ID A0A1Q3CEL1_CEPFO Unreviewed; 1038 AA.
AC A0A1Q3CEL1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=CFOL_v3_22134 {ECO:0000313|EMBL:GAV78669.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV78669.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) 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. {ECO:0000256|ARBA:ARBA00025162}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAV78669.1}.
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DR EMBL; BDDD01001844; GAV78669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3CEL1; -.
DR FunCoup; A0A1Q3CEL1; 980.
DR STRING; 3775.A0A1Q3CEL1; -.
DR InParanoid; A0A1Q3CEL1; -.
DR OrthoDB; 361630at2759; -.
DR Proteomes; UP000187406; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000054; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR053905; EF-G-like_DII.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF22042; EF-G_D2; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000187406}.
FT DOMAIN 509..682
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 166..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 111426 MW; 27B9F729D4E84503 CRC64;
MGSMVVLVGA MPSLAPSFVN LSVCGSTATT SSDSSSYSLV RRVPVSKPSI RGRKRWHCVS
PSSSVCRYSV TTTTDFIADP TDAVSLDSNN NTYTTNAIGD DNEIVLKPGP KPLLKSKSVA
PVLGVSPLSW DSVDDDDYDD KFDDVRERDK VIESLGEVLD KAEKLETSTS KELGSGKESW
NVNKPKSLSP IANTNSTSGS RPVDSVGTKK AKTLKSVWRK GDTVATVQRV VKESAKINSN
TVLKEESKIA GEGFVESKPS VPLRPTQPPL KPQPKLQQRP SVMPPPVMKK PVILKDVGAS
SKSSVVDETN STVKSKERTP ILIDKFASKK PVVDPLIAQA VIAPPKPARG PVPGKFRDAS
RRKNASAGGS RRRMVDEVDI DEETSELNIS IPGVARKGRK WSKASRKAAR LKAAREAAPV
KVEILEVAEK GMLIEELAYN LTISEGEILG LLYSKGIKPD GVQTLDKDMV KMICKEYEVE
VIDADPIKVE EMARKKEIFD EQDLENLEDR PPVLTIMGHV DHGKTTLLDH IRKSKVAASE
AGGITQGIGA YKVLVPVDGK LQSCVFLDTP GHEAFGAMRA RGARVTDIAI IVVAADDGIR
PQTNEAIAHA KAAGVPIVIA INKIDKDGAN PERVMQELSS IGLMPEDWGG DIPMVQISAL
KGENVDDLLE TVMLVAELQD LKANPHRNAK GTVIEAGLQK SRGPVATFIV QNGTLKIGDI
VVCGEAFGKV RALFDEGGNR VDKAGPSIPV QVIGLNNVPI AGDEFEVVLS LDVAREKAEA
RAESLRDDRI SAKAGDGMIT LSSLASAVSS GRHSGLDLHQ LNIILKVDLQ GSIEAVRQAL
QVLPQDNVTL KFLLQSAGDV SASDVDLAVA GKALILGFNV KTPGSVKSYA DNKGVEIRLY
KVIYELIDDV RNAMEGLLEP VEEQVKIGSA EVRAIFSSGS SRVAGCMVTE GKVMKGCGVR
VIRNGKLVYV GILDSLRRVK EIVNEVNAGL ECGIGIKDYK DSEEGDILEV FNRVQKKRTL
EEASASMAAA REGVGMEL
//
