ID A0A0R3S4E7_9BILA Unreviewed; 640 AA.
AC A0A0R3S4E7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000966601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000966601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0R3S4E7; -.
DR STRING; 1147741.A0A0R3S4E7; -.
DR WBParaSite; EEL_0000966601-mRNA-1; EEL_0000966601-mRNA-1; EEL_0000966601.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
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; 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 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}.
FT DOMAIN 476..640
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
SQ SEQUENCE 640 AA; 73102 MW; DC06A75304F98A72 CRC64;
MGRKENKADT SETKEEPFKV LIIADTFDAR FLPITSDSSI SCVRIANIGI LHHMLEWISR
TELRDVIIAL SSHPEGAIQR IINYWRMLFD SFVVILCQNC MSIGDALREV HSRCVIKSDF
LLLTTPMTIA ATDLSAQISS FKEIRKDKNN VMLVIYGEWK NKCPVIAYEK KSGRLIFYHQ
KDDASKLDVD KDVFAADSVV CNNLRDTGIT FCSLNVLVQF SDNFDFQCKD DLIREILVNE
EILSQKIYVS ILPKQIPAFC AHDYSDLLLM NKLLLQRFFF PLVPDNNSYS TYICRRNNIY
TPSDNLQPNH EPKRTLPSIC DGANVLLGKN CSIGLDVVLK NVSIGSDTSI GDGCEIVDCI
IGRGVSIGTK THLSECYIAD DVIIGDNVIL LPRCIVSSKV IIRDGKKLPS GSVISTEHYE
DDHEQFECIP SEYGFEWRMK NGRDFWHTTC SNLQLRGTAM ISTDVDDSKE TEQAVGEKEM
DNVDRFYDEV KESMDRIAEH KEYNEQLIKN LILEINSSKL AYNITMEDVA RNVFLSFLSL
SDTFSELKKL AKNWHSLFIN YYKPIKSQIQ ALIAVEEFLS SKPNFKLLAA KVIHFFYEED
IFEEDAILEW YDTVHENATI KTLVRPIIDW LQDTTEESDD
//