ID A0A0S7DUG5_9EURO Unreviewed; 122 AA.
AC A0A0S7DUG5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D1 {ECO:0000256|RuleBase:RU365054};
DE AltName: Full=snRNP core protein D1 {ECO:0000256|RuleBase:RU365054};
GN ORFNames=ALT_001190 {ECO:0000313|EMBL:GIM38800.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38800.1};
RN [1] {ECO:0000313|EMBL:GIM38800.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38800.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome.
CC {ECO:0000256|RuleBase:RU365054}.
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which consists
CC of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the
CC heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5,
CC LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring
CC structure with a doughnut shape. {ECO:0000256|ARBA:ARBA00025892}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365054}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
CC {ECO:0000256|ARBA:ARBA00008146, ECO:0000256|RuleBase:RU365054}.
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:GIM38800.1}.
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DR EMBL; BCLY01000008; GIM38800.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DUG5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_4467; -.
DR OrthoDB; 1092654at2759; -.
DR GO; GO:0097525; C:spliceosomal snRNP complex; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR CDD; cd01724; Sm_D1; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR034102; Sm_D1.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF18; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1; 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:RU365054};
KW mRNA splicing {ECO:0000256|RuleBase:RU365054};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365054};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365054}.
FT REGION 79..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13388 MW; C092EF71EB36D9F3 CRC64;
MKLVRFLMKC ANETVTIELK NGTILHGTIT AVSPQMNTSL RTVKMTPKGR DPISLDTINI
RGSTIRYYIL PDSLPLDTLL VDDQPKPKNK ARKETDRGRG RGGGGPRGGR GRGRGRGRGR
GF
//
