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Database: UniProt
Entry: A0A1F8DZJ3_9BACT
LinkDB: A0A1F8DZJ3_9BACT
Original site: A0A1F8DZJ3_9BACT 
ID   A0A1F8DZJ3_9BACT        Unreviewed;       492 AA.
AC   A0A1F8DZJ3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN   ORFNames=A2610_03765 {ECO:0000313|EMBL:OGM94004.1};
OS   Candidatus Wolfebacteria bacterium RIFOXYD1_FULL_48_65.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1802561 {ECO:0000313|EMBL:OGM94004.1, ECO:0000313|Proteomes:UP000179057};
RN   [1] {ECO:0000313|EMBL:OGM94004.1, ECO:0000313|Proteomes:UP000179057}
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:OGM94004.1}.
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DR   EMBL; MGIV01000018; OGM94004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8DZJ3; -.
DR   Proteomes; UP000179057; Unassembled WGS sequence.
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; 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:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000256|RuleBase:RU000644};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU000644}.
FT   DOMAIN          10..183
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   492 AA;  52804 MW;  AE1CF6CD7D446A4C CRC64;
     MPHTKNKLLP RPPIVVVMGH VDHGKTTLLD TIKKTQIAAR EAGGITQAIG AYEIVHAGKK
     MTFIDTPGHE AFTHMRTRGA HVADLAILIV AADDGVQPQT KESIETLIGS NTPFVVAINK
     IDKANADIEK TKASLMQHGV YLEGAGGNIS WQKISAKQGT GVDELLDLLL LAAELENFTY
     DPHANAEGII LESKLDKQRG IIATGIIKNG TLKTGKNIET DSACGKIKLL EDFLGKRATK
     MEPSAPVVIM GFDTLPKVGE KFVSGDIELA VFDKYAAAII VPPTMQKSLI KETGNPELRL
     ILKADVSGSL EAFAAIVKSL NQTTVNIRIM GESVGEISDS DVKAAASGDA IIIGFNAKVS
     KSAEQMAQIK KIRIITGNII YKLVETIEEE IKAIEEPAPL GIAEIMATYS QKGKKQVIGG
     KITNGIIKNN TTLAVTRAGE VLGTGKLTNL QSSKRDVTQV EFPMEFGMVF ESSVDIQIGD
     LLSHEVQKRT AQ
//
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