ID A0A316Z070_9BASI Unreviewed; 783 AA.
AC A0A316Z070;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=FA10DRAFT_264861 {ECO:0000313|EMBL:PWN94318.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN94318.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN94318.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN94318.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819634; PWN94318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316Z070; -.
DR STRING; 215250.A0A316Z070; -.
DR InParanoid; A0A316Z070; -.
DR OrthoDB; 5474157at2759; -.
DR Proteomes; UP000245768; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR CDD; cd04197; eIF-2B_epsilon_N; 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; IPR001451; Hexapep.
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; PF00132; Hexapep; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 612..776
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 84705 MW; E42B0C9154731270 CRC64;
MPPKQGKAQR GGQAQLGPSG SRQKPGHQAQ NNEAPQEDPL VAVILADSFD SHYAPLTIDA
PRCLLPLAGV PLIDYSVEAA AIAGAQHVYV LSCAHSTQIK RYVTEELETK LHLKMQGIGV
TVMSTPEARS TGDVMRELDA KQVLRSDFLL FQPDCVTNLD LRSAVQRHKE RRKVDKDAIM
TMCATRVNER SAIRSRAEQA IHYLDPTTSQ VLHYETQYPH SSQPTKRATL PGELLQFDDK
SGHADIDVRT DLIGAGVDIC SIDVPPLFSE NFDYQSLPLD FIPGILTSDL LDSKIFVEIK
SNAYSARAKD TVTFDAIAQD VLRRWTSPMA PGSSAWIGGM YAEKPGWRYI GEGVKMDRTV
TLGNNVMVGS KTTLGTSSSA SRSVLGSGVT VGSSSSITGS HLFDNVKVGS NCHIERSIIG
QGAQILDGVT LGKGCLIGGG CIVGPNVKLA AGTRVGRRSI SDVEEDDWGS EQSVEGSSAP
ADAALGSKAA GYLWPNVLSH QSEGGKGQGS DEDDSEEEEG DEEEDLATRR VRALGYDEPR
AAEQTRGDGR DGDEDDESVS SIEGDSELSA SDGEDDDDDT KSAVSSTISG VGNINLTLDD
AADTAAEQAQ RKSQLQEFKN EAVASLTRAF DEGHTTDNAA IELKTLRMAS NVALAEVRRI
AIDFLLQRCD ANKPKDVEAL LNRWGPLLAN VAADDQVEAL VMVQSYCASH PATHGALFVP
LLKKFYNDDV VSDESIVAWW RAKESRMGSE KMVELRQRAE GVVRYILEDD EDEDDDDEDD
DDE
//
