ID A0A165P0N4_9APHY Unreviewed; 87 AA.
AC A0A165P0N4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=DAEQUDRAFT_728841 {ECO:0000313|EMBL:KZT67613.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67613.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67613.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67613.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429074; KZT67613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165P0N4; -.
DR STRING; 1314783.A0A165P0N4; -.
DR OrthoDB; 5113494at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
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 13..87
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 87 AA; 10187 MW; 2542E71CD74B602A CRC64;
MSGRQQRVMV QPINVIFKNL QQRTKVVIWL YDNIEMRIEG RIIGFDEFMN VVVDEAAEVY
VKDAKPRREL GRILLKGDNI TLIQQVV
//
