ID   IF2P_IGNH4              Reviewed;         609 AA.
AC   A8A8D3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Igni_0001;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
CC   -!- FUNCTION: Function in general translation initiation by promoting the
CC       binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC       along with eIF-2. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; CP000816; ABU81185.1; -; Genomic_DNA.
DR   RefSeq; WP_011998037.1; NC_009776.1.
DR   AlphaFoldDB; A8A8D3; -.
DR   SMR; A8A8D3; -.
DR   STRING; 453591.Igni_0001; -.
DR   EnsemblBacteria; ABU81185; ABU81185; Igni_0001.
DR   GeneID; 5562612; -.
DR   KEGG; iho:Igni_0001; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   PhylomeDB; A8A8D3; -.
DR   Proteomes; UP000000262; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_A; IF_2_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR004544; TF_aIF-2_arc.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00491; aIF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..609
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000335524"
FT   DOMAIN          12..230
FT                   /note="tr-type G"
FT   REGION          21..28
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          46..50
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          86..89
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          140..143
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          208..210
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         21..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   609 AA;  67806 MW;  55FA63280558D146 CRC64;
     MLNLSAEQRP RLRQPIVAVL GHVDHGKTTL LDKIRGTVVA LKEPGQITQH IGASLVPTDV
     IEKVTEPLKK IIPTVKLELP GLLFIDTPGH EIFSNLRRRG GAVADLAILV VDLNEGFQPQ
     TYEAVEILKQ RRVPFVVAAN KIDRIPGWRS YPDQPFLISY RKQSEEVRER LDNKIYEIMG
     ELAKLGFDSE RFDRITNFTR QIAIVPISAK TGEGIPELLA VLAGLAQRYM KGRLKYVEGP
     AKGVIMEVKE EPGYGSTIDT IIYDGIIRQG DTIVVGGIEG PIVTKVRALL VPAPLTEMRA
     TKRFEPVEEV SAAAGVKIVA PGLEKAVAGA PVYVVDSPEK LEELKEQVKR EVEEVMIETD
     KEGVIVKADT LGTLEALVQF LKNRGIPVRM ARVGPVTKRD IVEAMTVKSK NKEYGVILAF
     NVKVLPEAKE LAEKEGIKIF QHNVIYRLIE EFEEWLKALR EEEKRKVLET LVRPGKIRIL
     PGFVFRRSDP AIVGVEVLGG VIKPKYPLMK EDGSRVGSIL QIQDKGQSVP EARAGQQVAI
     SIKGRVMVGR HIHEGDVLYT DVPAEHAKLW LTKFKNELSD DEKFVLQEII KIKRKQNPLY
     GVVLPSPSS