ID   IF2C_NEOYE              Reviewed;         768 AA.
AC   Q1XDN0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
GN   Name=infB;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) 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}.
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DR   EMBL; AP006715; BAE92381.1; -; Genomic_DNA.
DR   RefSeq; YP_536938.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDN0; -.
DR   SMR; Q1XDN0; -.
DR   GeneID; 3978891; -.
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; 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   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..768
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000275386"
FT   DOMAIN          261..434
FT                   /note="tr-type G"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..176
FT                   /note="Disordered"
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         320..324
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..377
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   768 AA;  84825 MW;  88D7075C7D8B61E7 CRC64;
     MFLNNQNFEN RSSRSSSNIN SSETIVDLKN PQIIYKIRLE SVNNDNLLNL DLDKSESHTG
     GEQHLELSSP PKLDKKSKNF NKIHDLVDSK KNKNRQRKKI KTKIHIDDDD DNFRDSNSNV
     SQTAGDLAIS LMRPPKPKVE VVKKLTSNKK SIRQKKVAVT PSQNSASIQS NSPPESISIT
     NPLTIQELSK LICVQETDII KYLFLKRISV TMNQTIDASI ISSVADNFGI AVESNVKENN
     NGLSSNLDNS NAFYETGNYI KRPPIVTVMG HVDHGKTTLL DYIRKSNNAN KEIGGITQAI
     AAYEVEYIKK DNKQKIVFLD TPGHEAFTSM RSRGANLTDV AIIIIAADDG VKPQTIEAIN
     HIQKANVPFV IAISKIDKAG SNTDIIEQDL LKYNVMSEKL GGQVPIIPIS SLTGQNVDKL
     LETITLLAEL EDLKADPTQP AQGIIIEAHL DKSHGPVATL LIQNGTLNIS DNLVIGSAYA
     KIRVIINNAK EKINLAIPSS VVEIWGLSSV PATGEIALAV KSDKEAKLKA IENTSKDSSI
     IQKQRALNSR ITLDTLKNTN SKDISKQISL IIKTDNQGST EAILDSLSQF PQSKVQLNVV
     SIMPGEITAT DVELASTTNS TLIGFNTNFA PGTKQASAKS NILIENYQII YALIEDIKRR
     MEDLLDPEYS EVPVGEAEVS TVFSLANRKI AGCRVINNKL LKNSWIKVIR EEKVIYQGKI
     ESLKRVREDV EEIQAGNECG IFISEFQLWQ SGDKIHSFDL IPKQKSLF