IF2_ALISL
ID IF2_ALISL Reviewed; 891 AA.
AC B6ENE2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VSAL_I0598;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ78283.1; -; Genomic_DNA.
DR RefSeq; WP_012549406.1; NC_011312.1.
DR AlphaFoldDB; B6ENE2; -.
DR SMR; B6ENE2; -.
DR STRING; 316275.VSAL_I0598; -.
DR PRIDE; B6ENE2; -.
DR EnsemblBacteria; CAQ78283; CAQ78283; VSAL_I0598.
DR KEGG; vsa:VSAL_I0598; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001730; Chromosome 1.
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; 1.
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..891
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093754"
FT DOMAIN 390..559
FT /note="tr-type G"
FT REGION 50..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..406
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 424..428
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 499..502
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 535..537
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..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 499..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 891 AA; 97549 MW; 8D94BC6B0C3B1A6E CRC64;
MTKLTVKALS EDIGTPVDRL LQQFSDAGIN KKDGDSVSEG EKQSLLIHLK KEHGSADESA
SPTRLTLQRK TRSTLSVAGS GGKSKDVQVE VRKKRTYVKA STLEEEKKTE QMKVEAGDKA
KRDAEEAAVR ELEQKAKREA EEKAKREAEA EVKVKRDAEQ TAKRTKTEKA KKEMTTKNDQ
AKTEADELKL RQETEATRKA EAEAAKLVED ARKLAEENEG RWKEEEQKKT AAEKTADYHV
TTSTHAREAE DAADRKDEQQ PRRRKKKAKA APVERGGRNQ RGGRNRKPQV NKPTSMQHGF
DKSATVAKQD VAIGETIIVS ELANKMSVKA TEVIKVMMKM GAMATINQVI DQETAALVAE
EMGHKVVLRK ENELEEAVLS DRDNSATVEG RAPVVTIMGH VDHGKTSTLD YIRRAHVADA
EAGGITQHIG AYHVETDNGM ITFLDTPGHA AFTAMRARGA QATDIVVLVV AADDGVMPQT
IEAIQHAKAA GVPLIVAVNK IDKEGANPDN VKNELAQYDI IPEEWGGENM FVHISAKQGT
NIEGLLEAIL LQSEVLELTA VKEGMASGVV VESRLDKGRG PVATVLVQSG TLHKGDIVLC
GQEYGRVRAM RDENGKDIDS AGPSIPVEIL GLSGVPASGD EATVVRDERK AREVANYRQG
KFRDVKLARQ QKAKLENMFA NMEAGEVAEC NVVLKADVQG SVEAIADSLR KLSTDEVKVN
IVGSGVGGIT ETDATLAAAS NAILLGFNVR ADTSARRTIE NENLDLRYYS IIYQLIDEVK
QAMGGMLAPE FRQEIIGLAQ VREVFKSPKI GAVAGCMVTE GTIKRNNPIR VLRDNIVIYE
GELESLRRFK DDMPEVKNGY ECGIGVKNYN DVRVGDQIEV FEIVEIQRTL D
