ID   S8ATK1_PENO1            Unreviewed;       570 AA.
AC   S8ATK1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=PDE_00083 {ECO:0000313|EMBL:EPS25152.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25152.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS25152.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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}.
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DR   EMBL; KB644408; EPS25152.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8ATK1; -.
DR   STRING; 933388.S8ATK1; -.
DR   eggNOG; KOG1462; Eukaryota.
DR   HOGENOM; CLU_016743_1_0_1; -.
DR   OrthoDB; 161736at2759; -.
DR   PhylomeDB; S8ATK1; -.
DR   Proteomes; UP000019376; 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:UP000019376}.
FT   REGION          153..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  61165 MW;  31D72DF76A430FAC CRC64;
     MPPPSAVVPS VGIQALVLCG PGVSLNTFTT NEEYPKALIP LANRPLIYYQ LSWLKKSGIT
     DITLITPPST AAPLQAALQQ NPHLTSLPSP SPSVLAPKGL DLNMGTAELL RLPEVQACIK
     TDFLLLPCDL VCEISGESLL EAWMVSQSAL GGSSTVSEGR NAHGPTSSGP GGELGGRRGG
     LTVFYQTQDR EESVKGEGTD FLAIAPLDND ESPAVSHAVD GPAALRHNLS KVVLSMPMAT
     VKEKMEHEKG LLLRHSLVET HPRVKVLTTF RDAHLYIFPY WVKELALRQE TFQSISEDLV
     GFWAKAEWQR GLGEKLGMDE IFHRDNGHSA ESASHDGESI EEEIDLLAMS TTSSRPNINV
     GKPTTATSFA SRVSNAPSGA EKEQLKIPRL LAYIQRGSAP FVRRVDSSAI LLSTALRLAK
     LESIEEAGAA ASPFALPQKI ANPDGVAQRT TITKADCLVG ENTTVESKCV IKESVIGANV
     KICSGARLQK CLIMDGAVVN SSCTLTGCIV GRRAVIGKDS VLKDCEVGDG YLIEEETDAK
     NEKFMIFEGL EDDEDMGSAG DFDEEDELGF
//