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Database: UniProt
Entry: E0SQA7_IGNAA
LinkDB: E0SQA7_IGNAA
Original site: E0SQA7_IGNAA 
ID   E0SQA7_IGNAA            Unreviewed;       608 AA.
AC   E0SQA7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Igag_0208 {ECO:0000313|EMBL:ADM27057.1};
OS   Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignisphaera.
OX   NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27057.1, ECO:0000313|Proteomes:UP000001304};
RN   [1] {ECO:0000313|EMBL:ADM27057.1, ECO:0000313|Proteomes:UP000001304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC   {ECO:0000313|Proteomes:UP000001304};
RX   PubMed=21304693; DOI=10.4056/sigs.1072907;
RA   Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL   Stand. Genomic Sci. 3:66-75(2010).
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:0000256|ARBA:ARBA00024852, ECO:0000256|HAMAP-
CC       Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
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DR   EMBL; CP002098; ADM27057.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0SQA7; -.
DR   STRING; 583356.Igag_0208; -.
DR   KEGG; iag:Igag_0208; -.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001304; 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   CDD; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_A; IF_2_A; 1.
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   NCBIfam; TIGR00491; aIF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000001304}.
FT   DOMAIN          13..230
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   608 AA;  67593 MW;  616B0556C996622D CRC64;
     MVLEMSKHVD RKLRQPIVVV LGHVDHGKTT LLDKIRGTAV VKKEAGEMTQ HVGASMVPSS
     VIEKVAMPLK KIIPFKLEIP GLLFIDTPGH ELFSNLRKRG GSVADIAILV IDINEGVKPQ
     TIESIDVLKA RNVPFVIAAN KIDKIQGWKP YPDEPIISSL KKQSRAVVNK LETLLYNLIA
     QLSSYGVNAE YFERVRDFMK VVPIVPVSAK TGEGIPELLA ILAGITQRFL AERLRFAEGP
     AKGVVLEVKE QQGYGAALDV IIYDGVLRER DNIVVAGFNG PIVTKVRAIL MPKPLTDIRI
     ARTELQIVEE VAAAAGVRVI APGIEEAIAG SPFFVVPNEN EIEKYKRLVM EEVETIRFRR
     DIDGVIVKAD TLGTLEAIIL ALNRKSIPIR IADVGPLTKR DVIEASIVAK NNKYYGVILL
     FNVKALPDAE ELARKENIKI FSNNIIYKLI DDYINWIESE KMMELRREFE SIVPPAKIKI
     LPGYIFRRSD PAIVGVSILG GIIRPGMPLM RSDGRSIGEI QQIQYMGQTL REAKTGQEVA
     ISIKGNVIVG RHIKEDDILY SDIPLSHVKI LVSKFKNILD ETSLTVLKEI IKIKSLKEPE
     YAAFLMQL
//
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