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Database: UniProt
Entry: B8MLK6_TALSN
LinkDB: B8MLK6_TALSN
Original site: B8MLK6_TALSN 
ID   B8MLK6_TALSN            Unreviewed;       166 AA.
AC   B8MLK6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN   ORFNames=TSTA_049770 {ECO:0000313|EMBL:EED15539.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED15539.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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   -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which consists
CC       of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the
CC       heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5,
CC       LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring
CC       structure with a doughnut shape. {ECO:0000256|ARBA:ARBA00025892}.
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; EQ962657; EED15539.1; -; Genomic_DNA.
DR   RefSeq; XP_002485492.1; XM_002485447.1.
DR   AlphaFoldDB; B8MLK6; -.
DR   STRING; 441959.B8MLK6; -.
DR   GeneID; 8108741; -.
DR   VEuPathDB; FungiDB:TSTA_049770; -.
DR   eggNOG; KOG1782; Eukaryota.
DR   HOGENOM; CLU_076902_0_0_1; -.
DR   InParanoid; B8MLK6; -.
DR   OMA; RTWDQFA; -.
DR   OrthoDB; 1113423at2759; -.
DR   PhylomeDB; B8MLK6; -.
DR   Proteomes; UP000001745; 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   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:UP000001745};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU365047,
KW   ECO:0000313|EMBL:EED15539.1}; RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          37..112
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   166 AA;  18761 MW;  362E2D904357E968 CRC64;
     MERLPIRENA GSPRQQGQAG SRPVPQGPPQ LPPQMFTTAA QLLDLTDKKL VLVLRDGRKL
     IGVLRSWDQF ANLVLQDTVE RIYAGNLYAE EHVGLYLVRG ENVLLLGEID LDKEDDLPES
     LNQASVKEVR ELKAKEEEER KRKDKKSVGK LQNHGFEPEH SGEVLF
//
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