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Database: UniProt
Entry: Q5GS99
LinkDB: Q5GS99
Original site: Q5GS99 
ID   IF2_WOLTR               Reviewed;         777 AA.
AC   Q5GS99;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Wbm0537;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(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; AE017321; AAW71125.1; -; Genomic_DNA.
DR   RefSeq; WP_011256735.1; NC_006833.1.
DR   AlphaFoldDB; Q5GS99; -.
DR   SMR; Q5GS99; -.
DR   STRING; 292805.Wbm0537; -.
DR   KEGG; wbm:Wbm0537; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   Proteomes; UP000000534; Chromosome.
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; 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; 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; 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; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Reference proteome.
FT   CHAIN           1..777
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228260"
FT   DOMAIN          279..449
FT                   /note="tr-type G"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..295
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          313..317
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          334..337
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          388..391
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          425..427
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        98..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         288..295
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         334..338
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         388..391
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   777 AA;  86324 MW;  BC0B0EBD48667A21 CRC64;
     MNSKDISSKK LTLQGFSKLK LDFNLSSSAS PSMGATIVKK RRRKTHDTEE QDENKLLGSL
     TKKEQISRIN AVQNAALLKE RNLKEKEAIV KKDSIVKEDS NEKTNDRDSA TNTSFKETGK
     EVLNDVSLVE LIENNTDNED NNKKSLKTNK DIYSKHSKRI IAQSIDDKIE QPSVFKQRFG
     IRNRKSEFTK GKNISREVII PDEITIKELS IRMAEDSKSV LKMLKEEMGE NYGVDGLVDP
     EVACEIVEKF NHTAKRVSGA NKEKNLFFIE ERESLPKKPK PPIVTFMGHV DHGKTSLLDA
     FRESNVAERE LGGITQHIGA YQIITKDKKI TFIDTPGHEA FTAMRACGAN ITNIVVIVVA
     ADDGVMKQTI EAMNHAKAAN VSIIVAINKI DRSQSGDVER IISSLPQYDL IPEELGGDVI
     VVPVSAKKKI NLDKLEEAIL LIAELMKLEA IEDCRALGWV IESKIDKAKG ISATLIVEEG
     TLKVGDMLVV GTAYGKVRSM VNHLGQREKV ALPSSPIEIT GLNGIPNAGD KFVVVSSEKQ
     AREIAEYRLE LIKEKKEDLS NNNLDMFSRN DSEVEELSVV LKCDVTGSIE AISNSIDKLG
     KDQVKLNILH KAVGGITDSD VLLAEASSAV ILAFNVKVDS KIRDLAKRKG VEIHTYSIIY
     ELIDDMRMYL TKMLKPVTRE VRIGSASVRQ IFNVSRVGNI IGCYVSDGVV KKDSLIKVMR
     NNKLIYEGKL KALRRFKDNV KEVGTNFECG VSLDGNVDIK VGDILEAHQL VQEERVL
//
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