ID A0A0D2GTQ9_9EURO Unreviewed; 93 AA.
AC A0A0D2GTQ9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Sm protein F {ECO:0000256|ARBA:ARBA00030144};
GN ORFNames=Z517_10569 {ECO:0000313|EMBL:KIW75824.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW75824.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW75824.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75824.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 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; KN846975; KIW75824.1; -; Genomic_DNA.
DR RefSeq; XP_013279632.1; XM_013424178.1.
DR AlphaFoldDB; A0A0D2GTQ9; -.
DR STRING; 1442368.A0A0D2GTQ9; -.
DR GeneID; 25310059; -.
DR VEuPathDB; FungiDB:Z517_10569; -.
DR HOGENOM; CLU_076902_12_1_1; -.
DR OrthoDB; 20767at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
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:0000387; P:spliceosomal snRNP assembly; IEA:InterPro.
DR CDD; cd01722; Sm_F; 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 InterPro; IPR034100; Sm_F.
DR PANTHER; PTHR11021:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN F; 1.
DR PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 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 mRNA processing {ECO:0000256|PIRNR:PIRNR006609};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|PIRNR:PIRNR006609};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR006609};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR006609};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006609};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR006609}.
FT DOMAIN 7..80
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 93 AA; 10623 MW; 4D13D813B45AC3F3 CRC64;
MNFTPINPRP LLQSLINDEV IIRLKWGQTE YKGRLISVDS YMNIQLSNTE EYIDRKHTGT
LGQVLIRCNN VLWISAAKGV EMNGEGPDTK MED
//
