IF2G_METAC
ID IF2G_METAC Reviewed; 443 AA.
AC Q8TJT7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=MA_3690;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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 -!- 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}.
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DR EMBL; AE010299; AAM07045.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TJT7; -.
DR SMR; Q8TJT7; -.
DR STRING; 188937.MA_3690; -.
DR EnsemblBacteria; AAM07045; AAM07045; MA_3690.
DR KEGG; mac:MA_3690; -.
DR HOGENOM; CLU_027154_0_1_2; -.
DR InParanoid; Q8TJT7; -.
DR OMA; NIGMVGH; -.
DR PhylomeDB; Q8TJT7; -.
DR Proteomes; UP000002487; 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 3: Inferred from homology;
KW GTP-binding; Hydrolase; Initiation factor; Magnesium; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..443
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137453"
FT DOMAIN 38..235
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 47..54
FT /note="G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 75..79
FT /note="G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 122..125
FT /note="G3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 178..181
FT /note="G4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 213..215
FT /note="G5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 50..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 213..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
SQ SEQUENCE 443 AA; 47449 MW; 4AF077275EED3E3F CRC64;
MKSADPGVKI PGGTDFGKNT CLISDYLHST GGNYNLSQPC VNIGMVGHVD HGKTTLVKAL
SGVWTDTHSE EVKRGISIRL GYADSPFMKC PKCPAPQCYT VEKTCPNCGE KTEEHRIVSF
VDAPGHETLM ATMLSGAAIM DGAVLVIAAN EECPQPQTKE HLMALDIIGI KNIVIVQNKI
DLVSREKLVE NYHQIKEFVK GTVAENAPII PISAQQNINI DVLIDALETQ IPTPVHKVDK
PASMLIARSF DINKPGASID EIRGGVIGGT LTEGVLHPGD ELEIRPGIKV TTEGSTKWIP
IVTTISSIYA GPTKVEEATP GGLLAVGTYL DPTLTKGDSL TGQIAGVPGT LPETRHQFVM
ELHLLDRVVG VTREEKINEI KTSEPLMLNI GTATTVGIVT SARKNEAQVA LKRPISAAVG
AMVAISRRID SRWRLIGVGV IKS
