ID F1LFY8_ASCSU Unreviewed; 94 AA.
AC F1LFY8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
GN Name=LSM5 {ECO:0000256|RuleBase:RU365055};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY49042.1};
RN [1] {ECO:0000313|EMBL:ADY49042.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- FUNCTION: Plays a role in U6 snRNP assembly and function. Binds to the
CC 3' end of U6 snRNA. {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365055}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365055}.
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DR EMBL; JI212736; ADY49042.1; -; mRNA.
DR AlphaFoldDB; F1LFY8; -.
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:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01732; LSm5; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR033871; LSm5.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR20971; U6 SNRNA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR20971:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM5; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 2: Evidence at transcript level;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365055};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365055}; Nucleus {ECO:0000256|RuleBase:RU365055};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365055};
KW RNA-binding {ECO:0000256|RuleBase:RU365055};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365055}.
FT DOMAIN 16..91
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 94 AA; 10224 MW; 20E28B43810C5BD0 CRC64;
MRGMASSTAT NPSTLLPLEL VDKCIGSRIW VIMKGEKEIV GTLTGFDDYV NMVLEDVVEY
ENTVDGKRVT KLDTILLNGN HITMLVPGGE GPDV
//
