IF2_PSET1
ID IF2_PSET1 Reviewed; 886 AA.
AC Q3IJ53;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PSHAa0997;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(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; CR954246; CAI86075.1; -; Genomic_DNA.
DR RefSeq; WP_011327686.1; NC_007481.1.
DR AlphaFoldDB; Q3IJ53; -.
DR SMR; Q3IJ53; -.
DR STRING; 326442.PSHAa0997; -.
DR EnsemblBacteria; CAI86075; CAI86075; PSHAa0997.
DR KEGG; pha:PSHAa0997; -.
DR PATRIC; fig|326442.8.peg.957; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; PHAL326442:PSHA_RS04870-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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..886
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228228"
FT DOMAIN 386..555
FT /note="tr-type G"
FT REGION 46..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..297
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 441..444
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 495..498
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 531..533
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 63..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..260
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 441..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 495..498
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 886 AA; 96674 MW; 073DAA4EC06142B3 CRC64;
MAEVNVEKLA GDIGTTVDKL LQQFSQAGIT KQAGESVTEA EKATLLDHLS KQHGGTGSDG
PARMTLQRKS KSTLSVTGST GKAKSVQVEV RKTRTYVKKS AMEQEQEELR LAAEEKLRLE
EQQKAAQEAA ELKAKQEAER KAKEDADRKA KEEAKRKADA ERKAKQKQMT PEQSAKSEKD
RIEAERLQKE AEEAALKKAE EEAKRQAEEA RKLAEENSAR WKKEEEERKK REETSDHHLT
TSTYAREAED VADARDEQGT RRAKKKKKAP AKDKFAASKG RNKGKLKAPT SLQHGFTKPT
ADVKNEVRIS ETITVAELAS RMAVKGAEVV KTMMKMGDMV TINQVIDQEA AQLVAEEMGH
KVIIVKENEL EQKVLNDRHE DGKSEPRAPV VTVMGHVDHG KTSTLDYIRS AKVASGEAGG
ITQHIGAYHV DVNGNMITFL DTPGHAAFTS MRARGAQATD IVILVVAADD GVMPQTKEAV
QHARAAGVPL IIAVNKMDKE GVDPDRVKNE LAQLDVIPEE WGGDTQYVHI SAKTGLGIDE
LLEAVLNQSE LLELTAPTVG MAAGVVIESR LDKGRGPVAS ILVQSGTLNQ GDIVLCGLEY
GRIRAMRDEN GKDIKSAGPS IPVEILGLSG IPAAGDEATV VKDERKAREV ALYRQGKFRD
VKLARQQKAK LENMFSHMTE GDVSEVNVVL KADVQGSIEA ISDSLTKLST DEVKVKIVGS
GVGGITETDA TLAAASNAIV VGFNVRADAS ARKVIESENL DLRYYSVIYS LIDEVKQAMS
GMLAPEFKQE IIGLAQVRDV FKSPKIGAIA GCMVTEGVIK RSAPIRVLRD NVVIYEGELE
SLRRFKDDVA DVRNGMECGI GVKNYNDVRV GDQIEVFETV EIQRTL
