ID A0A267GIA6_9PLAT Unreviewed; 185 AA.
AC A0A267GIA6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
DE Flags: Fragment;
GN Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN ORFNames=BOX15_Mlig025268g2 {ECO:0000313|EMBL:PAA85104.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA85104.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA85104.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA85104.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA85104.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA85104.1}.
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DR EMBL; NIVC01000347; PAA85104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GIA6; -.
DR STRING; 282301.A0A267GIA6; -.
DR Proteomes; UP000215902; 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; SSF81995; beta-sandwich domain of Sec23/24; 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:UP000215902};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 52..132
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA85104.1"
SQ SEQUENCE 185 AA; 21409 MW; 24D7ED17A2C89CC1 CRC64;
RQNQKGPPGP YQQMQTPPNQ RYQQQMQQQQ QQQQQHMYPA MAVGIGQTAY LAGTATLVQD
VDKQVLVVLR DNRILIGWLR SLDQFANLML HRSVERIYVH GPDSLVRFGD IERGLYLVRG
ENVLLMGEFD PSYDANLTQV SADEILQLQH QEQEDQKKRE ERRRRAMIEC GLMPTVPDAF
DEFGL
//
