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IF2G_AERPE
ID   IF2G_AERPE              Reviewed;         414 AA.
AC   Q9Y9C1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 120.
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=APE_2366.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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, ECO:0000305}.
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DR   EMBL; BA000002; BAA81379.2; -; Genomic_DNA.
DR   PIR; C72465; C72465.
DR   AlphaFoldDB; Q9Y9C1; -.
DR   SMR; Q9Y9C1; -.
DR   STRING; 272557.APE_2366.1; -.
DR   EnsemblBacteria; BAA81379; BAA81379; APE_2366.1.
DR   KEGG; ape:APE_2366.1; -.
DR   PATRIC; fig|272557.25.peg.1581; -.
DR   eggNOG; arCOG01563; Archaea.
DR   Proteomes; UP000002518; 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   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Initiation factor; Magnesium; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..414
FT                   /note="Translation initiation factor 2 subunit gamma"
FT                   /id="PRO_0000137449"
FT   DOMAIN          8..206
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          17..24
FT                   /note="G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          45..49
FT                   /note="G2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          93..96
FT                   /note="G3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          149..152
FT                   /note="G4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          184..186
FT                   /note="G5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         20..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         20
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         149..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         184..186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
SQ   SEQUENCE   414 AA;  45076 MW;  7637830ACD8D5B12 CRC64;
     MSGGDKRQPE VNIGVVGHVD HGKTTLVQAL TGVWTMRHSE EIRRGMTIKL GYADGEVWEC
     EGCGFPERFS PEPVCECDPQ ASASLRRRVS YVDAPGHEIL MATMLSGAAL MDGALLVVAA
     NEPCPQPQTK EHLVALEIIG IKNIVIVQNK VDVVSRERAK ESYQEILNFI KGTIAEGSPI
     IPVSALKRAN IDAVLAAIEK FIPTPPRDLD KPPVMYISRS FDVNRPGTPP ERLVGGVVGG
     SIIQGVFRVG DEIEISPGVA VRKPGGRVEY VRLHTTITSL RFGSIEVEEA RPGGLVAIGT
     QLDPSVTKAD NLVGNVVGKP GELPEPLTTL RIEHHLLEKV VGMKEEARVE PIRRGEMLML
     SVGTAITLGV VTRAGKDEIE VQLRRPVVTW PKARVALSRR IMGRWRLIGW GLIK
 
 
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