ID A0A1F5ZU46_9BACT Unreviewed; 498 AA.
AC A0A1F5ZU46;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN ORFNames=A3D78_03520 {ECO:0000313|EMBL:OGG15999.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_39_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798383 {ECO:0000313|EMBL:OGG15999.1, ECO:0000313|Proteomes:UP000176253};
RN [1] {ECO:0000313|EMBL:OGG15999.1, ECO:0000313|Proteomes:UP000176253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {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|RuleBase:RU000644}.
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:OGG15999.1}.
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DR EMBL; MFJM01000062; OGG15999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5ZU46; -.
DR STRING; 1798383.A3D78_03520; -.
DR Proteomes; UP000176253; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
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; TIGR00487; IF-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; PF03144; GTP_EFTU_D2; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 14..191
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 498 AA; 54599 MW; 0B921977BD1A6CE8 CRC64;
MTKKTAQNQI EAPVRPPIVA VLGHVDHGKT SILDYIRKTK IADKEEGGIT QHIGSYQIDV
PETVKKKYPN APDKISFIDT PGHEAFGAMR SRGVEACDIA ILVVAANDGV KPQTIESINY
IHDAKIISLV CINKIDLPNI NLESVKKQLN KAGIKLEEYG GDIPLVKVSA KTGEGIDKLI
ETIIFLADFY QIKSDKISPF QGVVIESTLS KFKGITATIF VKQGNLKLAD EVISENQIFK
IRALYDWQGK SLSGVNPGDP VEILGWKNIP AVGSLIYKKD ESEIINKPHQ DIEPIKQKPL
MVENQPDQSD IKKIKIIIKA DTVGTLEAVV NGLNIDVDII QKGVGLISES DILLAKTAKA
IVIGFNQKPL PQVSKLAQSE KVLIKIYNII YQLFDEIRDV SEAINKGDLV TILGEAKVLN
LYNFKNETIL GAKVVSGRIA RGDQVKIKRN NEEIGKNRIK SLKHFKDEIT KAEAGAEIGI
GLAQKTEILT GDSIISIG
//
