IF2G_METJA
ID IF2G_METJA Reviewed; 411 AA.
AC Q58657;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=MJ1261;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 9-411 IN COMPLEX WITH ZINC.
RX PubMed=14688270; DOI=10.1074/jbc.m310418200;
RA Roll-Mecak A., Alone P., Cao C., Dever T.E., Burley S.K.;
RT "X-ray structure of translation initiation factor eIF2gamma: implications
RT for tRNA and eIF2alpha binding.";
RL J. Biol. Chem. 279:10634-10642(2004).
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:0000250|UniProtKB:Q980A5,
CC ECO:0000255|HAMAP-Rule:MF_00119};
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; L77117; AAB99264.1; -; Genomic_DNA.
DR PIR; D64457; D64457.
DR RefSeq; WP_064496772.1; NC_000909.1.
DR PDB; 1S0U; X-ray; 2.40 A; A=9-411.
DR PDBsum; 1S0U; -.
DR AlphaFoldDB; Q58657; -.
DR SMR; Q58657; -.
DR STRING; 243232.MJ_1261; -.
DR EnsemblBacteria; AAB99264; AAB99264; MJ_1261.
DR GeneID; 1452159; -.
DR KEGG; mja:MJ_1261; -.
DR eggNOG; arCOG01563; Archaea.
DR HOGENOM; CLU_027154_0_1_2; -.
DR InParanoid; Q58657; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 25592at2157; -.
DR PhylomeDB; Q58657; -.
DR EvolutionaryTrace; Q58657; -.
DR Proteomes; UP000000805; 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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
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_0000137454"
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:0000255|HAMAP-Rule:MF_00119"
FT REGION 46..50
FT /note="G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 146..149
FT /note="G4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 181..183
FT /note="G5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 21..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
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:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
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:14688270, ECO:0007744|PDB:1S0U"
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:14688270, ECO:0007744|PDB:1S0U"
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:14688270, ECO:0007744|PDB:1S0U"
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:14688270, ECO:0007744|PDB:1S0U"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 181..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q980A5, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1S0U"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1S0U"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1S0U"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1S0U"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1S0U"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:1S0U"
FT STRAND 398..411
FT /evidence="ECO:0007829|PDB:1S0U"
SQ SEQUENCE 411 AA; 44596 MW; 75D94AF71088008F CRC64;
MAKKKQAKQA EVNIGMVGHV DHGKTSLTKA LTGVWTDRHS EELRRGISIR LGYADCEIRK
CPQCGTYTTK PRCPNCLAET EFLRRVSFVD SPGHETLMAT MLSGASLMDG AILVIAANEP
CPQPQTKEHL MALEILGIDK IIIVQNKIDL VDEKQAEENY EQIKEFVKGT IAENAPIIPI
SAHHEANIDV LLKAIQDFIP TPKRDPDATP RMYVARSFDI NKPGTEIKDL KGGVLGGAII
QGVFKVGDEI EIRPGIKVTE GNKTFWKPLT TKIVSLAAGN TILRKAHPGG LIGVGTTLDP
YLTKSDALTG SVVGLPGTLP PIREKITIRA NLLDRVVGTK EELKIEPLRT GEVLMLNIGT
ATTAGVITSA RGDIADIKLK LPICAEIGDR VAISRRVGSR WRLIGYGTIE G
