ID   IF2C_PORPU              Reviewed;         763 AA.
AC   P51257;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
GN   Name=infB;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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; U38804; AAC08143.1; -; Genomic_DNA.
DR   PIR; S73178; S73178.
DR   RefSeq; NP_053867.1; NC_000925.1.
DR   AlphaFoldDB; P51257; -.
DR   SMR; P51257; -.
DR   PRIDE; P51257; -.
DR   GeneID; 809886; -.
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   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..763
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000137292"
FT   DOMAIN          261..429
FT                   /note="tr-type G"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270..277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         316..320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         370..373
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   763 AA;  84305 MW;  8B33265DBD6A4DCE CRC64;
     MFLNNQNFEK KTSSYSTNNN SSEKIVDLKN PQFIYKIRLE STSTDNLLHL DIDKSETDGP
     NTEQHLELSS PPRIDKKNKN FNKAHDLLDN KKNKNRQRKK IKNKIHIDDD DDNFSDSTSN
     SAQTAGDLAI SLMRPPKPRS QSIKKVIGNN KIPQQKKQQV ASSIDQSITL PNSPPESISL
     INPLTIQELS RLICIPETDI IKYLFLKGIS VTINQTVDNT IISSVAKNFG IAVDSQEQNN
     KKKKLTNLDI PVIVDNHHCV NRPPVVTILG HVDHGKTSLL DYIHKSNNAN KEVGGITQNI
     VAYEVEFKHQ QIVFLDTPGH EAFTSMRSRG ANLTDIAIII IAADDGIKPQ TIEAIQHLQK
     ANVPFIVAIS KIDKNLDSVD KIQHDLVAQN VISEKLGGSV PIIPISSVTG ENIDKLLETI
     LLLAELENLQ ADPTQLAQGV IIEAHLDKFH GPAATLLIQN GTLHIGDNMV IGMTHAKIRA
     IINNAKQKIN LAAPSSVVEI WGLSSVPATG EVALVVNSDK EAKLKAIENE STNSIIVQKQ
     KSLNSRITLD TISTINAKDE NKQVTLIIKT DNQGSTEAIL DSLSQFPQSK VQLNVLSIFP
     GEITATDVEL ASTTNSSLIG FNTNFAPGSR QAAAKLNVII ENYQIIYALI EGVREKMETL
     LDPEYSEVPV GEAEVGTVFS LANRKIAGCR VTNNKLLKNS WIKVLRENEI VYQGKIESLK
     RIREDVEEIQ AGNECGIFIS EFQLWQTGDK IQSFDLVPKK RSL