IF2G_PYRFU
ID IF2G_PYRFU Reviewed; 411 AA.
AC Q8U082;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translation initiation factor 2 subunit gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00119};
DE AltName: Full=aIF2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE AltName: Full=eIF-2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
GN Name=eif2g {ECO:0000255|HAMAP-Rule:MF_00119}; OrderedLocusNames=PF1717;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2] {ECO:0007744|PDB:2D74, ECO:0007744|PDB:2DCU}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GTP; MAGNESIUM AND
RP ZINC.
RX PubMed=16924118; DOI=10.1073/pnas.0604165103;
RA Sokabe M., Yao M., Sakai N., Toya S., Tanaka I.;
RT "Structure of archaeal translational initiation factor 2 betagamma-GDP
RT reveals significant conformational change of the beta-subunit and switch 1
RT region.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13016-13021(2006).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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:0000255|HAMAP-Rule:MF_00119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00119,
CC ECO:0000269|PubMed:16924118};
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
CC -!- INTERACTION:
CC Q8U082; Q8U3I5: eif2b; NbExp=2; IntAct=EBI-2504997, EBI-2505077;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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DR EMBL; AE009950; AAL81841.1; -; Genomic_DNA.
DR RefSeq; WP_011012863.1; NZ_CP023154.1.
DR PDB; 2D74; X-ray; 2.80 A; A=1-411.
DR PDB; 2DCU; X-ray; 3.40 A; A=1-411.
DR PDBsum; 2D74; -.
DR PDBsum; 2DCU; -.
DR AlphaFoldDB; Q8U082; -.
DR SMR; Q8U082; -.
DR DIP; DIP-54412N; -.
DR IntAct; Q8U082; 2.
DR STRING; 186497.PF1717; -.
DR PRIDE; Q8U082; -.
DR EnsemblBacteria; AAL81841; AAL81841; PF1717.
DR GeneID; 41713548; -.
DR KEGG; pfu:PF1717; -.
DR PATRIC; fig|186497.12.peg.1785; -.
DR eggNOG; arCOG01563; Archaea.
DR HOGENOM; CLU_027154_0_1_2; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 25592at2157; -.
DR PhylomeDB; Q8U082; -.
DR EvolutionaryTrace; Q8U082; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00119; eIF_2_gamma; 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; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR022424; TIF2_gsu.
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 TIGRFAMs; TIGR03680; eif2g_arch; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Initiation factor; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..411
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137460"
FT DOMAIN 9..203
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 18..25
FT /note="G1"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 46..50
FT /note="G2"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 146..149
FT /note="G4"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 181..183
FT /note="G5"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT BINDING 21..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2DCU"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2DCU"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2D74,
FT ECO:0007744|PDB:2DCU"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2D74,
FT ECO:0007744|PDB:2DCU"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2D74,
FT ECO:0007744|PDB:2DCU"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2D74,
FT ECO:0007744|PDB:2DCU"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2DCU"
FT BINDING 181..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16924118, ECO:0007744|PDB:2DCU"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2DCU"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:2D74"
SQ SEQUENCE 411 AA; 45038 MW; 377B25EC26B2D88C CRC64;
MGEKRKTRQA EVNIGMVGHV DHGKTTLTKA LTGVWTDTHS EELRRGITIK IGFADAEIRR
CSNCGRYSTS PICPYCGHET EFIRRVSFID SPGHEALMTT MLAGASLMDG AILVIAANEP
CPRPQTREHL MALQIIGQKN IIIAQNKIEL VDKEKALENY RQIKEFIKGT VAENAPIIPI
SALHGANIDV LVKAIEEFIP TPKRDSNKPP KMLVLRSFDV NKPGTPPEKL VGGVLGGSIV
QGKLKVGDEI EIRPGVPYEE HGRIKYEPIT TEIVSLQAGG QFVEEAYPGG LVGIGTKLDP
YLTKGDLMAG NVVGKPGKLP PVWTDLRLEV HLLERVVGTE QELNVEPIKR KEVLLLNVGT
ARTMGLVTAL GKDEIELKLQ IPVCAEPGER VAISRQIGSR WRLIGYGIIK E
