ID A0A1X0RR56_RHIZD Unreviewed; 76 AA.
AC A0A1X0RR56;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
DE Flags: Fragment;
GN Name=LSM5 {ECO:0000256|RuleBase:RU365055};
GN ORFNames=BCV71DRAFT_187169 {ECO:0000313|EMBL:ORE14505.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE14505.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE14505.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE14505.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC -!- FUNCTION: Plays a role in U6 snRNP assembly and function. Binds to the
CC 3' end of U6 snRNA. {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365055}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365055}.
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DR EMBL; KV921468; ORE14505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0RR56; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_212915; -.
DR OMA; NNICTLI; -.
DR Proteomes; UP000242381; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01732; LSm5; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR033871; LSm5.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR20971; U6 SNRNA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR20971:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM5; 1.
DR Pfam; PF01423; LSM; 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|RuleBase:RU365055};
KW mRNA splicing {ECO:0000256|RuleBase:RU365055};
KW Nucleus {ECO:0000256|RuleBase:RU365055};
KW Reference proteome {ECO:0000313|Proteomes:UP000242381};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365055};
KW RNA-binding {ECO:0000256|RuleBase:RU365055};
KW Spliceosome {ECO:0000256|RuleBase:RU365055}.
FT DOMAIN 1..74
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ORE14505.1"
SQ SEQUENCE 76 AA; 8551 MW; 765D0578FD6081BD CRC64;
VELIDKCIGS RIWVVMKNEK EFTGKLLGFD DYVNMVLEDV TEYENTKEGY KTNKLEQILL
NGNNICVLIP GGTGPV
//
