ID   IF2P_THEPD              Reviewed;         601 AA.
AC   A1RXH6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Tpen_0499;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(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; CP000505; ABL77906.1; -; Genomic_DNA.
DR   RefSeq; WP_011752171.1; NC_008698.1.
DR   AlphaFoldDB; A1RXH6; -.
DR   SMR; A1RXH6; -.
DR   STRING; 368408.Tpen_0499; -.
DR   PRIDE; A1RXH6; -.
DR   EnsemblBacteria; ABL77906; ABL77906; Tpen_0499.
DR   GeneID; 4601333; -.
DR   KEGG; tpe:Tpen_0499; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000000641; 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..601
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000335536"
FT   DOMAIN          10..227
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          44..48
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          83..86
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          137..140
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          205..207
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         83..87
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         137..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   601 AA;  66557 MW;  997A90B8660B15B3 CRC64;
     MSNDQGSQFL RAPIVVVLGH VDAGKTTLLD KIRGTAVAKR EPGTMTQHIG ASFLPWKALE
     AVCGSLVSQI RAEVVIPGFL VIDTPGHEAF SNLRRRGGSI ADIAILVVDV LRGLEQQTFE
     SIDILRERKV PFIVAVNKID KIPGWKSFPN TPFVESVKRQ SEAAQLKLEE LLSYIIQQFA
     SLGFRSDRYD RIRDFTRVLA LVPVSAVTGE GIPDLLLVLA GLAQRYLKGR LLASIAPGKG
     VILELKEEAG LGMTATLILY DGVIRRGDIV VTGGIEGAFS TRVRALLMPK PLDEMRSPED
     RFLEVERIVA AAGVKLVAEG LEKAVPGAPL FVAVSEEEVG RLKQLVEEEI SGVKFERDVV
     GVVVKADTLG TLEALVGYLK KQGIPIRVAD IGPVVKRDVV QASMVKEKDP LYAAILAFNV
     KILPEAQDEA ARHGIPVFQE RIMYKLVENY QKWLQETRDA EVRKAFEKIT PPAVVQILPG
     YVFRRRDPII VGVRVVCGRI RSGVPLITKD GREIGEIMQI KEHDKVLDVV SEGAEVAISI
     RSKAIVGRQV KEGDYLYSNL SIEEINRLLE KYEKYLAENE KSYLRKLMRF KMGLSKEIEY
     P