ID A0A120E724_9BASI Unreviewed; 86 AA.
AC A0A120E724;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6 {ECO:0000256|ARBA:ARBA00014768};
DE Flags: Fragment;
GN ORFNames=RHOSPDRAFT_12961 {ECO:0000313|EMBL:KWU43398.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU43398.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU43398.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU43398.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000256|ARBA:ARBA00007927}.
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DR EMBL; KQ954490; KWU43398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120E724; -.
DR STRING; 1305733.A0A120E724; -.
DR OrthoDB; 412at2759; -.
DR Proteomes; UP000062823; 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: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; 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 SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 28..86
FT /note="Sm"
FT /evidence="ECO:0000259|SMART:SM00651"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 86
FT /evidence="ECO:0000313|EMBL:KWU43398.1"
SQ SEQUENCE 86 AA; 9104 MW; D31B90FEC1417E9B CRC64;
MSDAAQSPPN GNDNAPAAEE QQLPGPGAFL KGVVGQPVVV RLNSGVDYRG TSCLDGYMNI
ALEQTEEYVN GQKTNEYGDA FVRGNN
//
