IF2_RUBXD
ID IF2_RUBXD Reviewed; 689 AA.
AC Q1AW55;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rxyl_1411;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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; CP000386; ABG04373.1; -; Genomic_DNA.
DR RefSeq; WP_011564390.1; NC_008148.1.
DR AlphaFoldDB; Q1AW55; -.
DR SMR; Q1AW55; -.
DR STRING; 266117.Rxyl_1411; -.
DR EnsemblBacteria; ABG04373; ABG04373; Rxyl_1411.
DR KEGG; rxy:Rxyl_1411; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_11; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR PhylomeDB; Q1AW55; -.
DR Proteomes; UP000006637; 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; 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 PANTHER; PTHR43381; PTHR43381; 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; 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..689
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335506"
FT DOMAIN 192..361
FT /note="tr-type G"
FT REGION 41..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..208
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 226..230
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 247..250
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 301..304
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 337..339
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 247..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 301..304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 689 AA; 74404 MW; A40256C31F6923F4 CRC64;
MSKRVYEIAK ELDLDTKEVI GRLNAAGIEV KNHFATVEDP DYERVFGGGN GRSEAGEERG
RKGRQKKRRR VVIDASATNR GPRAAAPSRP SRGRGAAREE APAAEEREAP EVVRVEPGAT
VRDLGEALGV PPTRIIQILM GLGEMKTVTQ TLSTEEIELV AEELGRRVEV GALEEPAPEE
IGPEDSPEDL VEKPPVITVM GHVDHGKTSL LDRIRRTNVV SGEAGGITQH IGAYQVEHEG
RRITFIDTPG HEAFTEMRAR GARVTDIVVL VVAADDGVMP QTEEAIEHAR AAGVPIVVAI
NKIDVPNANP DRVMGELAER GLTPEQWGGE TVTVPVSAKT GEGIEDLLEN ILVVAELEEL
RANPKAPASG YVIESRLDPG RGPVATLLLN RGTLHRGDVV LAGTAYGRVR AMFDYTGQRI
KEAGPGTPVE ILGLSGVPEA GTRFEVAENE RAARSRAQQA EERLRRQELA ASGPRRTTLE
ELLGEGGAEE LNLVVKADVA GSVEALKEAL AKLSTDEVRV NVVRSGVGAV TDSDIMLASA
SGGIVIGFNV RPTNTAKQVA EREGVEIRTY DVIYKVIEEI EAAMKGMLAP ETAERETATA
EVRATFRVPN VGTVAGCYVT SGEIRRNNRV RVVRDGTVVY DGQIASLKRF KDDVRTVREG
FECGVGIENF NDVKEGDVLE FYEVVEIPR
