ID A0A4P9ZAH0_9ASCO Unreviewed; 85 AA.
AC A0A4P9ZAH0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=METBISCDRAFT_18222 {ECO:0000313|EMBL:RKP29618.1};
OS Metschnikowia bicuspidata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=27322 {ECO:0000313|EMBL:RKP29618.1, ECO:0000313|Proteomes:UP000268321};
RN [1] {ECO:0000313|Proteomes:UP000268321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baker2002 {ECO:0000313|Proteomes:UP000268321};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
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}.
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DR EMBL; ML004480; RKP29618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9ZAH0; -.
DR Proteomes; UP000268321; 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:UP000268321};
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 14..85
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 85 AA; 9708 MW; DF780C2AEA047788 CRC64;
MSTVKSKKAI LPPIHLIFKY LQQQSFVTVW LHQTQRIQGR IRGFDEFMNV VMDEAHEVVA
DGTREELGRI LLKGDSITLI ASLDV
//
