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Database: UniProt
Entry: A0A0F8V680_9EURO
LinkDB: A0A0F8V680_9EURO
Original site: A0A0F8V680_9EURO 
ID   A0A0F8V680_9EURO        Unreviewed;       704 AA.
AC   A0A0F8V680;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Translation initiation factor eIF2B subunit epsilon {ECO:0000256|ARBA:ARBA00044144};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit epsilon {ECO:0000256|ARBA:ARBA00044345};
GN   ORFNames=ARAM_002256 {ECO:0000313|EMBL:KKK27263.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK27263.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK27263.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK27263.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK27263.1}.
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DR   EMBL; JZBS01000053; KKK27263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8V680; -.
DR   STRING; 308745.A0A0F8V680; -.
DR   OrthoDB; 5474157at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   CDD; cd04197; eIF-2B_epsilon_N; 1.
DR   CDD; cd05787; LbH_eIF2B_epsilon; 1.
DR   CDD; cd11558; W2_eIF2B_epsilon; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035543; eIF-2B_epsilon_N.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR003307; W2_domain.
DR   InterPro; IPR044123; W2_eIF2B_epsilon.
DR   PANTHER; PTHR45887; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR45887:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Initiation factor {ECO:0000313|EMBL:KKK27263.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          518..693
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          437..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..704
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  78331 MW;  E9C1F4371344B93A CRC64;
     MAPKKGGTAN KSRGNATEEV EETLQAVVLA DTFETRFEPF TLDKPRCLLP LANTPLIEYT
     FEFLANAGVE EVFLYGGAHS DQLENYINTS KWRSPSSPFK QFTFLKSTST SVGDVMRDLD
     GKHLITGDFL VVSGDVISNL PIEGALAAHR ARREADKNAI MTMILREAGG NHRTKASSVS
     PVFIVDPTKD RCLHYEEIDH YSPESSRLTI DTELLETHAE IDIRQDLIDC NIDICTPDVL
     SLWSDSFDYQ TPRKQFLFGI LKDYELNGKT IHTHIITDYY VARVRNLKAY DAISKDVISR
     WAYPLCPDTN LLPGHNYDLR KGNLYQEQGV TLARSCIVGR RTVIGQGTSI GDKTTVKNTV
     LGRNCKIGKN VTLDGAYIWD NAVIGDGTTV FQAIIADGVV VGNSCKVEPG ALISFGVKIA
     DGITVSEGMR ITKALSQEDG SQPENDADIV GEGGEGYEYV PYEDEDEDET ASNASSGLIY
     NMARLSLSTE SISTLSSEIS DYGRSRSGSF ATSVSDDDEQ DHHFVHDATT SIYDSLRDGV
     SSDVVQLELV SLRMTANASD YQVRRAVVSA FMKRIAQLME GGQGAGEAVK DIFGKYHEII
     DRALFDRERS AKTDQVDLLV LLQQDLVHRV RGETVLLFAA KELYDLEVLE EEAYEQWWAD
     ERSSNSEEMR KVRSQTQQFV DWLANAEEEE SSEEEEEESE EEDD
//
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