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Database: UniProt
Entry: IF2_BURMS
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ID   IF2_BURMS               Reviewed;         975 AA.
AC   A1V3N4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=BMASAVP1_A1507;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAVP1;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000526; ABM50690.1; -; Genomic_DNA.
DR   RefSeq; WP_004197388.1; NC_008785.1.
DR   AlphaFoldDB; A1V3N4; -.
DR   SMR; A1V3N4; -.
DR   GeneID; 56595459; -.
DR   KEGG; bmv:BMASAVP1_A1507; -.
DR   HOGENOM; CLU_006301_6_0_4; -.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR004161; EFTu-like_2.
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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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..975
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008213"
FT   DOMAIN          475..644
FT                   /note="tr-type G"
FT   REGION          48..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..491
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          509..513
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          530..533
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          584..587
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          620..622
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        48..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         484..491
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         530..534
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         584..587
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   975 AA;  104751 MW;  447642044BA93AA7 CRC64;
     MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE TDKARLLDHL RKSHGATDGD
     KRKITLTRRH TSEIKQADAT GKARTIQVEV RKKRTFVKRD DVSETGADQA QAQTDEQAEA
     ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
     AAAQAEAAQQ AAAAREQAQR AQSEPAEQSA QDEARAAAER AAQREAAKKA EDAAREAADK
     ARAEQEEIRK RREAAEAEAR AIREMMNTPR RAQVKAVEPP KPAEPPAAKA AEAKGTLHKP
     AKPAGEAAAA RPAAKKPASG APAPAAAPAG DRTKKPGTGK SGWQDDAAKR RGIKTRGDSS
     GGVDRGWRGG PKGRGKHQDS ASSFQAPTEP IVREVHVPET ISVADLAHKM SIKASEVIKV
     MMKMGQMVTI NQVLDQETAM IVVEELGHRA LAAKLDDPEA LLVEGEIGSD AEQLPRPPVV
     TVMGHVDHGK TSLLDYIRRA KVAAGEAGGI TQHIGAYHVE TPRGVVTFLD TPGHEAFTAM
     RARGAKATDI VILVVAADDG VMPQTKEAIS HAKAGGVPIV VAINKIDKPE ANPDRVKQEL
     VAEGVVPEEY GGDSPFVPVS AKTGAGIDDL LENVLLQAEV LELKAPVESP AKGIVIEAKL
     DKGKGPVATV LVQSGTLSRG DVVLAGTAYG RVRAMLDENG KPTKEAGPSI PVEIQGLSEV
     PGAGDEVIVL PDERKAREIA LFRQGKFRDV KLAKQQAAKL ESMLEQMGEG EVQNLPLIIK
     ADVQGSQEAL VQSLLKLSTD EVRVQIVHSA VGGISESDVN LATASKAVII GFNTRADAQA
     RKLAEANGID IRYYNIIYDA VDEVKAAMSG MLAPEKREVV TGMVEVRQVF KVPKVGTVAG
     CMVTDGVVKR SSSVRVLRNN VVIFTGELDS LKRFKDDVKE VKQGFECGMS LKNFNDIVEG
     DQFEVFEVTE VARTL
//
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