ID A0A1G2FKD1_9BACT Unreviewed; 502 AA.
AC A0A1G2FKD1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN ORFNames=A3E90_00925 {ECO:0000313|EMBL:OGZ38038.1};
OS Candidatus Portnoybacteria bacterium RIFCSPHIGHO2_12_FULL_40_11.
OC Bacteria; Candidatus Portnoybacteria.
OX NCBI_TaxID=1801998 {ECO:0000313|EMBL:OGZ38038.1, ECO:0000313|Proteomes:UP000177247};
RN [1] {ECO:0000313|EMBL:OGZ38038.1, ECO:0000313|Proteomes:UP000177247}
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:OGZ38038.1}.
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DR EMBL; MHNC01000037; OGZ38038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2FKD1; -.
DR Proteomes; UP000177247; 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 CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 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; IPR044145; IF2_II.
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 14..183
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 502 AA; 55631 MW; 6DE70FD649BC9427 CRC64;
MKKNPEKKQD NMEIRPPVVV ILGHVDHGKT SILDYIRKAH IAEKEAGGIT QHIGAYQIEH
QGKIITFIDT PGHEAFSAMR SRGAKVADIA VLVVAAEEGI KPQTKEAINH IKKSGLPLIV
ALNKIDKKEA QPEKVKRELK DAEIVVESLG GQVPSINVSA KTGQSIDELL EMINLVAEME
ELKSNPDKPA SGVIIESRLD SLRGPTATLL VKDGTLKNID IIGTGSAFGR IKTMEDFRIQ
VIKETGPSAP VIVTGFNQVP QIGEKFDVFE NSEAAQKKVE QKTAKRKEEK EVFFIPVDKK
VLNILLKADV RGSLEAIRES LQAIPQEEIV LRVLKSEVGE INENDIKLAQ SGQAKIIGFR
VKTSSKIQQI AEQQKVKILT FEIIYELIQK TRDLLAGLLA PEIIKNVLGQ LKVLAIFPAK
KGRQIIGGKV TNGQIKRGAF IEIIRENKRI GKGKLIQLQH NKKDVEEVAK NQECGIMFEG
GATIEERDII EVYEEEKKKR EL
//
