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Database: UniProt
Entry: A0A1V6PWY1_9EURO
LinkDB: A0A1V6PWY1_9EURO
Original site: A0A1V6PWY1_9EURO 
ID   A0A1V6PWY1_9EURO        Unreviewed;       352 AA.
AC   A0A1V6PWY1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Translation initiation factor eIF2B subunit alpha {ECO:0000256|ARBA:ARBA00044208};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit alpha {ECO:0000256|ARBA:ARBA00044236};
GN   ORFNames=PENANT_c027G02195 {ECO:0000313|EMBL:OQD81455.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD81455.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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:OQD81455.1}.
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DR   EMBL; MDYN01000027; OQD81455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PWY1; -.
DR   STRING; 416450.A0A1V6PWY1; -.
DR   OrthoDB; 51607at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1070; Translation initiation factor eIF-2B, N-terminal domain; 1.
DR   InterPro; IPR042528; elF-2B_alpha_N.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR45860; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR45860:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 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:UP000191672}.
FT   REGION          292..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  37792 MW;  2AC9E74F28448A5B CRC64;
     MASTTESAAA ASAKPFDIVA TYNELLRSDP DLTMPIAAIE ALVLLLTQSA SSTISETLDL
     LEKSTAHLKK SIPNPIGLSA GTDLFQRYLI TTLQRPGQLG PAGDFKAIRT HLLSNGRLFI
     RRAKESRYKI ADFGRGFIRD GSTILTNGGS RAVSALLQKA ADEEGGPSAV RFRVIYVLSS
     TATTSGDSSE EPEGMETVRA LREKGVPVST IPESAVAYSL GKADMVIVGA EGVVENGGIV
     SRMGTYQIGL LAKAIGKPFY VVAESHKFVR LYPLGQYDLP IEQRVLDFKS EEDIAESTQQ
     SSETTTNEER PIELPLSASV DFTPPHLISA LITDSGVLTP SAVSEELIKI WF
//
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