ID LSM6_LODEL Reviewed; 80 AA.
AC A5DRQ6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 28-JUN-2023, entry version 63.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=LSM6; ORFNames=LELG_00042;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Component of LSm protein complexes, which are involved in RNA
CC processing and may function in a chaperone-like manner, facilitating
CC the efficient association of RNA processing factors with their
CC substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is
CC thought to be involved in mRNA degradation by activating the decapping
CC step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-
CC LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8
CC associates with multiple snRNP complexes containing the U6 snRNA (U4/U6
CC di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds
CC directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the
CC biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes.
CC LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by
CC targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs
CC and U3 snoRNA (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK41864.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH981524; EDK41864.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001527522.1; XM_001527472.1.
DR AlphaFoldDB; A5DRQ6; -.
DR SMR; A5DRQ6; -.
DR STRING; 379508.A5DRQ6; -.
DR GeneID; 5235585; -.
DR KEGG; lel:LELG_00042; -.
DR eggNOG; KOG1783; Eukaryota.
DR HOGENOM; CLU_076902_7_4_1; -.
DR InParanoid; A5DRQ6; -.
DR OrthoDB; 412at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0120114; C:Sm-like protein family complex; IEA:UniProt.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01726; LSm6; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR016487; Lsm6/sSmF.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 1.
DR PANTHER; PTHR11021:SF1; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM6; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF006609; snRNP_SmF; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome;
KW tRNA processing.
FT CHAIN 1..80
FT /note="U6 snRNA-associated Sm-like protein LSm6"
FT /id="PRO_0000333599"
FT DOMAIN 11..80
FT /note="Sm"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
SQ SEQUENCE 80 AA; 8845 MW; 44F81044701BCACE CRC64;
MSEAESLDRI DPSKFLGGII GSSVKVKLHN GVEYQGDLQT IDGYMNVALE NGKEVIDNKV
TKHYGDVFLR GNNVLYISEN
//
