ID W2G591_PHYPR Unreviewed; 151 AA.
AC W2G591;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, 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=LSM1 {ECO:0000256|RuleBase:RU365047};
GN ORFNames=L915_15671 {ECO:0000313|EMBL:ETK78238.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK78238.1};
RN [1] {ECO:0000313|EMBL:ETK78238.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK78238.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KI688248; ETK78238.1; -; Genomic_DNA.
DR AlphaFoldDB; W2G591; -.
DR EnsemblProtists; ETK78238; ETK78238; L915_15671.
DR VEuPathDB; FungiDB:PPTG_15677; -.
DR Proteomes; UP000053236; 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 Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 6..81
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 17740 MW; C84E71001139048C CRC64;
MSGIFPGNSS LIQQLDKQVL MVLRDGRHLV GYLRSFDQYS NIILEDTFER HVAGGLFCDI
ELGLNIIRGD NIVLLGELVR MLVNLSNWWL CCLIAEEMNY YLHLYLQDSD KERDQPHMKR
VELEEVLEAE ERLNEEGNTS VRQQWDFEQQ H
//
