ID   IF3C_EUGGR              Reviewed;         538 AA.
AC   P36177;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Translation initiation factor IF-3, chloroplastic;
DE            Short=IF-3chl;
DE   Flags: Precursor;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=B;
RX   PubMed=8144528; DOI=10.1016/s0021-9258(17)36900-4;
RA   Lin Q., Ma L., Burkhart W., Spremulli L.L.;
RT   "Isolation and characterization of cDNA clones for chloroplast
RT   translational initiation factor-3 from Euglena gracilis.";
RL   J. Biol. Chem. 269:9436-9444(1994).
RN   [2]
RP   ERRATUM OF PUBMED:8144528.
RX   PubMed=8207023; DOI=10.1016/s0021-9258(19)89490-5;
RA   Lin Q., Ma L., Burkhart W., Spremulli L.L.;
RL   J. Biol. Chem. 269:16984-16984(1994).
CC   -!- FUNCTION: Involved in chloroplast protein synthesis. It enhances the
CC       poly(A,U,G)-dependent binding of the initiator tRNA to chloroplast 30S
CC       subunits.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000305}.
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DR   EMBL; L23760; AAA20996.1; -; mRNA.
DR   PIR; A58905; A54391.
DR   AlphaFoldDB; P36177; -.
DR   SMR; P36177; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.80; -; 1.
DR   Gene3D; 3.30.110.10; -; 1.
DR   HAMAP; MF_00080; IF_3; 1.
DR   InterPro; IPR036788; T_IF-3_C_sf.
DR   InterPro; IPR036787; T_IF-3_N_sf.
DR   InterPro; IPR019813; Translation_initiation_fac3_CS.
DR   InterPro; IPR001288; Translation_initiation_fac_3.
DR   InterPro; IPR019815; Translation_initiation_fac_3_C.
DR   InterPro; IPR019814; Translation_initiation_fac_3_N.
DR   PANTHER; PTHR10938; PTHR10938; 1.
DR   Pfam; PF00707; IF3_C; 1.
DR   Pfam; PF05198; IF3_N; 1.
DR   SUPFAM; SSF54364; SSF54364; 1.
DR   SUPFAM; SSF55200; SSF55200; 1.
DR   TIGRFAMs; TIGR00168; infC; 1.
DR   PROSITE; PS00938; IF3; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Initiation factor; Plastid;
KW   Protein biosynthesis; Transit peptide.
FT   TRANSIT         1..?140
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?141..538
FT                   /note="Translation initiation factor IF-3, chloroplastic"
FT                   /id="PRO_0000014501"
FT   REGION          141..290
FT                   /note="Head"
FT   REGION          146..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..474
FT                   /note="IF-3 like"
FT   REGION          484..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..529
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  58255 MW;  F92B0881839B03E0 CRC64;
     MVRSSCLQCD QPSQGSNSTF GCGGPLAAVC ATGLLVLVLY SPSSQTANWS AQGISTKALY
     PAVPVPSTLL PGSAPAKHQL HVWRAHAMSE ATTNNSFKQS LFGYNAISSI WLQLAGVAAT
     FFAFGALMAA VTQRKEIAVF SASGQAAEPE GAEPLKRPFP SPAAKPKPLF STPANSFSNI
     FQAPPSLRTD STYGRGPRST SFTDISNWPS NNALRNPQSV IDIGGGVDFL GDRSPGNPFT
     RLRGSPSSTL SNLGMGLGLG LGKGKGFGKG FGKGRGFPVE EEVEEEQEVL SWADRRRALA
     DPDAPPMNED IKYPQLRLVR AVPGGRDEKL GVMSRQEALE LAEAEDIDLV LVSIDTDPPV
     AKLVNYSKLK YESEKKKKDS HKKGKVKEVK ELKVSHKIGQ HDYDVRVKQA RKFLEGGHRI
     KVSMEFKGRE NQFVEIGRAV MKRFQNDLAD MGKADAVPKK LGTRLILNLA PAGEALKVIA
     ERRAERDRKA AAEEEGEGDD LDFVDENEDE DVEGEGEEEE AEELEEETAE GTEVPTRS