IF2_ALIF1
ID IF2_ALIF1 Reviewed; 893 AA.
AC Q5E7L5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VF_0486;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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; CP000020; AAW84981.1; -; Genomic_DNA.
DR RefSeq; WP_011261258.1; NC_006840.2.
DR RefSeq; YP_203869.1; NC_006840.2.
DR AlphaFoldDB; Q5E7L5; -.
DR SMR; Q5E7L5; -.
DR STRING; 312309.VF_0486; -.
DR EnsemblBacteria; AAW84981; AAW84981; VF_0486.
DR KEGG; vfi:VF_0486; -.
DR PATRIC; fig|312309.11.peg.476; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000537; 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..893
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228258"
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..299
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 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; 97555 MW; 7FE41029382211C6 CRC64;
MTKLTVKALS EEIGTPVDRL LQQFSDAGIN KKDGDSVTES EKQSLLVHLK KEHGSVDDSA
SPTRLTLQRK TRSTLSVAGS GGKSKDVQVE VRKKRTYVKA SALEEEKKAE QLKAEAEEQA
KRDAEEAAVR ELEQKAQREA EEQAKREAEA EAKAKREAEE KAKRAEADKA KKEMTKKNEQ
AKKEAEELKA 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 NKIDKEDANP DNVKNELAQY DVIPEEWGGE NMFVHISAKQ
GTNIDGLLEA ILLQSEVLEL TAVREGMASG VVVESRLDKG RGPVATVLVQ SGTLNKGDIV
LCGQEYGRVR AMRDENGKEI ESAGPSIPVE ILGLSGVPAS GDEATVVRDE RKAREVANYR
QGKFRDVKLA RQQKAKLENM FSNMTAGEVA ELNVVLKADV QGSVEAIADS LRKLSTDEVK
VNIVGSGVGG ITETDAVLAA ASNAIILGFN VRADATARRT IENENLDLRY YSIIYQLIDE
VKAAMGGMLA PEFKQEIIGL AQVRDVFKSP KLGAIAGCMV TEGTIKRSNP IRVLRDNVVI
YEGELESLRR FKDDVAEVKN GYECGIGVKN YNDVRVGDQI EVFEIVEIKR TLD
