IF2_TRIL1
ID IF2_TRIL1 Reviewed; 949 AA.
AC B3EAE7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Glov_1669;
OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS lovleyi).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Trichlorobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-2008) 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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001089; ACD95385.1; -; Genomic_DNA.
DR RefSeq; WP_012469727.1; NC_010814.1.
DR AlphaFoldDB; B3EAE7; -.
DR SMR; B3EAE7; -.
DR STRING; 398767.Glov_1669; -.
DR EnsemblBacteria; ACD95385; ACD95385; Glov_1669.
DR KEGG; glo:Glov_1669; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 79180at2; -.
DR Proteomes; UP000002420; Chromosome.
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:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..949
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093789"
FT DOMAIN 449..618
FT /note="tr-type G"
FT REGION 46..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..465
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 483..487
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 504..507
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 558..561
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 594..596
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 305..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 504..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 558..561
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 949 AA; 101298 MW; 411889980431F450 CRC64;
MSKTRVSNLA EKLGIDTKEV LARLKALGYD AKAGSSTVDD EAVAKLTASR PAESGPEEVR
VTTNIVRRRS RPSAAAEPEA EAPAVVEPAA PAAPAVAVEK AAPVIPERVS VVKKAVEAIV
APAVTEAAPV PAAVTAHVDA GTAAEPAVAQ EASPAVTAAK PVPATPAAPP QPERASATQA
RILGMIEIPI TPEARPYRRE PGRGPGPGGD RGPRPTGGQD NRGPRPAGTQ DNRGPRPTGG
QDSRGPRPAG AQDSRGPRPA GPPRDAAAPR PAGARPVQLT QVDLPPQGEE RRKTLGPNRK
PGGPAKDTAA DKAKKGAAAK GKGREQLSKQ ALLSREERQF DPFHKSRKKG KEREEPGKTE
LTTPKAIKRI IKISETITIG ELAKRMGIKA TDLIKAMMKM GSMVTINHVL DHDAAVLLAS
DYGYEVENVA VDLDEILEFT PDAPELLQER PPVVTIMGHV DHGKTSLLDA IREANVIAGE
AGGITQHIGA YDVELHGRKI TFLDTPGHEA FTAMRARGAK VTDIVILVVA ADDGVMPQTK
EAINHSKAAG VPIIVAINKI DKPDARPEKV KQELTEHGIV SSEWGGDVTM VEVSAKKRLN
LEELLEMILL QADLMDLKAN PDKAAKGTIV EGKLDKGRGP VATVLVQEGT LRTGDYCVVG
VHSGRVRAMQ NDRGERVLAA GPAMPVEVVG LPGVPDAGDI FVAMTDEKQA KEIATLRQIK
QRELELAKHA KMSLEQLYEK IQKGEVKDLN VIVKADVQGS VEAVAESLRK LSTEAVRLNV
IHTAVGAITE TDVNLATASN AIIIGFSIRP EVKAQAMAEK EGVDIRLYNV IYDAVDDVRK
AMEGLLEPVF KEKYLGRAEI REIFSVPKVG NVAGCYIQDG KILRNAQVRL LRDNVVVYQG
KLGTLRRFKD DVKEVATGYE CGMGLENYND IKVGDIIEAF EMEKVAAKL
