ID   IF2C_GRATL              Reviewed;         744 AA.
AC   Q6B8S2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Translation initiation factor IF-2, chloroplastic;
GN   Name=infB; OrderedLocusNames=Grc000132;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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; AY673996; AAT79713.1; -; Genomic_DNA.
DR   RefSeq; YP_063638.1; NC_006137.1.
DR   AlphaFoldDB; Q6B8S2; -.
DR   SMR; Q6B8S2; -.
DR   GeneID; 2943949; -.
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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Chloroplast; GTP-binding; Initiation factor; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..744
FT                   /note="Translation initiation factor IF-2, chloroplastic"
FT                   /id="PRO_0000232592"
FT   DOMAIN          244..417
FT                   /note="tr-type G"
FT   REGION          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..260
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          278..282
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          303..306
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          357..360
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          393..395
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253..260
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..307
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..360
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   744 AA;  82984 MW;  70CFA35E6AB08B5A CRC64;
     MRYSNVIDFS ICMSIKSENT FLLENPKFIK NLKFFNIHSS QEPKSPTDIR NSVENSDFNV
     QLENKLKNSF KQDGKQKSKK KKILSVDLDQ EHIFKKKNKS KVIISAPDDL TNNSEGSFKS
     GKQKKKEKGK HKQNVNKDIH HTKNNRLSNL DPLDDINKDK SVIIDSSLSI EELSIKLKIP
     PAEIITGLFL KGISVTVNQI IDIAIATQVA QKYNFTVINQ NQNNQSELDQ SDKLQQVSTI
     TSINRAPIVT ILGHVDHGKT TLLDAIRNTN AAGKEIGGIT QSIKAYEVNW PYNSSNQKLI
     FIDTPGHEAF SSMRLRCAQI TDIVILIIAA DDGLKPQTIE AINYISSKKT PFIVAINKID
     KANLNLIRVR EELATYNIIS TDWGGEIQFI EISALQKRNI SQLLTAICSL AEFINLKADP
     TELVQGSILE AYLDKTKGIV VNIIVLSGTL HIGDIIVSGH SYGRVKKIIN SLGNELIQAG
     PSSILEVLGF YSIPQTGRYF QVVNSEKEAK KMIAQIPLSG ITQTTKNILN LNPKVYNHNL
     NTRSLNLIIK ADTQGTIDAI INSFIQISQK KIKLNILTAS LGVVSNTDLD LAFSTQALII
     AFNINISTNI LNAAEKLNLS LRKFVLIYDL VDYVTYSMLD LVDPEYDKIL IGQAEVQTTF
     TINKGTVAGC IVKSGKLKKD ALIGVYRKNK LIYEGVINSL KRMKNDVNEV VIGNECGILS
     KDYHFWQSED LIKAYELHEK AKTL