ID   IF2C_EUGGR              Reviewed;         822 AA.
AC   Q9XEK9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
DE   Flags: Fragment;
GN   Name=INFB;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B;
RA   Ward J.M., Ma L., Blanchard K., Spremulli L.L.;
RT   "Characterization of a 'gamma' form of initiation factor 2 from Euglena
RT   gracilis chloroplast.";
RL   Submitted (NOV-1998) 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF109129; AAD20591.1; -; mRNA.
DR   AlphaFoldDB; Q9XEK9; -.
DR   SMR; Q9XEK9; -.
DR   PRIDE; Q9XEK9; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 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; PF04760; IF2_N; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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   2: Evidence at transcript level;
KW   Chloroplast; GTP-binding; Initiation factor; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           <1..822
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000137293"
FT   DOMAIN          311..486
FT                   /note="tr-type G"
FT   REGION          1..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..327
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          345..349
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          372..375
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          426..429
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          462..464
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         320..327
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..376
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         426..429
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   822 AA;  87702 MW;  6B22467AAE52BE52 CRC64;
     FQSSGSPIKP RINLDRPSTS TPTPPEAPTS PSARQPVTQV PQANSVPAGA VASQAEVKKP
     ADPQPPATPS APVLRRPVRT AMPASPPRMV INLDDIPDRS KPVWPAPPPR AKGQGGGKGG
     KGGKGGKGGK GGKGDREQPA VVRRAKPRRT ASTAEGPAAE SKESGGREAQ IWVTPKGGKG
     RDKWKKGKEE VDKSEALLLK ARKKTRLERK ERREEVREAN AAKKEEIIEV GPQGMTVSEI
     AGKLAITPAN VVTVLFKKGI MSAPSQTIAY DLVKIVCDEY KVEVLEVEEE DGIASMEDRF
     VLDEEAEALV SRPPVVTIMG HVDHGKTSLL DYIRKSNVVA GEASGITQAI GAYHVEFASP
     TDGTPTFISF IDTPGHEAFT AMRARGATVT DITIIVVAAD DGVRPQTKEA IAHCKAAGVP
     MVVAINKIDK DGADPERVMN ELAQAGLVPE EWGGEVPTVK ISAKKGLGIK ELLEMILLTA
     EVADLKANPA APAEGTVIEA YLDRTRGPVA TVLVQNGTLR AGDVVVTNAT WGRVRAIMDE
     KGAMLEAAPP SLPVQVLGLD DVPAAGDKFE VYASEKEARD KVDEFERTKK EKNWASLASR
     DLVRLDNNAD GKGLEVMNVI LKTDVSGSCE AIRAALDTLP QTKIELRLIL ASPGDITVSD
     VNLAASTGSI ILGFNVDTFS AAEALIKNLG IKCMTFDVIY DLVDQMKAVM EGKLGDEQIP
     EKAGEAEVKA VFAARNGKKA AGCLVVAGRL VAPAFIEVLR KKKILFSGQL FQLRRMKDNV
     SEVGTDTECG VTLDDFDDWQ EGDRIVCYST VTRQRALEAT PA