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Database: UniProt
Entry: A0A0R3MHC0_9BRAD
LinkDB: A0A0R3MHC0_9BRAD
Original site: A0A0R3MHC0_9BRAD 
ID   A0A0R3MHC0_9BRAD        Unreviewed;       676 AA.
AC   A0A0R3MHC0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE   Flags: Fragment;
GN   ORFNames=CQ14_12035 {ECO:0000313|EMBL:KRR17125.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR17125.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR17125.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR17125.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000645}.
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:KRR17125.1}.
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DR   EMBL; LLYB01000123; KRR17125.1; -; Genomic_DNA.
DR   RefSeq; WP_057862116.1; NZ_LLYB01000123.1.
DR   AlphaFoldDB; A0A0R3MHC0; -.
DR   STRING; 722472.SAMN05444321_2189; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000051660; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
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   Pfam; PF04760; IF2_N; 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.
DR   PROSITE; PS01176; IF2; 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          172..343
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRR17125.1"
SQ   SEQUENCE   676 AA;  72859 MW;  789421D657CA4B8E CRC64;
     ATPAARTPVA ADGSDEDEGP RQVRRGPGGA MRPVAAPKTT HKPGPQKERG RLTVVTALND
     DVRERSIASF RRRTQRLKGH ASNEPKEKLI REVTIPEAIT IQELANRMSE RAVDVIRLLM
     KQGAMHKITD VIDADTAQLI AEELGHTVKR VAASDVEEGL FDIVDDTTDT EPRSPVVTVM
     GHVDHGKTSL LDALRHANVV SGEAGGITQH IGAYQVTSPE SGKKITFIDT PGHAAFTAMR
     ARGAKVTDIV ILVVAADDGV MPQTVEAINH AKAAKVPMIV AINKIDKPDA KPERVRTELL
     QHEVQVESFG GEVVDVEVSA KNKTNLDKLL EMIALQAELL DLKTNSERPA EGTVIEAKLD
     RGRGPVATVL VQRGTLRVGD IIVAGAEMGR VRALISDQGE NIDEAGPSVP VEVLGFNGPP
     EAGDRLAVVE NEARARQVTS YRAHQKRENA AASISGMRGS LEQMMSQLKT AGRKEFPLIV
     KADVQGSLEA ILGSLEKLGT EEVAARILHA GVGGISESDV TLAEGFNAAI IGFSVRANKE
     AAAAAKRNGI EIRYYNIIYD LVDDIKKAMS GLLAPTLRET MLGNAQILEV FNISKVGKVA
     GCRVTDGTVE RGANVRLIRD NVVVHEGKLS TLKRFKDEVK EVQSGQECGM AFENYGDMRV
     GDVIECYRVE TIQRSL
//
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