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Database: UniProt
Entry: A1C7L1_ASPCL
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Original site: A1C7L1_ASPCL 
ID   A1C7L1_ASPCL            Unreviewed;        98 AA.
AC   A1C7L1;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm2 {ECO:0000256|PIRNR:PIRNR016394};
GN   ORFNames=ACLA_074190 {ECO:0000313|EMBL:EAW14382.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14382.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW14382.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC       {ECO:0000256|PIRNR:PIRNR016394}.
CC   -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which consists
CC       of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the
CC       heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5,
CC       LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring
CC       structure with a doughnut shape. {ECO:0000256|ARBA:ARBA00025892}.
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; DS027045; EAW14382.1; -; Genomic_DNA.
DR   RefSeq; XP_001275808.1; XM_001275807.1.
DR   AlphaFoldDB; A1C7L1; -.
DR   STRING; 344612.A1C7L1; -.
DR   EnsemblFungi; EAW14382; EAW14382; ACLA_074190.
DR   GeneID; 4707803; -.
DR   KEGG; act:ACLA_074190; -.
DR   VEuPathDB; FungiDB:ACLA_074190; -.
DR   eggNOG; KOG3448; Eukaryota.
DR   HOGENOM; CLU_130474_3_0_1; -.
DR   OMA; DNISCTD; -.
DR   OrthoDB; 101568at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:EnsemblFungi.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:EnsemblFungi.
DR   GO; GO:0005682; C:U5 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0005688; C:U6 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0008266; F:poly(U) RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0030620; F:U2 snRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR   GO; GO:0008033; P:tRNA processing; IEA:EnsemblFungi.
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:UP000006701};
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;  11250 MW;  55BFF29744E0AA97 CRC64;
     MLFFSFFKTL TNQTVTIELK NDIRIRGTLK SVDQYLNIKL DDVDVLDLDK YPHLSSVKNM
     FIRGSVVRYV MLPRSEVDVG LLEDATRREA ANQAGKAR
//
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