ID A0A0N4UBM2_DRAME Unreviewed; 132 AA.
AC A0A0N4UBM2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm4 {ECO:0000256|RuleBase:RU365049};
GN Name=LSM4 {ECO:0000256|RuleBase:RU365049};
GN ORFNames=DME_LOCUS8493 {ECO:0000313|EMBL:VDN58520.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000461001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000461001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN58520.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365049}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365049}.
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DR EMBL; UYYG01001169; VDN58520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4UBM2; -.
DR STRING; 318479.A0A0N4UBM2; -.
DR WBParaSite; DME_0000461001-mRNA-1; DME_0000461001-mRNA-1; DME_0000461001.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01723; LSm4; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034101; Lsm4.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF16; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM4; 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|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365049};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365049};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365049};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365049};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365049}.
FT DOMAIN 3..76
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 86..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 14881 MW; 81B099B4A1E48D7A CRC64;
MVLPLSLMRT AQNHPMLVEL KNGETYNGHL VTCDGWMNIH LRDAICTSKD GDRFLKMHEV
FIRGSTVKYL RIPDEVVELV KEEVKEVRRQ QKDQQRAKRE VQGGRGGGQS NRGTLRGGRG
GTVKGRGRSK PV
//