ID V2XTF2_MONRO Unreviewed; 95 AA.
AC V2XTF2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm2 {ECO:0000256|PIRNR:PIRNR016394};
GN ORFNames=Moror_6409 {ECO:0000313|EMBL:ESK97052.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK97052.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK97052.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97052.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|PIRNR:PIRNR016394}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|PIRNR:PIRNR016394}.
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:ESK97052.1}.
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DR EMBL; AWSO01000036; ESK97052.1; -; Genomic_DNA.
DR RefSeq; XP_007843663.1; XM_007845472.1.
DR AlphaFoldDB; V2XTF2; -.
DR STRING; 1381753.V2XTF2; -.
DR KEGG; mrr:Moror_6409; -.
DR HOGENOM; CLU_130474_3_0_1; -.
DR OrthoDB; 101568at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd01725; LSm2; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR13829; SNRNP CORE PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR13829:SF2; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM2; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF016394; U6_snRNA_Lsm2; 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|PIRNR:PIRNR016394};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|PIRNR:PIRNR016394};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR016394};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR016394};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR016394};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR016394}.
FT DOMAIN 2..76
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 95 AA; 10952 MW; 0C0B5BEFA70F9E8F CRC64;
MLIFSVFKTL TDQQVTVELK NDLSITGVLK SVDQFLNIRL DNIKVLDEAR HPHMMAVKNC
FIRGSVVRYV QLPAEHVDTQ LLEDATRREA QSQKR
//
