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Database: UniProt
Entry: A0A075B4E6_ROZAC
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ID   A0A075B4E6_ROZAC        Unreviewed;       701 AA.
AC   A0A075B4E6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=O9G_003454 {ECO:0000313|EMBL:EPZ36295.1};
OS   Rozella allomycis (strain CSF55).
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ36295.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ36295.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ36295.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT   microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
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; KE560603; EPZ36295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075B4E6; -.
DR   STRING; 988480.A0A075B4E6; -.
DR   EnsemblFungi; EPZ36295; EPZ36295; O9G_003454.
DR   HOGENOM; CLU_012507_1_0_1; -.
DR   OMA; ECLHYEP; -.
DR   OrthoDB; 5474157at2759; -.
DR   Proteomes; UP000030755; 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:0003743; F:translation initiation factor activity; IEA:EnsemblFungi.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
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; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; 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   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT   DOMAIN          510..694
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
SQ   SEQUENCE   701 AA;  79089 MW;  8E560D7AB2354F79 CRC64;
     MAPKKGNKEA AQVADNNEIR QAVVIADTFD TMFMPLTLHR PRCLMPLCNV PIIEYTLEAL
     SSAGIQEIFI YCRSHIEMIK SYLQSSKWSQ QNAIKIDILI SNRLRSVGDA LRDLDSRGLI
     IADKNPFLLV HGDLVTNLQL GKIFDEESAK MKKDPNCIMT MITIPALSTH PLRSFNDSAV
     FGYDSKSNHL IFYEPIKMNT KRITFNGESL AKHPSCRVRF DLLDCQIDIC SNEVLALLTE
     NFDYGDIRKD FVRGVLHSEI LGHSIAIHIA EEGYATRVRS SRLYDSISRD LIQRWAFPVV
     PDLNLFGKTS YSFKRPFVYL ENDIFLARTS VVQRGSMIGS GTRLGEETVI KESVLGRNCM
     IDRNCSLNSS YLLENIQVGK FCSIESSIIG SNVIIKDNVT ISRGCLIGDN VILGAGVTLA
     PFTKISSIPI KDLNEEFVSM KITDHFDENS FDQEIVGLDG KGFSWEKDSS IKEDSEAGSI
     EDEEVNFNSI GFESTKKVEE SDSETEDEFY DDDDDFEEDV IKSFKNKIQD LIKIAIENGH
     DPQHVAVELQ ACKLATDAKQ NQLLTSFYDC LDAIIFTLVQ LIDVNPQPSA LSSSVKSIFS
     KWAPLIIRFT ASASDSHSLI DIIMKHFNDR KLIKSFWIAI YTLYENDALN ENIVLEWYND
     DKWSHVDASA VAARNELSKF VDWLENASEE ESEDDDDDDD E
//
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