ID A0A4Y8CZH1_9HELO Unreviewed; 94 AA.
AC A0A4Y8CZH1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Small nuclear ribonucleoprotein E {ECO:0000256|RuleBase:RU365053};
DE Short=snRNP-E {ECO:0000256|RuleBase:RU365053};
DE AltName: Full=Sm protein E {ECO:0000256|RuleBase:RU365053};
GN ORFNames=BOTCAL_0208g00110 {ECO:0000313|EMBL:TEY57695.1};
OS Botryotinia calthae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botryotinia.
OX NCBI_TaxID=38488 {ECO:0000313|EMBL:TEY57695.1, ECO:0000313|Proteomes:UP000297299};
RN [1] {ECO:0000313|EMBL:TEY57695.1, ECO:0000313|Proteomes:UP000297299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL2830 {ECO:0000313|EMBL:TEY57695.1,
RC ECO:0000313|Proteomes:UP000297299};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing. Binds and is required for the
CC stability of snRNA U1, U2, U4 and U5 which contain a highly conserved
CC structural motif called the Sm binding site. Involved in cap
CC modification. {ECO:0000256|RuleBase:RU365053}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365053}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365053}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TEY57695.1}.
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DR EMBL; PHWZ01000208; TEY57695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y8CZH1; -.
DR STRING; 38488.A0A4Y8CZH1; -.
DR Proteomes; UP000297299; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005685; C:U1 snRNP; IEA:UniProtKB-UniRule.
DR GO; GO:0005686; C:U2 snRNP; IEA:UniProtKB-UniRule.
DR GO; GO:0005687; C:U4 snRNP; IEA:UniProtKB-UniRule.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005682; C:U5 snRNP; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR CDD; cd01718; Sm_E; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR027078; snRNP-E.
DR PANTHER; PTHR11193; SMALL NUCLEAR RIBONUCLEOPROTEIN E; 1.
DR PANTHER; PTHR11193:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN E; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|RuleBase:RU365053};
KW mRNA splicing {ECO:0000256|RuleBase:RU365053};
KW Nucleus {ECO:0000256|RuleBase:RU365053};
KW Reference proteome {ECO:0000313|Proteomes:UP000297299};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365053};
KW RNA-binding {ECO:0000256|RuleBase:RU365053};
KW Spliceosome {ECO:0000256|RuleBase:RU365053}.
FT DOMAIN 16..94
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 94 AA; 10492 MW; 6D5C4BEF8FBC966C CRC64;
MNRGGGGGRK VLLPPINFIF KLLQQHTPVS IWLYEQLGIR IEGKIRGFDE FMNLVLDDAV
EVRQATKDKE ESRRALGQIL LKGDNVSLIQ SASG
//
