ID J8Q0P3_SACAR Unreviewed; 172 AA.
AC J8Q0P3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN ORFNames=SU7_1738 {ECO:0000313|EMBL:EJS43183.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS43183.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS43183.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- FUNCTION: Component of the cytoplasmic LSM1-LSM7 complex which is
CC involved in mRNA degradation. {ECO:0000256|RuleBase:RU365047}.
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC seven-membered ring structure 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}.
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:EJS43183.1}.
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DR EMBL; ALIE01000111; EJS43183.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q0P3; -.
DR HOGENOM; CLU_076902_0_1_1; -.
DR OrthoDB; 1113423at2759; -.
DR Proteomes; UP000006968; Chromosome X.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000339; F:RNA cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
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:UP000006968};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 41..118
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 172 AA; 20327 MW; C03CA747A18DB5B2 CRC64;
MPANSKERNQ SSQDNKRLQQ NFSKKISEGE ADLYLDQYNF TTTAAIVSSV DRKIFVLLRD
GRMLFGVLRT FDQYANLILQ DCVERIYFSE ENKYAEEERG IFMIRGENVV MLGEVDIDKE
DQPLEAMERI PFKEAWQIKE QNDEKRFKEE TNKGKNMARH GIVYDFHKSD MY
//
