IF2G_PYRAB
ID IF2G_PYRAB Reviewed; 411 AA.
AC Q9V1G0; G8ZGH1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
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}; Synonyms=aif2G;
GN OrderedLocusNames=PYRAB04670; ORFNames=PAB2040;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3] {ECO:0007744|PDB:1KJZ, ECO:0007744|PDB:1KK0, ECO:0007744|PDB:1KK1, ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-411 IN COMPLEX WITH GTP AND
RP ZINC.
RX PubMed=11927566; DOI=10.1093/emboj/21.7.1821;
RA Schmitt E., Blanquet S., Mechulam Y.;
RT "The large subunit of initiation factor aIF2 is a close structural
RT homologue of elongation factors.";
RL EMBO J. 21:1821-1832(2002).
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:11927566};
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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, ECO:0000305}.
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DR EMBL; AJ248284; CAB49389.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69850.1; -; Genomic_DNA.
DR PIR; F75163; F75163.
DR RefSeq; WP_010867591.1; NC_000868.1.
DR PDB; 1KJZ; X-ray; 1.85 A; A=2-411.
DR PDB; 1KK0; X-ray; 1.95 A; A=2-411.
DR PDB; 1KK1; X-ray; 1.80 A; A=2-411.
DR PDB; 1KK2; X-ray; 2.10 A; A=2-411.
DR PDB; 1KK3; X-ray; 1.90 A; A=2-411.
DR PDBsum; 1KJZ; -.
DR PDBsum; 1KK0; -.
DR PDBsum; 1KK1; -.
DR PDBsum; 1KK2; -.
DR PDBsum; 1KK3; -.
DR AlphaFoldDB; Q9V1G0; -.
DR SMR; Q9V1G0; -.
DR STRING; 272844.PAB2040; -.
DR EnsemblBacteria; CAB49389; CAB49389; PAB2040.
DR GeneID; 1495363; -.
DR KEGG; pab:PAB2040; -.
DR PATRIC; fig|272844.11.peg.494; -.
DR eggNOG; arCOG01563; Archaea.
DR HOGENOM; CLU_027154_0_1_2; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 25592at2157; -.
DR PhylomeDB; Q9V1G0; -.
DR EvolutionaryTrace; Q9V1G0; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Zinc.
FT CHAIN 1..411
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137459"
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:11927566, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KJZ,
FT ECO:0007744|PDB:1KK0, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KJZ,
FT ECO:0007744|PDB:1KK0, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KJZ,
FT ECO:0007744|PDB:1KK0, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KJZ,
FT ECO:0007744|PDB:1KK0, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
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:11927566, ECO:0007744|PDB:1KK1,
FT ECO:0007744|PDB:1KK2, ECO:0007744|PDB:1KK3"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1KK0"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1KJZ"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 249..260
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 263..278
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1KK1"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1KK1"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1KJZ"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1KJZ"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:1KK1"
FT STRAND 400..410
FT /evidence="ECO:0007829|PDB:1KK1"
SQ SEQUENCE 411 AA; 44931 MW; 4C7E60EC5A8C837D CRC64;
MGEKRKSRQA EVNIGMVGHV DHGKTTLTKA LTGVWTDTHS EELRRGITIK IGFADAEIRR
CPNCGRYSTS PVCPYCGHET EFVRRVSFID APGHEALMTT MLAGASLMDG AILVIAANEP
CPRPQTREHL MALQIIGQKN IIIAQNKIEL VDKEKALENY RQIKEFIEGT VAENAPIIPI
SALHGANIDV LVKAIEDFIP TPKRDPNKPP KMLVLRSFDV NKPGTPPEKL VGGVLGGSIV
QGKLKVGDEI EIRPGVPYEE HGRIKYEPIT TEIVSLQAGG QFVEEAYPGG LVGVGTKLDP
YLTKGDLMAG NVVGKPGKLP PVWDSLRLEV HLLERVVGTE QELKVEPIKR KEVLLLNVGT
ARTMGLVTGL GKDEIEVKLQ IPVCAEPGDR VAISRQIGSR WRLIGYGIIK E
