ID A0A061F873_THECC Unreviewed; 676 AA.
AC A0A061F873;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=TCM_025971 {ECO:0000313|EMBL:EOY10664.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY10664.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY10664.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(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; CM001883; EOY10664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061F873; -.
DR EnsemblPlants; EOY10664; EOY10664; TCM_025971.
DR Gramene; EOY10664; EOY10664; TCM_025971.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR001451; Hexapep.
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; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 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 Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Plastid {ECO:0000256|ARBA:ARBA00022528};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 557..676
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 439..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 75208 MW; D676FE662C9BFE70 CRC64;
MGAQKKGATA RVSEDPEELA RHPLQAILLA DSFTTKFRPI TLERPKVLLP LANIPMIDYT
LAWLESAGVE EVFVFCCAHS KQVIDYLESS DWSSQPNFLV ATIESHNSIS AGDALRLIYE
RHVIHGDFVL ISGDTVSNMS LTQALQEHKE RRKKDANAIM TMVVKQSKPS PITQQSRLGT
DELFMAINPD TKQLLCYEDK AEYSKGFISL DKTLIADNPS TVLHNDKQDC YIDICSEEVL
SLFTDNFDYQ HLRRHFVKGL LVDDIMGYKI FTHEIHSSYA ARIDNFRSYD TISKDIIQRW
TYPFVPDVLC GNSAIRVERR GTYRASEITL SRSAQIGPFI VIGQGTEIGN DTKISHSVIG
EGCTIGSNVT IEGSYIWNNV TIEDGCELRH AIVCDGVTMK SGAVLEPGVV LSFKVVVGQQ
FVVPAYSMVS LLQQPTQQDS DEELEYADSS SGNVELPSAK LNGDITSDLS ETRHGPTSEL
GTGGVGYIWS IFEGGHDEEW RHSVAPIPTD KLAKIMLDKD EDEELLTQDG NVLSPSGELK
SDSDANDSED GDNEGSRDDY VSFEKEVEAT FLRAVHENVK VDHVILEVNA LRLSYNMASV
DCAGAIFYSM MKLAVESPHS SSSELHRNAA DVITTWQNLL KSFLHDIDEE IEVILKFEEI
CLESAKEFSP LFAQTF
//
