ID A0A437AEM9_9PEZI Unreviewed; 145 AA.
AC A0A437AEM9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm4 {ECO:0000256|RuleBase:RU365049};
GN Name=LSM4 {ECO:0000256|RuleBase:RU365049};
GN ORFNames=DFL_000707 {ECO:0000313|EMBL:RVD89712.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD89712.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD89712.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD89712.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365049}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365049}.
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:RVD89712.1}.
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DR EMBL; SAEB01000001; RVD89712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437AEM9; -.
DR STRING; 97331.A0A437AEM9; -.
DR VEuPathDB; FungiDB:DFL_000707; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR GO; GO:0097525; C:spliceosomal snRNP complex; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01723; LSm4; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034101; Lsm4.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF16; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM4; 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:RU365049};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365049};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365049};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365049};
KW Spliceosome {ECO:0000256|RuleBase:RU365049}.
FT DOMAIN 2..75
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 80..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 145 AA; 15387 MW; EF3B839CDBB2EF64 CRC64;
MLPLTLLTTV QGHPLLVELK NGETLNGHLV SCDTWMNLTL KEVIQTSPDG ETFHRLPEAY
VRGNNIKYLR VPDEIIDIVK EQQAQQAASG DHHRSGGGDR GGGNRRGGGG GGGRGDHRGD
RGRGSGRGEF RGRGGGGRGG RGRGN
//