ID   A0A135LGF3_PENPA        Unreviewed;       543 AA.
AC   A0A135LGF3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Translation initiation factor eIF2B subunit gamma {ECO:0000256|ARBA:ARBA00044196};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit gamma {ECO:0000256|ARBA:ARBA00044229};
GN   ORFNames=PGRI_019320 {ECO:0000313|EMBL:KXG48062.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG48062.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG48062.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG48062.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC       {ECO:0000256|ARBA:ARBA00007878}.
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:KXG48062.1}.
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DR   EMBL; LHQR01000065; KXG48062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LGF3; -.
DR   STRING; 5078.A0A135LGF3; -.
DR   OMA; YPKCLIQ; -.
DR   OrthoDB; 161736at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   CDD; cd04652; LbH_eIF2B_gamma_C; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR45989; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR45989:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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:UP000070168}.
FT   REGION          151..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  59878 MW;  A698EA2E91E55A5A CRC64;
     MPPGGPMDFQ ALILCGPGGS LNTFTSKPEE YPKCLIQVAN RPMVFYAIDF CRRSGITDIT
     LITPPLSYPP LRAALDQNPY LTSFYSPPVS IVAPKGLEMT MGTADLLRLL EVQRCITTNF
     LLLPCDIICE IPGELILEAW MATQCVVGEG DNNDSKSARQ RPPPTKSFFD RQLEPRSGGL
     AVYYQTENRE ESIQEEATDF VAIAPLERDE GPMIPPPEGS PAPRFGLSKL LLTMPMDTIK
     ERMEHDKGLL IRHSLVQNFP RIRMLTTSRD AHIYVFPYWV KDLVHHQNKL ESVSEDLVGA
     WAKSAWQKGL GDKLGLTTDF NQDINDQGWS SLESSHTGAF VDKVIDLREM STTRNRLTSQ
     MQADQLHPFA ATELPLMLAY VHRGPTPFIR RVDSTGVLLS TSLFLAKLPS IEEVGRQAAS
     PFAHAHKVAY PEGVTSPSNI TKKDCLLGEN VIVESAAVIK ESVIGANCHI AASARIIRCV
     LMDGVVVESR AQLTGCVIGR RAQIGRESVL KGCEVQDANV IPKGTIARDE KFMVSETFSL
     EGV
//