ID A0A165IDX5_9APHY Unreviewed; 83 AA.
AC A0A165IDX5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Sm protein F {ECO:0000256|ARBA:ARBA00030144};
GN ORFNames=LAESUDRAFT_808444 {ECO:0000313|EMBL:KZT12945.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12945.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12945.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12945.1,
RC ECO:0000313|Proteomes:UP000076871};
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427605; KZT12945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IDX5; -.
DR STRING; 1314785.A0A165IDX5; -.
DR InParanoid; A0A165IDX5; -.
DR OrthoDB; 20767at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
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 8..80
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 83 AA; 9245 MW; 9AA519D27B0DE3D2 CRC64;
MSAVNPVNPK PFIQELTGKP VYVKLKWGLE YKGFLVSTDG YMNLQLANTE EFQDGKSNGA
LGEVFIRCNN VLYIREAPPA PPE
//
