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Database: UniProt
Entry: A0A1S3IMZ2_LINUN
LinkDB: A0A1S3IMZ2_LINUN
Original site: A0A1S3IMZ2_LINUN 
ID   A0A1S3IMZ2_LINUN        Unreviewed;       133 AA.
AC   A0A1S3IMZ2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=LOC106165695 {ECO:0000313|RefSeq:XP_013399453.1};
GN   Synonyms=LSM1 {ECO:0000256|RuleBase:RU365047};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013399453.1};
RN   [1] {ECO:0000313|RefSeq:XP_013399453.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013399453.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Probably involved with other LSm subunits in the general
CC       process of degradation of mRNAs. {ECO:0000256|RuleBase:RU365047}.
CC   -!- SUBUNIT: LSm subunits form a heteromer 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   RefSeq; XP_013399453.1; XM_013543999.1.
DR   AlphaFoldDB; A0A1S3IMZ2; -.
DR   STRING; 7574.A0A1S3IMZ2; -.
DR   EnsemblMetazoa; XM_013543999.1; XP_013399453.1; LOC106165695.
DR   GeneID; 106165695; -.
DR   KEGG; lak:106165695; -.
DR   InParanoid; A0A1S3IMZ2; -.
DR   OrthoDB; 1113423at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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:UP000085678};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW   RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          5..80
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   133 AA;  15347 MW;  52BD06B0D73679B0 CRC64;
     MNYLPGTASL IEEIDKKLLV VLRDGRTLIG YLRSIDQFAN LVLHRTIERI HVGKKYGDIP
     RGIFVVRGEN VVLLGEIDME KEGQLPLEEV KIEEILAMQQ EEQTVKKQEE EKKKKALVER
     GIQPHVDQIQ EDF
//
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