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Database: UniProt
Entry: A0A166EYW4_9EURY
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ID   A0A166EYW4_9EURY        Unreviewed;       595 AA.
AC   A0A166EYW4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ECO:0000313|EMBL:KZX17153.1};
GN   ORFNames=MBCUT_03850 {ECO:0000313|EMBL:KZX17153.1};
OS   Methanobrevibacter cuticularis.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX17153.1, ECO:0000313|Proteomes:UP000077275};
RN   [1] {ECO:0000313|EMBL:KZX17153.1, ECO:0000313|Proteomes:UP000077275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX17153.1,
RC   ECO:0000313|Proteomes:UP000077275};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZX17153.1}.
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DR   EMBL; LWMW01000064; KZX17153.1; -; Genomic_DNA.
DR   RefSeq; WP_067258205.1; NZ_LWMW01000064.1.
DR   AlphaFoldDB; A0A166EYW4; -.
DR   STRING; 47311.MBCUT_03850; -.
DR   PATRIC; fig|47311.3.peg.426; -.
DR   OrthoDB; 30957at2157; -.
DR   Proteomes; UP000077275; Unassembled WGS sequence.
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:UP000077275}.
FT   DOMAIN          3..220
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   595 AA;  66613 MW;  EE25D9EA5D50298B CRC64;
     MKIRSPIVSV LGHVDHGKTT LLDFIRGSTI ASKEAGGITQ HIGATEIPID TVENICGTFI
     EKLTIKDIIP GLFFIDTPGH EAFTSLRKRG GALADLAILV VDINEGFKPQ TYEALNILKM
     YKTPFIVAAN KMDKIFGWEI HEFDSFSKSF STQAQSVQQE LDKRIYEIVG ILHKEGFQSE
     RFDRVSDFSS QITIIPISAK TGEGIIELLA MLLGLAQEYL TEQLKIEENS PAKGTVLEIK
     EETGLGVTID TIIYDGIVKK NDEIALMETE DVLTTKIRSI LRPLPLEEMR DSKKKFKKVD
     EVVAAAGIKI VAPKLENIVS GSPLRVTRDG DHVKEDILKE LEDITIHTND NGVMAKADTL
     GSLEALVNLL QDMDIPIRIA EIGDVSRRDV INASIVKQED PNHGVIIAFN VKVHPKAEEE
     LNNSDIKLFS GNVIYKITED YDAWIKEREE EQKKKWMDAI IKPAKIRVIP KLVFRQSKPA
     IVGIEVISGS IKQNYSLMDL NGNFVGTIEG MQDKGDNLPS ISKGQKIAMA IKDAIVGKDF
     EEGDELYVDI PEKHYKILER EFKNKLTEDE FQTLNEIIEI KRKIDPNWGT FGLFE
//
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