ID A1DNX7_NEOFI Unreviewed; 704 AA.
AC A1DNX7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=NFIA_058490 {ECO:0000313|EMBL:EAW16498.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16498.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000256|ARBA:ARBA00024813}.
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; DS027698; EAW16498.1; -; Genomic_DNA.
DR RefSeq; XP_001258395.1; XM_001258394.1.
DR AlphaFoldDB; A1DNX7; -.
DR STRING; 331117.A1DNX7; -.
DR EnsemblFungi; EAW16498; EAW16498; NFIA_058490.
DR GeneID; 4584911; -.
DR KEGG; nfi:NFIA_058490; -.
DR VEuPathDB; FungiDB:NFIA_058490; -.
DR eggNOG; KOG1461; Eukaryota.
DR HOGENOM; CLU_012507_1_0_1; -.
DR OMA; LAQSCKI; -.
DR OrthoDB; 5474157at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IEA:EnsemblFungi.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IEA:EnsemblFungi.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
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:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
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; IPR018357; Hexapep_transf_CS.
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; PS00101; HEXAPEP_TRANSFERASES; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Initiation factor {ECO:0000313|EMBL:EAW16498.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 518..693
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 431..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..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; 78386 MW; 9E9A7E563BE8D424 CRC64;
MGPKKGGGSQ AKQRGNATEE VEETLQAVVL ADTFETRFEP FTLEKPRCLL PLANTPLIEY
TFEFLANAGV EEVFLYGGAH SDQLERYINA SKWRSNSSPF KQLTFLKSTS TSVGDVMRDL
DGKHLITGDF IVVSGDVISN LPIEGALATH RARRQADKNA IMTMILREAG RNHRTKSSSV
SPVFVLDPTK DRCLHYEEIE HHSDEPSRLT IDTELISSHA EIDIRQDLID CNIDICTPDV
LSLWSDSFDY QSPRKHFLFG VLKDYELNGK TIHTHIIKDH YAARVRNLKA YDAVSKDIIS
RWTYPLCPDT NLLPGHTYDL RKGNLYAEQG VTLARSCVVG RRTVIGKGTS IGDKTTVKNT
VLGRDCKIGK NVTLDGAYIW DGVVIGDGTT VRQAIIADKV VVGNNCSVEP GALLAYEVRI
ADGVTVSEGR RITKASREED GGPPANDPDV VGEGGEGHEY FHEEDEDEDD TVSNASSGLV
YNMAQLSLST ESISTLSSEI SHFGGSRSES FGTSYSEDED ADHFVHDAAA SVYDSLKDGV
TSDVVQLELV SLRMTANASD HQVRRAVVTA FMKRTQQLIE GGKGAGEAIR DLFGTYREVV
ERCMFDRDSD EKTDQVDFLL LLQQDLVHRP RGETVLLFAA KELYDLELFE EEAYEQWWAD
ERSSASEEMR QVRSQTQQFV DWLANAEEEE SSEEEESEEE SDEE
//
