IF2_DESOH
ID IF2_DESOH Reviewed; 884 AA.
AC A8ZZ65;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dole_3035;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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; CP000859; ABW68838.1; -; Genomic_DNA.
DR RefSeq; WP_012176449.1; NC_009943.1.
DR AlphaFoldDB; A8ZZ65; -.
DR SMR; A8ZZ65; -.
DR STRING; 96561.Dole_3035; -.
DR EnsemblBacteria; ABW68838; ABW68838; Dole_3035.
DR KEGG; dol:Dole_3035; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008561; 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..884
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093781"
FT DOMAIN 384..553
FT /note="tr-type G"
FT REGION 58..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..400
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 418..422
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 439..442
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 529..531
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 393..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 439..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 884 AA; 95549 MW; 419E0836ECCC3983 CRC64;
MAKIRIFELA RSLNMTNPDL LDRLKEMGIE AKSHLSSLED DIVEKVRQGV FRTEVEKPEK
VEQKRVRSNV IRKRRQPVKS EAEPEAEAPA AQAPEAEEVT APTAEEAVPE EAADADVSAK
AETPTAPETP EEAEISVSEE APVEEAADQV PPTDEAVDPA EAAPAEEESS PSRKKAKAKK
HQAAKIIKFP DAPQRLSNKG VLEVVDDTAP ADSPAAPAAA TPAGEKDKKP SRKDRKKRGK
TESVETEEAV PVKKKGVFKR KEIVEGVALY DRTRGRMRKK GKGGAKVPGG AKTQITTPKA
IKRKVRINES ISVAELAKRM GVKASEVIAR LMGMGVMATL NQQVDFDSAA LVAAEFEYEV
EKASATEEEL LELNVEEDQG NLKKRAPVVT IMGHVDHGKT SLLDVIRQSR ITEGEAGGIT
QHIGAYKVNT ANGEVVFLDT PGHEAFTAMR ARGARATDIV ILVVAADDGI MPQTIEAINH
SRAAGVPIVV AVNKIDKEGA DPDRVKREAS DHGLVPEDWG GDTMFVNVSA KQKLGISDLL
DMVLLQAEML ELKANPDKKA RGVVIEAKLD PGRGPVATVL IHEGTLSVGE TVVCGIHYGK
IRAMFDDKGA PLDQAGPATP VELIGLGGVA TSGDDLFAVG DEKSAKTVSE NRQQKQRTED
LARKDSISLE NFFEKMQEKE EKVLNIIIKA DVNGSCEAIA DSLQKFSSGE VKIHVVHSAP
GTIIESDVTL ASASNAIVLG FNVRPSPKVR ALAAEENVDI RSYDIIYDLI DDIKKALTGM
MSSTFEEEVL GRAEVRELFV IPKKGTIAGS YVLDGKIERG RPARLLRDGV IAYNGVIGSL
RRHKDDAKEV ASGYECGIGI ENYNDIKPGD VIECYFLREI KPEL
