IF2_RHIE6
ID IF2_RHIE6 Reviewed; 917 AA.
AC B3PXE3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=RHECIAT_CH0000153;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-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}.
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DR EMBL; CP001074; ACE89149.1; -; Genomic_DNA.
DR RefSeq; WP_012482212.1; NC_010994.1.
DR AlphaFoldDB; B3PXE3; -.
DR SMR; B3PXE3; -.
DR EnsemblBacteria; ACE89149; ACE89149; RHECIAT_CH0000153.
DR KEGG; rec:RHECIAT_CH0000153; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000008817; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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.
FT CHAIN 1..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117336"
FT DOMAIN 415..582
FT /note="tr-type G"
FT REGION 1..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..431
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 449..453
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 560..562
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 917 AA; 98950 MW; D9AC2C191C377394 CRC64;
MTDSNDDKTL SVTGKKTLTL KPSGMSQGTV RQDMGRGRTK AVVVETRKRR PMRPEDEKPI
TPAAPAAPVR AAEPAPAPVQ ARPPQPTPAP RVHQPGSSQA NQRPQQSYQP QRSNDRPRPV
VLNHLSPEEM DARRRALAES QARDAQDAIR RAEEEKRRAA EEAIRKAAEA EEAARRAAEE
AARQAEAPAA AEPAVAAAPA PVVTEARPTA PRPASPAPAA RRPDGAGAPA AARPAPGAGA
PAGARGRRDD EGDDDRGAAR GGPARGRVVR PEPAKPVTTR PKTDDERRRG KLTITTADVD
GEDTGRSRSL SAMRRRQEKF RRSQMQETRE KISREVVLPE TITIQELSQR MSERAVDVIK
FLMKEGQMMK PGDVIDADLA ELIAGEFGHT VKRVSESDVE LGIFNIADVE GDRVSRPPVV
TIMGHVDHGK TSLLDAIRHA NVVAGEAGGI TQHIGAYQVE QNGQKITFID TPGHAAFTAM
RARGAQATDI AILVVAADDS VMPQTIESIN HAKAAGVPII VAINKIDKHE ADPQKVRNQL
LQHEVFVESM GGETLDVEVS AKTGKNLDKL LEAVLLQAEI LDLKANPNRT AEGTVIEAQL
DRGRGSVATV LVQNGTLKPG QIIVAGDVWG RVRALVTDKG DHVKEAGPAT PVEVLGLSGT
PQAGDKFAVV ESESRAREIS EYRQRLARDK AAARQSGQRG SLEQMMTQMQ STGIKEFPLV
IKGDVQGSIE AIAGALEKLG TDEVRARIVH SGAGGITESD ISLAEASNAA IIGFNVRANA
QARQFAERQG IEIRYYNIIY DLVDDVKAAM SGLLSPERRE TFIGNAEILE VFNITKVGKV
AGCRVVEGKV ERGAGVRLIR NDVVVHEGKL KTLKRFKDEV SEVPMGQECG MAFENYEDMR
VGDVIECFRV EHITRTL
