IF2_ANADE
ID IF2_ANADE Reviewed; 950 AA.
AC Q2IPZ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Adeh_1102;
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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; CP000251; ABC80877.1; -; Genomic_DNA.
DR RefSeq; WP_011420160.1; NC_007760.1.
DR AlphaFoldDB; Q2IPZ7; -.
DR SMR; Q2IPZ7; -.
DR STRING; 290397.Adeh_1102; -.
DR EnsemblBacteria; ABC80877; ABC80877; Adeh_1102.
DR KEGG; ade:Adeh_1102; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001935; 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; 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..950
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008195"
FT DOMAIN 449..618
FT /note="tr-type G"
FT REGION 57..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..465
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 483..487
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 504..507
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 558..561
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 594..596
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 504..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 558..561
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 950 AA; 100890 MW; F27176B98F9726BA CRC64;
MSKKRVHELG KQLKEQGIEL SNQELVEKLH ALGYLEVKSH SSSLEDDQAH AAYEKILAER
KPKPAPARPS GPGFVVRKRA HVEPPTVTAP AAPPSPEPEY AEPQYAEPQA EQAYEPEPQA
AQPEAGAEPA AAPEPPAEAA PLAAQAAPSP GAEAAAPAAP QAQPAQPAAP AAPPAPTAQP
SAPPPAAAQP RPPQPSAPSR PPPPGYRPAP PPGARPPVSA APGAPGQPGA AGQPPRPPVD
PRTLRPTSTQ AVVISRPLVP VRRVTPPTSA RQQFPVAPGP RALGEVRELK VVPGSLGRER
EFIDVSRDKR RGRQPGRPIS EEQAKSLSGK ELLQAAISDR AYIPIRGKKK KPTKKGAKTQ
ITEKAEHKKV IRIEESISVS ELSQVMGVKA SDLIRKLMQM GKMVTINAQI DADTAATLAL
EHGYTVEKKG FEVEEFIPEV EVDESKLVIR PPVVTVMGHV DHGKTSLLDA IRQADVAAGE
AGGITQHIGA YSVNTPQGPI TFLDTPGHEA FTAMRQRGAQ VTDLVVLVVA ADDGVMPQTV
ESIKAAKAAG VTILVAINKV DKPQAAPERV MQQLTEYELV AEQWGGTTIM LPVSARTKQG
IPELLEYIAL QSEVLELKAN PDKLAAGRVI EAKLEKGRGP VATVLVEEGT LRVGDALVTG
VHFGRVRAMM NERGEQVDNV GPGYPVEVLG LSGVPVAGDE FDVVEDEKAA KEVAQHRATK
QRQKELGGVK KATLEDLFAK AKTSAQKVLN LVVKADVQGS SEAVSQALEK AATKKVGVKI
LESAVGAITK SDVLTAAAGN AVIVGFNTKP ETEIENIASQ QGVKILMFGI IYEAVDRIRE
EMAGLLEPII KEKPLGKAEV RQVFNIPRVG QIAGSAVTEG VVKRAGHVRV VRDRKVVFTG
KIGSLKRVKD DVREVAQGFE CGIGVDGFSD VKQGDVLEVY ELEEIRQSLD
