IF2_AQUAE
ID IF2_AQUAE Reviewed; 805 AA.
AC O67825;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=aq_2032;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07794.1; -; Genomic_DNA.
DR PIR; E70474; E70474.
DR RefSeq; NP_214394.1; NC_000918.1.
DR RefSeq; WP_010881330.1; NC_000918.1.
DR AlphaFoldDB; O67825; -.
DR SMR; O67825; -.
DR STRING; 224324.aq_2032; -.
DR EnsemblBacteria; AAC07794; AAC07794; aq_2032.
DR KEGG; aae:aq_2032; -.
DR PATRIC; fig|224324.8.peg.1571; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_0; -.
DR InParanoid; O67825; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..805
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137166"
FT DOMAIN 306..474
FT /note="tr-type G"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..322
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 340..344
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 362..365
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 416..419
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 452..454
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 315..322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 362..366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 416..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 805 AA; 91600 MW; 8A1BF300C69CA51E CRC64;
MSLTKTKRVS DVAKELGVKS KEIIEFLNEY YPRPDGKPWK ASHGLDEQAL EMIYDAFGIK
EEEEKEEVVT EQAQAPAEVE EKKEEEKKEE VIVEEVVEEK KPEVIVEEIE EKKEEEEKKE
EEKPKKSVEE LIKEILEKKE KEKEKKKVEK ERKEEKVRVV EVKKEERKEE KKEEKKEEEK
PKIKMSKKER EIMRKLEHAV EKEKKKQEKR EKEKKKKEEE VKIIYIPEVI TVRELAELLD
VPANKVIAEL MKRGVLATIN QPVPPEVAVE VAESFGYLAE VKKEEEELEE EALLKEEEER
EEELQPRPPI VVVMGHVDHG KTTLLDRIRK TNVAEREKGG ITQHIGASQV ELPDGRKITF
LDTPGHEAFT TLRARGAKVT DISVLVVAAD DGVMPQTIEA INHAKAFNVP IIVAVNKIDK
PNADPMKVRR ELSEHGLIPE EWGGDTIFVD ISAKTGQNVD QLLEMILLLA DILELKANPN
KKARGTIIES KLDRKRGPVA TVIVEDGTLR VGDHFVAGTT YGRVRAMFDD KGRQVKEAPP
STPVEVLGFE ELPEAGDELI VVDDERTARE IAEKRKEKKE REEKLQTIRL EDIYKKIQTG
ETKELRIVLK TDTMGSLEAL KKSLEELSNE KVQVKIIHGA VGGITENDIM LAKASGAIVI
GFNTRPDPKA RELMEKEKVD VRLYGVIYEA IEDVKKALVG LLEPIKKEEV IGMAEVRATF
KIKKVGTVAG CYVLNGKLVR GAKARLIREG VVIYDGEIES LKRFKEDVQE VTAGYECGVK
LKDYNDVKVG DQIECYEIRY EKPTL
