ID E4ZG86_LEPMJ Unreviewed; 84 AA.
AC E4ZG86;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
GN Name=LSM5 {ECO:0000256|RuleBase:RU365055};
GN ORFNames=LEMA_P064320.1 {ECO:0000313|EMBL:CBX90306.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBX90306.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- FUNCTION: Plays a role in U6 snRNP assembly and function. Binds to the
CC 3' end of U6 snRNA. {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365055}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365055}.
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DR EMBL; FP929064; CBX90306.1; -; Genomic_DNA.
DR RefSeq; XP_003833671.1; XM_003833623.1.
DR AlphaFoldDB; E4ZG86; -.
DR STRING; 985895.E4ZG86; -.
DR EnsemblFungi; CBX90306; CBX90306; LEMA_P064320.1.
DR GeneID; 13292002; -.
DR eggNOG; KOG1775; Eukaryota.
DR HOGENOM; CLU_076902_6_1_1; -.
DR InParanoid; E4ZG86; -.
DR OMA; GSPIWVI; -.
DR OrthoDB; 275126at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01732; LSm5; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR033871; LSm5.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR20971; U6 SNRNA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR20971:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM5; 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 mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365055};
KW mRNA splicing {ECO:0000256|RuleBase:RU365055};
KW Nucleus {ECO:0000256|RuleBase:RU365055};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365055};
KW RNA-binding {ECO:0000256|RuleBase:RU365055};
KW Spliceosome {ECO:0000256|RuleBase:RU365055}.
FT DOMAIN 7..79
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 84 AA; 9113 MW; 781CEA1E6074ECB3 CRC64;
MALENLLPLE LIDKCVGSQI WVIMNGGKEF TGKLVGFDDY VNMVLEDVTE IDASEGNVKL
PKILLNGNNI CMMVPGGDGE TVLE
//