ID A8QDC2_MALGO Unreviewed; 789 AA.
AC A8QDC2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=MGL_4182 {ECO:0000313|EMBL:EDP41489.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP41489.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP41489.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP41489.1}.
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DR EMBL; AAYY01000021; EDP41489.1; -; Genomic_DNA.
DR RefSeq; XP_001728703.1; XM_001728651.1.
DR AlphaFoldDB; A8QDC2; -.
DR STRING; 425265.A8QDC2; -.
DR GeneID; 5852992; -.
DR KEGG; mgl:MGL_4182; -.
DR VEuPathDB; FungiDB:MGL_4182; -.
DR InParanoid; A8QDC2; -.
DR OMA; ECLHYEP; -.
DR OrthoDB; 5474157at2759; -.
DR Proteomes; UP000008837; 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; 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; PF02020; W2; 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:UP000008837}.
FT DOMAIN 598..773
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 533..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 86528 MW; 2761FA02048E7794 CRC64;
MAPDEVDQED PLQAVVLCDV FNQRFAPLTL DHPRCLLPVC NVPLIEWTLE SLASAGVQEV
FLLATWHVEK VREYLEKHHP LLFKPQSSRS QGPSATSLSR ISLIPVPEAR SVGDAMRELD
ARQVIKSDFV LVHGDSLGNL DIASVVRAHK ERRRVDRNAI MTICAMSVAE NSRARRHGDL
SVFTLVPNTS QLVHYTSIPA IPRVALLKLP LELFESARDL DVRNDLVDCG VDVCAIDVPP
LFTENFDYQS LRREFVQGIL TSDLLEAKIF MHVSPPASST STSAGEPFST VSGGVLGSPT
YGAGYMLRVC DPARYDAVSR DVLAGWTFPY TPRLGMPDGA KYTKSSGSCF VSDRVTISSS
ASIGRRTMLD AHTRIEDGAI VGESVLGKNV LVGPGSVVRH SYLWDSVSVG RNCTIDGCIL
GVGVQIMDHV HLAHGTMVGD GCIIGPDVSL APFSRVSMHA YRTSEDDSGD EDMDTDADTA
LGKASRGCLW ASLDAAAASL AHDESDDDDV DVLEHPRNAK LFMIRPDTSG VELSDAASDL
SSIDADSEPG LMGSDMGDSD DEDSDLSSSL SANGYGSMSL TLPGGTESQT YGEKLETEER
VREFENEARA SLERAFEEKH APENAAIELK TLRMASNVPP GEVRKVVVSF LLGRCSVERA
KETADLLDHW GPLLQEVAQD DQVEALALMQ SYCALHLSHT RLFLPLLKKV YNDEIVSDEA
ILTWWRHPSS RHVVLHDEHK KADAQQVVLE LRKRAEPVVR HILETDDDDD EDDDDEEEEE
EDEDDDDDE
//
