ID A0A165IMW1_9BASI Unreviewed; 93 AA.
AC A0A165IMW1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm3 {ECO:0000256|RuleBase:RU365046};
GN Name=LSM3 {ECO:0000256|RuleBase:RU365046};
GN ORFNames=CALCODRAFT_480442 {ECO:0000313|EMBL:KZT60780.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60780.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60780.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60780.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|RuleBase:RU365046}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365046}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365046}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365046}.
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DR EMBL; KV423928; KZT60780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IMW1; -.
DR STRING; 1353952.A0A165IMW1; -.
DR InParanoid; A0A165IMW1; -.
DR OrthoDB; 5485754at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005688; C:U6 snRNP; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd01730; LSm3; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034105; Lsm3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR040002; Sm-like_LSM3.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR13110; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3; 1.
DR PANTHER; PTHR13110:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3; 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:RU365046};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365046};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365046};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365046};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365046};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365046}.
FT DOMAIN 10..93
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 93 AA; 10374 MW; 2DD039401A29B057 CRC64;
MADLSAQVQE PFDLVRLSLS ERVFVKLKGE RSLVGVLHAY DGHMNMIMSD VEETILMVEP
EEEANGVVQS VKRNLEMLFV RGDSVILVSP GSR
//
