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Database: UniProt
Entry: J6EFH1_SACK1
LinkDB: J6EFH1_SACK1
Original site: J6EFH1_SACK1 
ID   J6EFH1_SACK1            Unreviewed;       172 AA.
AC   J6EFH1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=YJL124C {ECO:0000313|EMBL:EJT42849.1};
GN   Synonyms=LSM1 {ECO:0000256|RuleBase:RU365047}, SKDI10G0960
GN   {ECO:0000313|EMBL:CAI4043590.1};
GN   ORFNames=SKDI_10G0960 {ECO:0000313|EMBL:CAI4043590.1}, SKUD_136503
GN   {ECO:0000313|EMBL:EJT42849.1};
OS   Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS   NBRC 1802 / NCYC 2889) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT42849.1, ECO:0000313|Proteomes:UP000002753};
RN   [1] {ECO:0000313|EMBL:EJT42849.1, ECO:0000313|Proteomes:UP000002753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC   {ECO:0000313|EMBL:EJT42849.1};
RX   PubMed=12775844; DOI=10.1126/science.1084337;
RA   Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA   Waterston R., Cohen B.A., Johnston M.;
RT   "Finding functional features in Saccharomyces genomes by phylogenetic
RT   footprinting.";
RL   Science 301:71-76(2003).
RN   [2] {ECO:0000313|EMBL:EJT42849.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT42849.1};
RA   Cliften P.F., Johnston M.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000002753}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753};
RX   PubMed=22384314; DOI=10.1534/g3.111.000273;
RA   Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA   Rine J., Johnston M., Hittinger C.T.;
RT   "The awesome power of yeast evolutionary genetics: New genome sequences and
RT   strain resources for the Saccharomyces sensu stricto genus.";
RL   G3 (Bethesda) 1:11-25(2011).
RN   [4] {ECO:0000313|EMBL:EJT42849.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT42849.1};
RA   Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA   Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CAI4043590.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4043590.1};
RA   Byrne P K.;
RL   Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; OX365905; CAI4043590.1; -; Genomic_DNA.
DR   EMBL; AACI03001146; EJT42849.1; -; Genomic_DNA.
DR   AlphaFoldDB; J6EFH1; -.
DR   STRING; 226230.J6EFH1; -.
DR   HOGENOM; CLU_076902_0_1_1; -.
DR   Proteomes; UP000002753; Unassembled WGS sequence.
DR   Proteomes; UP001162087; Chromosome 10.
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:UP000002753};
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"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   172 AA;  20521 MW;  6D4034C410827D0D CRC64;
     MSTNSRERNQ PNQDNKRQQQ SFSKKISEGE ADLYLDQYNF TTTAAIVSSV DRKIFVLLRD
     GRMLFGVLRT FDQYANLILQ DCVERIYFSE ENKYAEEDRG IFMIRGENVV MLGEVDIDKE
     DQPLEIMERI PFREAWQIKQ QNDEKRFKEE THKGKEMARH GIVYDFHRSD MY
//
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