IF2_AROAE
ID IF2_AROAE Reviewed; 945 AA.
AC Q5NZS1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AZOSEA33180;
GN ORFNames=ebA5841;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI09443.1; -; Genomic_DNA.
DR RefSeq; WP_011239106.1; NC_006513.1.
DR AlphaFoldDB; Q5NZS1; -.
DR SMR; Q5NZS1; -.
DR STRING; 76114.ebA5841; -.
DR PRIDE; Q5NZS1; -.
DR EnsemblBacteria; CAI09443; CAI09443; ebA5841.
DR KEGG; eba:ebA5841; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006552; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
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..945
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228162"
FT DOMAIN 445..614
FT /note="tr-type G"
FT REGION 52..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..461
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 479..483
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 590..592
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 554..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 945 AA; 102381 MW; CE0909705D79DD7D CRC64;
MEQMSVTQFA GELKMPASVL LEQLQKAGVE KTGADQLLTE QDKARLLEYL RRSHGQSQPK
GKITLTRKQT SEIRATDSSG RARTVQVEVR KKRVFMKRDE VSAETGSLES AQIEEETAGL
PMGEIEPTPE PENIVEPVAE AIPEPEPVRE PEPEPEPIVE PEPEPEPEPE PEPQPEPEPR
PEPEPATVES GAPAKPEAPV RAPSRPPLRV SILSDEERAA REREARRHQE LRARQAADLK
AKQDREAAAR AAAEARRAEE EARVRAEAER RAEAAKPQPK EAAKAPAGTL HRPAKTEEKP
AGKDAKRTAR GDTAGESAKR RGLKTRGEVG ATTGSWRGAR GGGRRGAQDE HKSFQAPTEP
VVREIHVPET ISVADLAHKM SVKAAEVIKI LMKMGSMVTI NQVLDQETAM ILVEEMGHKA
FAAKLDDPDT YLESAEAHHD AAVEPRAPVV TVMGHVDHGK TSLLDYIRRA KVASGEAGGI
TQHIGAYHVE TPRGMLTFLD TPGHEAFTAM RARGAKATDI VILVVAADDG VMPQTREAIH
HAKAANVPLV VAVNKIDKPD ANPDRVKQEL VAEGVLPEEY GGDVMFINVS AKTGVGIDSL
LEAVLLQAEV LELTAPVDSP AKGLIIEARL DKGRGPVASL LVLSGTLRKG DVMLVGATFG
RIRAMLDENG KAIDHAGPSI PVEVLGLSDV PAAGDEAIAL ADEKKAREIA LFRQGKYREV
KLAKQQAAKL ESMFEQMAEG EVKTLPLIIK ADVQGSQEAL VQALNKLSTD EVRVNAIHSA
VGAISESDVN LAQASGAVII GFNTRADAGA RKLAETFGVD IRYYNIIYDA VDEVKAALSG
MLAPERRENV IGLVEVRQVF KVPKVGTVAG CYVLEGVVKR GSQVRVLRNH VVIHNGELES
LKRFKDDVKE VKFGFECGLS IRNFNDVQEG DQLEVFEIQE IARTL
