ID F2SHF0_TRIRC Unreviewed; 80 AA.
AC F2SHF0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6 {ECO:0000256|ARBA:ARBA00014768};
GN ORFNames=TERG_01681 {ECO:0000313|EMBL:EGD85408.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD85408.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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. {ECO:0000256|ARBA:ARBA00025365}.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR006609}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000256|ARBA:ARBA00007927,
CC ECO:0000256|PIRNR:PIRNR006609}.
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DR EMBL; GG700649; EGD85408.1; -; Genomic_DNA.
DR RefSeq; XP_003236957.1; XM_003236909.1.
DR AlphaFoldDB; F2SHF0; -.
DR STRING; 559305.F2SHF0; -.
DR GeneID; 10373413; -.
DR eggNOG; KOG1783; Eukaryota.
DR HOGENOM; CLU_076902_7_4_1; -.
DR InParanoid; F2SHF0; -.
DR OMA; EQTVEYV; -.
DR OrthoDB; 412at2759; -.
DR Proteomes; UP000008864; 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-UniRule.
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 {ECO:0000256|ARBA:ARBA00022490};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR006609};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|PIRNR:PIRNR006609}; Nucleus {ECO:0000256|PIRNR:PIRNR006609};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR006609};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006609};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR006609};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 11..80
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 80 AA; 8612 MW; 408A30A05238DF09 CRC64;
MEATSASEGK DPSAFLGEIT GAPVTVKLNS GVVYKGELQS VDGYMNIALE KTEEYVNGKM
RRSYGDAFVR GNNVLYISAD
//
