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Database: UniProt
Entry: Q2GP92_CHAGB
LinkDB: Q2GP92_CHAGB
Original site: Q2GP92_CHAGB 
ID   Q2GP92_CHAGB            Unreviewed;       182 AA.
AC   Q2GP92;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN   ORFNames=CHGG_10212 {ECO:0000313|EMBL:EAQ83808.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ83808.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(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   -!- 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; CH408035; EAQ83808.1; -; Genomic_DNA.
DR   RefSeq; XP_001228139.1; XM_001228138.1.
DR   AlphaFoldDB; Q2GP92; -.
DR   STRING; 306901.Q2GP92; -.
DR   GeneID; 4396977; -.
DR   VEuPathDB; FungiDB:CHGG_10212; -.
DR   eggNOG; KOG1782; Eukaryota.
DR   HOGENOM; CLU_076902_0_0_1; -.
DR   InParanoid; Q2GP92; -.
DR   OMA; RTWDQFA; -.
DR   OrthoDB; 1113423at2759; -.
DR   Proteomes; UP000001056; 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|ARBA:ARBA00022664,
KW   ECO:0000256|RuleBase:RU365047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU365047};
KW   RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          44..128
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   182 AA;  20038 MW;  172DCC6348DB7C0B CRC64;
     MENLTISDPP PPPMQQQHGG PGGMPPALGR PPPPPQQLPA QMFTTAAQLL DLTDKKLMLA
     LRDGRKLVGI LRSWDQFANL VLQSTKERIF VPPGTAPDQV RGLYADVDRG LFLVRGENVL
     LLGEIDLDKE DDAPPGYDLA DVELVQSLAK QRKQQDKIKE KTKVKMLAKE GFEGENLGEV
     LL
//
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