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Database: UniProt
Entry: A0A0J0XXS4_9TREE
LinkDB: A0A0J0XXS4_9TREE
Original site: A0A0J0XXS4_9TREE 
ID   A0A0J0XXS4_9TREE        Unreviewed;       135 AA.
AC   A0A0J0XXS4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN   ORFNames=CC85DRAFT_306392 {ECO:0000313|EMBL:KLT45861.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT45861.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT45861.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT45861.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) 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; KQ087179; KLT45861.1; -; Genomic_DNA.
DR   RefSeq; XP_018282352.1; XM_018425691.1.
DR   AlphaFoldDB; A0A0J0XXS4; -.
DR   STRING; 879819.A0A0J0XXS4; -.
DR   GeneID; 28986294; -.
DR   OrthoDB; 1113423at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
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   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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:UP000053611};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU365047};
KW   RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          8..83
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   135 AA;  15434 MW;  7EDA4039EA228984 CRC64;
     MDALIQFTTS GSLVDLVDKK VLVMLRDGRK LIGVLRSYDQ FANFLLESTV ERLHLGHEFA
     EADIGVLLIR GENVVALGEI DLILEDEVPL RQISEEEMKA KLKEFERRRE RDNSIKDRVM
     TSIGFVSDRH EGDAY
//
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