ID A0A0A2KZB0_PENIT Unreviewed; 117 AA.
AC A0A0A2KZB0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D3 {ECO:0000256|RuleBase:RU365050};
DE Short=Sm-D3 {ECO:0000256|RuleBase:RU365050};
DE AltName: Full=snRNP core protein D3 {ECO:0000256|RuleBase:RU365050};
GN ORFNames=PITC_045350 {ECO:0000313|EMBL:KGO69675.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO69675.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO69675.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO69675.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365050}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
CC {ECO:0000256|ARBA:ARBA00008146, ECO:0000256|RuleBase:RU365050}.
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:KGO69675.1}.
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DR EMBL; JQGA01001127; KGO69675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KZB0; -.
DR STRING; 40296.A0A0A2KZB0; -.
DR HOGENOM; CLU_099537_1_0_1; -.
DR OMA; PWLNQQN; -.
DR OrthoDB; 5474715at2759; -.
DR PhylomeDB; A0A0A2KZB0; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR GO; GO:0097525; C:spliceosomal snRNP complex; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR CDD; cd01721; Sm_D3; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR034099; SmD3.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF17; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D3; 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:RU365050};
KW mRNA splicing {ECO:0000256|RuleBase:RU365050};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365050};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365050}.
FT DOMAIN 10..82
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 117 AA; 12938 MW; 53FA0FDC51C525E0 CRC64;
MGKLTSTIGI PIKLLNEAQG HVVTIEITSG VVYRGKLLEA EDNMNVQLKD ITVTARDGRV
SHLDQVYIRG SHVRFFIVPD MLRNAPMFRT RGQRGRGVGL ARGKATVQRA RGQRGRG
//
