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Database: UniProt
Entry: A0A1V6PGM5_PENDC
LinkDB: A0A1V6PGM5_PENDC
Original site: A0A1V6PGM5_PENDC 
ID   A0A1V6PGM5_PENDC        Unreviewed;       302 AA.
AC   A0A1V6PGM5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN   ORFNames=PENDEC_c005G03925 {ECO:0000313|EMBL:OQD76168.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD76168.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
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:OQD76168.1}.
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DR   EMBL; MDYL01000005; OQD76168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PGM5; -.
DR   STRING; 69771.A0A1V6PGM5; -.
DR   OMA; DVNEHQR; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000191522; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd04452; S1_IF2_alpha; 1.
DR   Gene3D; 3.30.70.1130; EIF_2_alpha; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR044126; S1_IF2_alpha.
DR   InterPro; IPR024055; TIF2_asu_C.
DR   InterPro; IPR024054; TIF2_asu_middle_sf.
DR   InterPro; IPR011488; TIF_2_asu.
DR   PANTHER; PTHR10602; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   Pfam; PF07541; EIF_2_alpha; 1.
DR   Pfam; PF00575; S1; 1.
DR   SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR   SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191522}.
FT   DOMAIN          17..75
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  34410 MW;  957509E1EA3C2155 CRC64;
     MSLTNCRFYE EKFPEVDSYV MVNVKQIAEM GAYVKLLEYD NIDGMILLSE LSRRRIRSIQ
     KLIRIGRNEV VIVLRYIDLS KRRVSPEDVV KCEERYNKSK AVHSIMRHVA EATQTPLETL
     YQKIAWPLDR KFGHSHDAFK LAITNPDVWN DVEFPSEPVK KELQEYITKR LTPHPTKVRA
     DIEVTCFGYD GIDAVKEALR TAEADNTPDN QIKVKLVAPP LYVLTSQCLD KSLGIKMLEA
     AIEKISAKIK EANGNCSVKM APKAVTEHDD AVLAELMEKR ERENQQVSGD EDDSESDADV
     PE
//
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