IF2_ALIFM
ID IF2_ALIFM Reviewed; 893 AA.
AC B5FA79;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VFMJ11_0487;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) 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; CP001139; ACH65211.1; -; Genomic_DNA.
DR RefSeq; WP_012532896.1; NC_011184.1.
DR AlphaFoldDB; B5FA79; -.
DR SMR; B5FA79; -.
DR PRIDE; B5FA79; -.
DR EnsemblBacteria; ACH65211; ACH65211; VFMJ11_0487.
DR KEGG; vfm:VFMJ11_0487; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001857; 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.
FT CHAIN 1..893
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093843"
FT DOMAIN 392..561
FT /note="tr-type G"
FT REGION 51..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..408
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 426..430
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 447..450
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 501..504
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 537..539
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 59..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401..408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 447..451
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 501..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 893 AA; 97336 MW; D5CB3D1BC7998098 CRC64;
MTKLTVKALS EEIGTPVDRL LQQFSDAGIN KKDGDSVSEG EKQSLLVHLK KEHGSADDSA
SPTRLTLQRK TRSTLSVAGS GGKSKDVQVE VRKKRTYVKA SALEEEKKAE QLKAEAEEQA
KRDAEEAAVR ELEQKAQREA EEQAKREAEA EAKAKREAEE KAKRAEADKA KKEMTKKNEQ
AKKEADELKA RQELEATRKA EAEAAKLVEE ARKLAEENEA RWKEEEQKKS AAEKDADYHV
TTSSHAREAE DAADRKEEQQ PRRRKKKAKP AEAAAPRGGR NQRGGRNKKA QVNKPTSMQH
GFDKSATVAK QDVAIGETIV VSELASKMSV KATEVIKVMM KMGAMATINQ VIDQETAQLV
AEEMGHKVIL RKENELEEAV LSDRDNSAEA EGRAPVVTIM GHVDHGKTST LDYIRRAHVA
DAEAGGITQH IGAYHVETDN GMITFLDTPG HAAFTAMRAR GAQATDIVVL VVAADDGVMP
QTIEAIQHAK AAGVPLIVAV NKIDKEGANP DNVKNELAQY DVIPEEWGGE NIFVHISAKQ
GTNIDGLLEA ILLQSEVLEL TAVREGMASG VVVESRLDKG RGPVATVLVQ SGTLNKGDIV
LCGQEYGRVR AMRDENGKDI ESAGPSIPVE ILGLSGVPAS GDEATVVRDE RKAREVANYR
QGKFRDVKLA RQQKAKLENM FANMEAGEVA ELNVVLKADV QGSVEAIADS LLKLSTDEVK
VNIVGSGVGG ITETDATLAA ASNAIILGFN VRADATARRT VENENLDLRY YSIIYQLIDE
VKAAMGGMLA PEFKQEIIGL AQVRDVFKSP KLGAIAGCMV TEGTIKRSNP IRVLRDNVVI
YEGELESLRR FKDDVAEVKN GYECGIGVKN YNDVRVGDQI EVFEIVEIKR TLD
