ID   IF2C_GUITH              Reviewed;         735 AA.
AC   O78489;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
GN   Name=infB;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(1999).
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; AF041468; AAC35680.1; -; Genomic_DNA.
DR   RefSeq; NP_050746.1; NC_000926.1.
DR   AlphaFoldDB; O78489; -.
DR   SMR; O78489; -.
DR   GeneID; 857051; -.
DR   HOGENOM; CLU_006301_5_2_1; -.
DR   OMA; NRDNRTG; -.
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..735
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000137291"
FT   DOMAIN          239..411
FT                   /note="tr-type G"
FT   REGION          248..255
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          273..277
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          298..301
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          352..355
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          388..390
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..255
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         298..302
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         352..355
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   735 AA;  82595 MW;  732B5E58BA68BA84 CRC64;
     MKFDNHTYIQ NYTSSDDETI VLINPLILNL FNKTNYDISQ SNKQKDSIYH LDINIKTNSK
     LDKKSKKIDR NQDEVDELAK SKTKSKKKVQ VEFETDDEYL NVFNKPKHFD IVEKNIRKTE
     ILNEIKTINS ATGKKNKKLL SRKKEEIVED NQIPKELRIN SSLTVQEFAE LTCISDIEII
     RTLFLKGQAV TVNQILDINT IIELGKDFHI NIQIEEKNGL NEVNIEKNNF IKFSENTIRR
     APIVTILGHV DHGKTTLLDK IRQTQIAQKE AGGITQKIAA YKVNVQYKNE NRNIVFLDTP
     GHEAFSNMRS RGINVTDIVI LLVAADDGVK PQTIEAINAI KAAKLPIIVA INKIDKDQAN
     IEKVQQELSK YELIPESWGG QTPMIPISAS QGTNIDSLLE LILLMADIEN YQAIEEDLAS
     GTILESHIDR TRGPIASILV QNGTLKLGDI IVTGTSLGKI RGMLDSEGNK INTLTPSSPG
     IIWGLNKSLN SGDKFQTFSN EKDAKTYFSK ESENNKKITY NYISENPSNQ ILEESSKKIL
     NFILKTDTQG SIEAIVNAIS RIKTKQLQIK ILYSNLGEVT ETDVEFASTT NAFVLAFNTR
     LAPGAKKTAR QLNIDIREYN VVYDLVEDIE SLIAQHSEPE YKKLKIGAAT VKAVFPLGKN
     FVAGIIINEG KIVRSAHIQV QRKSGLVFEG DITTIKIVKK DVEEVSEGNE CGLFIEEFSE
     WKVGDSIEIF ELIQI