ID A0A1G2PL93_9BACT Unreviewed; 506 AA.
AC A0A1G2PL93;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN ORFNames=A2806_01890 {ECO:0000313|EMBL:OHA49067.1};
OS Candidatus Terrybacteria bacterium RIFCSPHIGHO2_01_FULL_48_17.
OC Bacteria; Candidatus Terrybacteria.
OX NCBI_TaxID=1802362 {ECO:0000313|EMBL:OHA49067.1, ECO:0000313|Proteomes:UP000177629};
RN [1] {ECO:0000313|EMBL:OHA49067.1, ECO:0000313|Proteomes:UP000177629}
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:OHA49067.1}.
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DR EMBL; MHSS01000001; OHA49067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2PL93; -.
DR STRING; 1802362.A2806_01890; -.
DR Proteomes; UP000177629; 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: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; PF03144; GTP_EFTU_D2; 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 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:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 16..185
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 506 AA; 54888 MW; 6EB61D5D82211853 CRC64;
MAATAGKKRK EIAQTTRPPV VVVLGHVDHG KTTLLDYIRK TNVVARESGG ITQHIGAYQV
EHDGKKITFL DTPGHEAFSA IRKRGAAVAD IAVLVIAAND GMKPQTREAL EAIRAAKIPY
LVAFTKIDLP QADVQRAKTQ LAEAGVLLEG WGGDVPNLEV SGKTGTGIAE LLELLLLVAE
VAELKDTVDE PFWGVVIEAH RDSRQGPTAT VLVKSGILKV GDVISAGTVV GKVKAMENFL
KNSVTEASPA IPVVLLGFND VPDVGDRVLT FDSEKEAVAA AEKEASRRTF EKILGGQESE
ATLAVIIRAD VVGSLEAIVG ELEKLANPYV ALHIVSADTG EVSENDIDQA EATRAQIFAF
RTKIRGQIAL RAERTGVKIH MLAVIYDLTD IVKRALQDTV PPEIIREDLG QVRVLALFRD
EGTQQIVGGR VASGIIRKGE FAEVMRDDRL LGRGRLKEVQ QNKIPVDEVK QGNECGMLIE
IKGSIDIVEG DMLRVFHEER RERKLF
//
