ID A0A2B7X0K8_9EURO Unreviewed; 101 AA.
AC A0A2B7X0K8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D2 {ECO:0000256|RuleBase:RU365051};
DE Short=Sm-D2 {ECO:0000256|RuleBase:RU365051};
DE AltName: Full=snRNP core protein D2 {ECO:0000256|RuleBase:RU365051};
GN ORFNames=AJ80_08380 {ECO:0000313|EMBL:PGH05144.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH05144.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH05144.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH05144.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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|RuleBase:RU365051}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
CC {ECO:0000256|ARBA:ARBA00008146, ECO:0000256|RuleBase:RU365051}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH05144.1}.
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DR EMBL; PDNA01000190; PGH05144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7X0K8; -.
DR STRING; 1447883.A0A2B7X0K8; -.
DR OrthoDB; 5485754at2759; -.
DR Proteomes; UP000224634; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01720; Sm_D2; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR027248; Sm_D2.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR12777; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2; 1.
DR PANTHER; PTHR12777:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365051};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365051};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365051};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365051}.
FT DOMAIN 35..101
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 82..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 101 AA; 11607 MW; 2200E767C7C3F35D CRC64;
MADVKIQDLL NKPRNELTEY EVLTLEEHEL TTGPLSILQT ATRSHSQVLI SCRNNRKLLA
RVKAFDRHCN MVLENVKEMW TEKPKGGKGK GVNKDRFVSK M
//
