IF2_ACICJ
ID IF2_ACICJ Reviewed; 887 AA.
AC A5FV21;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Acry_0225;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
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 Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-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; CP000697; ABQ29453.1; -; Genomic_DNA.
DR RefSeq; WP_011941367.1; NC_009484.1.
DR AlphaFoldDB; A5FV21; -.
DR SMR; A5FV21; -.
DR STRING; 349163.Acry_0225; -.
DR EnsemblBacteria; ABQ29453; ABQ29453; Acry_0225.
DR KEGG; acr:Acry_0225; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000245; 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; 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; 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..887
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008189"
FT DOMAIN 386..556
FT /note="tr-type G"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..402
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 420..424
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 532..534
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 395..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 887 AA; 95356 MW; FCE3051B674F0CCF CRC64;
MSDEQDQGET KGRLSLRPVN RGELGRTVDA GSVRQSFSHG RSKVVQVEVR KKRGGAAGAE
TGRPSAPSRA SGGAAAPRGL TAAEQAARQR AVVEQQREAA RLEAERREQE KISILSAAEE
ARRKAEEEAR AAEEAERLRA EEEARRREEE EAERRRAAEA SQATAAPPAP AAAASPRAAM
PAPTAAPARP GAAPARRTAP VPPATSASET LRLRAARTGR DEEEEASRPA RRPGSGAAPS
RKPSVPAPKK VGDDRRRGAR IDVQAALSGD DERVRSLASV RRQRDRERRQ AELERLRSDQ
VRVVREVVLP ETITVQELAN RMAARVPEVV KSLMKLGVMA TATQTIDADT AELVVEEFGH
RSKRVSESDV ELGLEGQEDS ETDLKVRPPV VTIMGHVDHG KTSLLDALRS TDVAAREAGG
ITQHIGAYQV TLESGAKMTF IDTPGHEAFT AMRARGASVT DIVILVVAAD DGVMPQTVEA
IRHAKAANVP IIVAINKIDR PDANPNRVRS ELLQYDIAVE AMGGETQDVE VSALKRQGLD
ALQEAILLQA ELLDLKANPN RSAEGAVIES SLDRGRGPVA TVLVQKGTLR QGDIVVAGTE
QGRVRAMLDD HGQPLKDAGP STPVEILGLS GVPGAGEVFV VVENEGRARE IAEFRQRKLR
EHAAAAGAAA RGTLDQMLAR IQAGEQKEVA LVIKADVQGS AEAIQATVQK LGNDEVRVRV
LLAGVGQITE SDVQLAKASD AIIVAFNVRA NAQARTLASR DGVDIRYYSI IYQVSDDIET
MVKGKLAPIE REKFLGYAEI RQVFNITKVG KVAGCYVTEG LVKRGAGVRL LREGVVIHQG
ELSQLKRFKD DVREVARGYE CGLSFAGFSD LREGDVVECY ETETVPA
