_text_unavailable: true
- id: file:NEUCR/NCU09880/NCU09880-uniprot.txt
  title: 'UniProt record for NCU09880: domain and family evidence'
core_functions:
- description: NCU09880 is a canonical SmG protein that binds snRNA in the heptameric Sm ring. SmG-containing
    U1, U2, U4 and U5 small nuclear ribonucleoproteins assemble into the spliceosome and support pre-mRNA
    splicing. SmG also participates in the assembly intermediates that build these RNA-protein particles.
  supported_by:
  - reference_id: PMID:27417296
    supporting_text: 'A seven-subunit Sm protein ring forms a core scaffold of the U1, U2, U4, and U5

      snRNPs that direct pre-mRNA splicing.'
  - reference_id: PMID:27417296
    supporting_text: 'Tests of pairwise combinations of

      SmG, SmE, SmF, SmB, and SmD3 alleles highlighted the inherent redundancies

      within the Sm ring, whereby simultaneous mutations of the RNA binding sites of

      any two of the Sm subunits are lethal.'
  - reference_id: file:NEUCR/NCU09880/NCU09880-uniprot.txt
    supporting_text: DR   InterPro; IPR034098; Sm_G.
  directly_involved_in:
  - *id001
  - *id002
  molecular_function: *id003
  in_complex: *id004
  locations:
  - *id005
