IF2_FERNB
ID IF2_FERNB Reviewed; 685 AA.
AC A7HN01;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Fnod_1441;
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-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; CP000771; ABS61284.1; -; Genomic_DNA.
DR RefSeq; WP_011994589.1; NC_009718.1.
DR AlphaFoldDB; A7HN01; -.
DR SMR; A7HN01; -.
DR STRING; 381764.Fnod_1441; -.
DR EnsemblBacteria; ABS61284; ABS61284; Fnod_1441.
DR KEGG; fno:Fnod_1441; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002415; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..685
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071289"
FT DOMAIN 175..352
FT /note="tr-type G"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..191
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 209..213
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 230..233
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 284..287
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 321..323
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 184..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 230..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 284..287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 685 AA; 77128 MW; EE8EC897C1601254 CRC64;
MARLRVYELA KQLDMDTKEL LHELEELGIE VKSHMSFIDE ETVNILLDIY KQTLDEEEDI
SLAKTREPSK EKTEAKKPPV HITEADLKLD KFAEKIKIPQ NRIIQDFFMK GEILKPGQTI
SISLAKKIAK MYDVRLTFEE DETAVKEQPK LENPLDELKR QFEEIYQNNK DKLVNRPPVV
TVMGHVDHGK TTLLDYIRKT RVAEKEEGGI TQSVGAYQVI VNGKKITFID TPGHEVFTEM
RARGAQATDI VVLVVAADDG VMPQTIEAYN HAKSANVPII VAINKIDKAN ANVDMTKQEL
VTKLNLIPED WGGDTIVVPI SARNGINVDT LLEMILLVAE MQDIRCIPDS PVRAVTIETR
LDKGYGPVAN AIVKDGVLKV GDYVVAGKVF GKVKALIDDK GKRLKEAEPS TPVMIVGFEE
LPDPHSIIYV VDSKEKALEI VEKVREIEAR ELRKKRQVKL EEILKRMQET EKRELKLILK
ADTVGSLQAL QNAIAKLRTN EIDIDIVHSA VGAINSSDIM LASASEAIIL GFRVKADNQA
SKLAESEGVQ IKTYTIIYKL LEDLKAALEG MLEPEEVEEK TGYGEIKKAF KIHKYGNIAG
VQMYDGYVDK SGFVRIYRNG ALVFEGKIES LKHYQQDVNK VSAPQECGIK FQNFDDIKEG
DELEFYIIKK IPRKLTIIEE EKQQI