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Database: UniProt
Entry: A0A0J8R2E3_COCIT
LinkDB: A0A0J8R2E3_COCIT
Original site: A0A0J8R2E3_COCIT 
ID   A0A0J8R2E3_COCIT        Unreviewed;        80 AA.
AC   A0A0J8R2E3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6 {ECO:0000256|ARBA:ARBA00014768};
GN   ORFNames=CISG_07433 {ECO:0000313|EMBL:KMU78916.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU78916.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS268167; KMU78916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8R2E3; -.
DR   SMR; A0A0J8R2E3; -.
DR   STRING; 454286.A0A0J8R2E3; -.
DR   Proteomes; UP000054559; 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:UP000054559};
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;  8580 MW;  38D88ADD65E4AA6C CRC64;
     MESRGAADSQ DPSAFLSGIT GASVTVKLNS GVVYKGELQS IDGYMNIALE KTQEFVNGKL
     RKSYGDVFVR GNNVLYISAD
//
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