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Database: UniProt
Entry: A0A1Y2VJJ1_9PEZI
LinkDB: A0A1Y2VJJ1_9PEZI
Original site: A0A1Y2VJJ1_9PEZI 
ID   A0A1Y2VJJ1_9PEZI        Unreviewed;        98 AA.
AC   A0A1Y2VJJ1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm2 {ECO:0000256|PIRNR:PIRNR016394};
GN   ORFNames=M434DRAFT_392323 {ECO:0000313|EMBL:OTA96888.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA96888.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA96888.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA96888.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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}.
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DR   EMBL; KZ112429; OTA96888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VJJ1; -.
DR   STRING; 1001938.A0A1Y2VJJ1; -.
DR   Proteomes; UP000194361; 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:UP000194361};
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   98 AA;  11183 MW;  119F9C8EE2813381 CRC64;
     MLFFSFFKTL IDHEVTVELK NDIQIRGTLK SVDQYLNIKL DDIQVVEEIK YPHLSSVKNV
     FIRGSVVRYV HLPANAVDIP LLEDATRREA AQQAGKGK
//
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