ID A0A0V1C878_TRIBR Unreviewed; 231 AA.
AC A0A0V1C878;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D1 {ECO:0000256|RuleBase:RU365054};
DE AltName: Full=snRNP core protein D1 {ECO:0000256|RuleBase:RU365054};
GN Name=Snrpd1 {ECO:0000313|EMBL:KRY45477.1};
GN ORFNames=T03_3981 {ECO:0000313|EMBL:KRY45477.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY45477.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY45477.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY45477.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRY45477.1}.
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DR EMBL; JYDI01000356; KRY45477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1C878; -.
DR STRING; 45882.A0A0V1C878; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 2.30.30.100; -; 2.
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; 2.
DR SMART; SM00651; Sm; 2.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 2.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365054};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365054};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365054};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365054};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 2..74
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 87..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 25738 MW; EC1F5DD043CEB036 CRC64;
MKLVHFLMNL SRETVTIELK NDTILHGTVT GVDVAMNTHL RAVKMTMKDG QTTQLDVMSV
RGNNIRYFIL PDTISLDCCL MNNLKKPKKK PAKDDSACGR GRFRGRGRGR GRGRGWGFRR
RGTGRITIEL KNGTILHGTI SGVDVAMNTH LRAVKMTLKD GQTVQLDVLS VRGNNIRYFI
LPETIPLDQY LVDDLPKPKR KPTTGGATRA RGRGRGRGRG FRGRGTGRSR I
//