ID IF2_MYXXD Reviewed; 1072 AA.
AC Q1DAM6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MXAN_2068;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF88832.1; -; Genomic_DNA.
DR RefSeq; WP_011552152.1; NC_008095.1.
DR AlphaFoldDB; Q1DAM6; -.
DR SMR; Q1DAM6; -.
DR STRING; 246197.MXAN_2068; -.
DR EnsemblBacteria; ABF88832; ABF88832; MXAN_2068.
DR GeneID; 41359476; -.
DR KEGG; mxa:MXAN_2068; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002402; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1072
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335491"
FT DOMAIN 570..737
FT /note="tr-type G"
FT REGION 55..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..586
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 604..608
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 625..628
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 679..682
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 715..717
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 120..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 579..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 625..629
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 679..682
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1072 AA; 111900 MW; FC8036DAD2C79839 CRC64;
MSKKRVHEIA KELKSHGIEL DNKEVVTELS SLGYDVKSHS SSLDDDQATA AVQKILDKRK
PKQATPPVTA KGFVVRRKVG PPAGATADSG AEASQAAEPA YEPPSAPEPA TFAAEEPVQA
PPPVEAPRAP VEAPSAPEPQ RVEAPVAAAT EPTAPAAVTS TPPAQVAEAT KAPAAAEVAS
PPPAAEAPQA PVEAPRAAVP APAAAQPRPS VQESTTLPQP PPRSPVPPAV RTPSSTSSSA
TVVSRGPAPG YQQRGGPGGG RPGGPGGPGG RPGGPGGPGG RPGGPGGPGG RPGGPGGPGG
RPGGPGGRPS YQGPGSYQGA GRPGQGPVRP TSAPGTGVQA SASASPIPQG PTIMVGGVPH
AQVSPTGTAR PTATQAVVIS RPLIQVRRVT PTAGQAKQYP MAPGRTGIPE RREYKVVPDH
LGRGRELVDV SKNKERGQRK RTSGDTQSVS KQELTDMVWG RVTIPIRGKK RKPTKKGAKT
QITQMAEEKK VIKLQEGISV SDLGQRMGVR SAELIKKLMG LGKMATANQL VDADTAEMIA
GDYGWKIDRV GFEVEDYLPE VETRPEDERP RPPVVAIMGH VDHGKTSLLD AIRKASVAQG
EAGGITQHIG AYSITTARGD VTFLDTPGHE AFTSMRARGA DVTDIVVLVV ASDDGVMPQT
VEAIKHAKAA EVPIVVAINK MDLPTANLDR VKKDLATHEL VPEEWGGDTI MVPVSAKTKE
NLELLLENLA LQAEVLELAS NPLRPSVGAI IEAKLDRGRG PVATVLVQEG TLKLGDAVVT
GSHYGRVRAM TNSRGEQVKE VKPGYCAEVV GLSGVPGAGD AINVVADEKA AKQIAEHRNM
KERQTELSKV SRESLEQLFA KTKAGGGPKE LRVVIKADVQ GSAEAVKQAV QKLSTHKVKV
EVVHSGVGAI TEGDVMRAAA SKGVVLGFNV NPESGAEAAA KAQEVVLKSY SIIYELIDGV
RTEMEGLLEP IRTERKLGRA EVRNTFNVPR LGTIAGAAVL DGVMKRGAIV RLMRENKQLF
SGKMASLRRF KDDVKEVAQG FECGIGIESF NDLKPGDIIE AYEIVETRQS LT
//
