ID   IF2C_RHDSA              Reviewed;         751 AA.
AC   A6MVX8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
GN   Name=infB;
OS   Rhodomonas salina (Cryptomonas salina).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX   NCBI_TaxID=52970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1319 / NEPCC76 / CS-174;
RX   PubMed=17522086; DOI=10.1093/molbev/msm101;
RA   Khan H., Parks N., Kozera C., Curtis B.A., Parsons B.J., Bowman S.,
RA   Archibald J.M.;
RT   "Plastid genome sequence of the cryptophyte alga Rhodomonas salina
RT   CCMP1319: lateral transfer of putative DNA replication machinery and a test
RT   of chromist plastid phylogeny.";
RL   Mol. Biol. Evol. 24:1832-1842(2007).
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}.
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DR   EMBL; EF508371; ABO70809.1; -; Genomic_DNA.
DR   RefSeq; YP_001293557.1; NC_009573.1.
DR   AlphaFoldDB; A6MVX8; -.
DR   SMR; A6MVX8; -.
DR   GeneID; 5228605; -.
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: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; 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.
PE   3: Inferred from homology;
KW   Chloroplast; GTP-binding; Initiation factor; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..751
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000335538"
FT   DOMAIN          250..423
FT                   /note="tr-type G"
FT   REGION          86..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..266
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          284..288
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          309..312
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          363..366
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          399..401
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        86..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         259..266
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..313
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         363..366
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   751 AA;  83013 MW;  F9F663D70CC71E02 CRC64;
     MNNNIAISKE NTIKLSFPLV FDTKTTNTST KEYVETIKED EKVDLFDPTI DTKLFVKPDR
     KTKKNDKSDQ RDSDIDIIKT KLKSKKKEKS KFRKDEDYDS LKREDNQSPQ GAMSSLPFAR
     PEVPAKKMVS NTNTLNKKNV VKSSTKKSKK QTSAKNRELE QNLLVKPENV VIAGPLSVQE
     LAVLLTVSET EIIRSLFLKG IGVTINQILD VSTAKTVGED LGINIDHVKD SDEESKKLQI
     HEIDNESLEK RPPVIAIMGH VDHGKTTLLD KIRKTQIAQK EAGGITQKIG AYEVEIDYKD
     QTKKLTFLDT PGHEAFSGMR SRGVQVTDIA ILVVAADDGV KPQTVEAIKY IQAANVPIIV
     AINKIDKENA DIENIKQQLT QYNLIPENWG GDTLMVPISA MKGTNMENLL EMIILVSEIE
     DLKANTKVKA QGTVLEAHLD RTKGAVATLL VQNGTLRIGD ILTAGTSMAK IRGMINSLGE
     KIEECLPSSP VLIWGLSKLP ASGEHFEIFD DEKQAKIAVQ KAQEANKENQ TIANTISENY
     TLSNSNTKGV INLIIKTDIQ GSAEAIIGSI NKIPQDKVQV RVLYASAGEI TETDIDFADT
     SGAIVLAFNT SLATGASKAA RHLNVKVKEY DVIYDLLDYI ELTIEEITGP EYDKKSLGKA
     IVQGVFPLAK SFVAGLRVTE GKITKNAHIE VIRQDLVVFD GSITSLKKVK EDIGEAIEDS
     ECGLFVEEFD TWQENDIVQA FELIPKKRKE K