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
//