ID F1A088_DICPU Unreviewed; 131 AA.
AC F1A088;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN ORFNames=DICPUDRAFT_157882 {ECO:0000313|EMBL:EGC30382.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC30382.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: Probably involved with other LSm subunits in the general
CC process of degradation of mRNAs. {ECO:0000256|RuleBase:RU365047}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a donut shape.
CC {ECO:0000256|RuleBase:RU365047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365047}.
CC Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365047}.
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DR EMBL; GL871333; EGC30382.1; -; Genomic_DNA.
DR RefSeq; XP_003293079.1; XM_003293031.1.
DR AlphaFoldDB; F1A088; -.
DR STRING; 5786.F1A088; -.
DR EnsemblProtists; EGC30382; EGC30382; DICPUDRAFT_157882.
DR GeneID; 10510636; -.
DR KEGG; dpp:DICPUDRAFT_157882; -.
DR eggNOG; KOG1782; Eukaryota.
DR InParanoid; F1A088; -.
DR OMA; IHVGREY; -.
DR OrthoDB; 1113423at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd01728; LSm1; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034104; Lsm1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR15588; LSM1; 1.
DR PANTHER; PTHR15588:SF8; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM1; 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 Cytoplasm {ECO:0000256|RuleBase:RU365047};
KW mRNA processing {ECO:0000256|RuleBase:RU365047};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 2..77
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 131 AA; 14973 MW; A3E1E790478813E7 CRC64;
MSGNSGLGDE VDKKLIVVLR DGRKFIGMMR TFDQFANIVL QDTIERIYVG DCYSDKNLGV
FFIRGDNVVI LGEIDPDREV QEKKLKKVSW DEITKAAALE KQKKEEEELL KRKIMTESGL
TIDSILNIDD F
//
