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Database: UniProt
Entry: A0A2H3I5B2_9EURO
LinkDB: A0A2H3I5B2_9EURO
Original site: A0A2H3I5B2_9EURO 
ID   A0A2H3I5B2_9EURO        Unreviewed;       319 AA.
AC   A0A2H3I5B2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   SubName: Full=Nucleic acid-binding, OB-fold {ECO:0000313|EMBL:PCG94296.1};
GN   ORFNames=PENO1_079170 {ECO:0000313|EMBL:PCG94296.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG94296.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG94296.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG94296.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC       {ECO:0000256|ARBA:ARBA00010254}.
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:PCG94296.1}.
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DR   EMBL; NPFK01000284; PCG94296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3I5B2; -.
DR   STRING; 290292.A0A2H3I5B2; -.
DR   OrthoDB; 297148at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000266; Ribosomal_uS17.
DR   Pfam; PF00366; Ribosomal_S17; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   REGION          50..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  35684 MW;  71F5C16E4949DE16 CRC64;
     MAPSNILRSS LLLSSTVARS ATRVNAFPQT RYAAALNASS PRRSIWNFLS GDKSKDQAAT
     KGEEAETQIE EHEHVESEVE VEEQSTPLEV QHDQQQQQPD TQNLASTSTT IDTETQQPIE
     PIPIISQVKE VESELVPETL STEASWPSDL PPPSIRQYPY TLKRGTVTSV GLMSKTVRVA
     YQHREWDRKI RKYYPKTTTY LVHDPRNSLR EGDVIEFSSG APRAPSVRHV VERIISPFGS
     AVEDRPAVMT REEREEEMVA KRMTKLMRQA TKKAAAEGGE KDVQKVMREV VERKEHVGRI
     RGLVIERAAA AAAESQASA
//
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