ID A0A0A2L8U4_PENIT Unreviewed; 300 AA.
AC A0A0A2L8U4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE SubName: Full=S15/NS1, RNA-binding {ECO:0000313|EMBL:KGO75591.1};
GN ORFNames=PITC_098740 {ECO:0000313|EMBL:KGO75591.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75591.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO75591.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75591.1,
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000256|ARBA:ARBA00008434, ECO:0000256|RuleBase:RU003919}.
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:KGO75591.1}.
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DR EMBL; JQGA01000456; KGO75591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L8U4; -.
DR STRING; 40296.A0A0A2L8U4; -.
DR HOGENOM; CLU_078264_0_0_1; -.
DR OMA; HLQEHRN; -.
DR OrthoDB; 2091567at2759; -.
DR PhylomeDB; A0A0A2L8U4; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR InterPro; IPR000589; Ribosomal_uS15.
DR InterPro; IPR005290; Ribosomal_uS15_bac-type.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR PANTHER; PTHR23321:SF26; 37S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23321; RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003919};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003919}.
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 33241 MW; 87E52920D7BD5E1C CRC64;
MPPRVSVQSS LKALTGSTFG SSLSTNSINT SIRAASSKVL VRRKHDPFMM AQARQRKAAN
VSRQKVLAEE RESSLGDPVK SQPTPFILEM TAIQSNSHIP SSLSEDLNYY LKSNELDTAL
DFSKDLTAPI KNPDRNAADP QAEKDALNLH NQEHKNAQEA INRIVNLNNG NTKDRVRLNI
TKCIETFGRH YTDSNLPPKP SAVAHGSAPV HPERAPRVGP DTGSAEVQAA ILTVKIMNLS
RHLETANKDK HNKRNMQLLV HKRQKLLQYV RKKERGGPRW QNLMGTLGLS DAAWKGEIAL
//
