ID B8MD11_TALSN Unreviewed; 718 AA.
AC B8MD11;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=TSTA_113610 {ECO:0000313|EMBL:EED17537.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17537.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962655; EED17537.1; -; Genomic_DNA.
DR RefSeq; XP_002481529.1; XM_002481484.1.
DR AlphaFoldDB; B8MD11; -.
DR STRING; 441959.B8MD11; -.
DR GeneID; 8101673; -.
DR VEuPathDB; FungiDB:TSTA_113610; -.
DR eggNOG; KOG1461; Eukaryota.
DR HOGENOM; CLU_012507_1_0_1; -.
DR InParanoid; B8MD11; -.
DR OMA; LAQSCKI; -.
DR OrthoDB; 5474157at2759; -.
DR PhylomeDB; B8MD11; -.
DR Proteomes; UP000001745; 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:EED17537.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 523..702
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..718
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 79691 MW; 9BB92E327E2F1CC5 CRC64;
MGPKQKGGGG GGNKQKGNAT EEVEETLQAV VFADTFETRF EPFTLEKPRC LLPLANTPLI
EYTLEFLANA GVQDVFLYGG AHSNLLEKHI STSRWKAPSS PFKKLTFLKS TSTSVGDVMR
DLDGKHLITG DFIAVSGDVI SNFPIDEVLS KHRARRQADR NAIMTMVLRE AGAQHRTKSS
SVSPVFVVDP TKDRCLHYEE IDHSDKSSSS GPARLTIDTE ILTSHAEIDI RRDLIDCNID
ICTPDVLSLW SDSFDYQSPR KHFLYGVLKD YELNGKTIHT HIIQEHYAAR VRNLKAYDAI
TKDIISRWTY PLCPDTNLLP GHTYELRRGS IYQEQGVILA RSCIVGRRTV IGQGTSIGDK
TTVTNSVLGR NCRIGKNVVL DGAYIWDGVV IGDNTEIRQA ILAGDVVVGD NCKVEPDVLL
SYGVKISNGV TVAQGTRISA APREDGSVPA NEENIVGSEG RGYEYVGEED EEDEDNRSES
SGLIYNMANL SLSTDSISTL SSEISADDEY FHGQRSDSFG TSVSEDSDRD HFQYDASNNL
YESMRDGVSA DVVALELVSL RMSANASDHQ VRHAVASSFM KRISQLISES GKGAGEAVHD
VFTRYKDVVD RCLFDKNKEA KTDQTDLLLQ IQQDLAHRAK GDTILLFTAK ELYDLDIIEE
EAFEAWWADE RSIATEELKK VRAQTQQFVD WLANASEEDD DDESEDDSED DEEEDSDE
//
