IF2G_ENCCU
ID IF2G_ENCCU Reviewed; 439 AA.
AC O96719; Q8SSL5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF-2-gamma;
DE EC=3.6.5.3;
GN OrderedLocusNames=ECU01_0700;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GB-M1;
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "Putative elongation factor 2, from Encephalitozoon cuniculi.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimeric G-protein composed of an alpha, a beta and a gamma
CC subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000250|UniProtKB:P32481}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AJ006823; CAA07260.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24940.1; -; Genomic_DNA.
DR PIR; T43813; T43813.
DR RefSeq; XP_965905.1; XM_960812.1.
DR AlphaFoldDB; O96719; -.
DR SMR; O96719; -.
DR STRING; 284813.O96719; -.
DR GeneID; 860245; -.
DR KEGG; ecu:ECU01_0700; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0700; -.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; O96719; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 903135at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..439
FT /note="Eukaryotic translation initiation factor 2 subunit
FT gamma"
FT /id="PRO_0000137445"
FT DOMAIN 11..215
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 20..27
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 48..52
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 103..106
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 159..162
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 193..195
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 193..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT CONFLICT 10
FT /note="K -> R (in Ref. 1; CAA07260)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> F (in Ref. 1; CAA07260)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="K -> N (in Ref. 1; CAA07260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 47773 MW; C45730945FD9BCA5 CRC64;
MNDALEIMKK QATLNIGTIG HVAHGKSTIV KAISGISTIK FKAELERNIT IKLGYANAKI
YKCDSKCVRP NCYQSFGSSS PDRLSCKKCG GTLKLVRHVS FVDCPGHDVL MATMLNGTAI
MDAVLLLIAA NEPCPQPQTT EHLFAVEIMD LKKVLVVQNK IDLVSREQAL EQHDQIQKFL
KTSNVSGPVI PTAAQIGVNI PALLDFIVNY IPEPVRDSTA RPKMIVIRSF DVNRPGTRVC
EMSGGVIGGS LVTGMLRVGD KIEIRPGLVI RKGNRFVCRP FVSEIVSLKA ESIDLSEAYP
GGLIGVGTTM DPSFCKADKL VGQVMGKLGF LPSIFHKITV EYSLFPKTTI QGSSKLKEGE
HVLLNIGSTT TGSVIGRINE TSGEFDLVKP ACCEIGERIA ISRKINNHWR LIGHGEIKDG
TCIEPEYDAE IDDAQRKAD
