ID F2PHK6_TRIEC Unreviewed; 83 AA.
AC F2PHK6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
GN Name=LSM5 {ECO:0000256|RuleBase:RU365055};
GN ORFNames=TEQG_00427 {ECO:0000313|EMBL:EGE01374.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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: 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 -!- 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; DS995718; EGE01374.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PHK6; -.
DR VEuPathDB; FungiDB:TEQG_00427; -.
DR eggNOG; KOG1775; Eukaryota.
DR HOGENOM; CLU_076902_6_1_1; -.
DR Proteomes; UP000009169; 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 Ribonucleoprotein {ECO:0000256|RuleBase:RU365055,
KW ECO:0000313|EMBL:EGE01374.1}; RNA-binding {ECO:0000256|RuleBase:RU365055};
KW Spliceosome {ECO:0000256|RuleBase:RU365055}.
FT DOMAIN 5..77
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 83 AA; 8985 MW; C4E01AC23BC4C693 CRC64;
MYCCVTVELI DKCVGSKIWI VMKGDKEFCG TLLGFDDYVN MVLEDVTEFD YSGGQTKLSK
ILLNGNNVCM LIPGGEGPVS AAP
//
