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Database: UniProt
Entry: A0A0A2L1F8_PENIT
LinkDB: A0A0A2L1F8_PENIT
Original site: A0A0A2L1F8_PENIT 
ID   A0A0A2L1F8_PENIT        Unreviewed;       188 AA.
AC   A0A0A2L1F8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Ribosomal protein S4/S9 {ECO:0000313|EMBL:KGO73859.1};
GN   ORFNames=PITC_035750 {ECO:0000313|EMBL:KGO73859.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73859.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO73859.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73859.1,
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000256|ARBA:ARBA00007465}.
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:KGO73859.1}.
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DR   EMBL; JQGA01000771; KGO73859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L1F8; -.
DR   STRING; 40296.A0A0A2L1F8; -.
DR   HOGENOM; CLU_097281_0_0_1; -.
DR   OMA; FRIKHEQ; -.
DR   OrthoDB; 5473811at2759; -.
DR   PhylomeDB; A0A0A2L1F8; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   InterPro; IPR022801; Ribosomal_uS4.
DR   InterPro; IPR001912; Ribosomal_uS4_N.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR   PANTHER; PTHR11831:SF1; U3 SMALL NUCLEOLAR RIBONUCLEOPROTEIN PROTEIN IMP3; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000313|EMBL:KGO73859.1};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00182}.
FT   DOMAIN          4..113
FT                   /note="Small ribosomal subunit protein uS4 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01390"
FT   DOMAIN          114..180
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   188 AA;  22177 MW;  D2715D89A431B6B3 CRC64;
     MVRELKHHEK KLLRKVDFHN YKSDGNHREH EIRQRYLLQD PMDYRKYNAL CGSLRQLAHK
     LSQLDPDADP LRKKLESELL EKLWRMGILK QSREQGAGLS KVEREVTVSA LCRRRLAVFM
     VRSGMVETIK AATTFIEQGH VRVGTEVVND PAFLVTRNME DFVTWVDSSK IKRNILRYRE
     KLDDFDLL
//
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