ID A0A8X7SFS0_BRACI Unreviewed; 1027 AA.
AC A0A8X7SFS0;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=Bca52824_034039 {ECO:0000313|EMBL:KAG2305388.1};
OS Brassica carinata (Ethiopian mustard) (Abyssinian cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=52824 {ECO:0000313|EMBL:KAG2305388.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2305388.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2305388.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2305388.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) 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:KAG2305388.1}.
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DR EMBL; JAAMPC010000007; KAG2305388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8X7SFS0; -.
DR OrthoDB; 361630at2759; -.
DR Proteomes; UP000886595; 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:UP000886595};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1027
FT /note="Translation initiation factor IF-2, chloroplastic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036465854"
FT DOMAIN 500..673
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..182
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..259
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..346
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 109495 MW; 74C4E923C2D88E2F CRC64;
MPSMLVLVGT VPSLVSLVSP GGGSVSGTSL SYGSYALVKR VSLSRRSVVK GSSSKRWLCR
YSVSSSATTS STSTDFIAEA NGNSVSIDSN SFKGDDDSSE IVLKQAPKPV LKPPVARVER
GSSAPWSKEL SNGVKFDGEE ERNKVIESLG EVLDKAESLE IPKPGNKEGV KPSQPSASSS
DSRNGAFASG GGTRKTKTMK SVWRKGDAVA AVEKVVKEEP KIDSRGRQGD GTQLSPPQRP
PLRPQPPLRA QPQLQGKPMV GPPPVKKPIL KDLGMSSKPS GPILKDVGMA SKPPVSEEVD
SSSTKSKERK PILVDKFASK KKGADPAASQ AVLAPTKPGK GPPSSKFRVE HRNKKNASAN
PRRRMVAEDD ADEDASELNV SIPGSGRKGR KWSKASRKAA RLQAARDAAP VKAEILEVEE
EGMSIEDLAY NLAIGEGDIL GYLYSKGIRP DGVQTLDREM VRMICKDYDV EVLDADSVQV
EEMAKKKEIF DEEDLDKLED RPPVITIMGH VDHGKTTLLD YIRKSKVAAS EAGGITQGIG
AYKVSVPVDG EVQSCVFLDT PGHEAFGAMR ARGARVTDIA IIVVAADDGI RPQTNEAIAH
AKAAGVPIVI AINKIDKDGA SPERVMQELS SIGLMPEDWG GDVPMVQISA LKGENIDDLL
ETVMLVAELQ ELKANPHRNA KGIVIEAGLD KAKGPFATFI VQKGTLKRGD VVVCGEAFGK
VRALFDHSGE RVDEAGPSIP VQVIGLNNVP IAGDEFEIVS SLDVAREMAE ARAVSLRDER
ISAKAGDGKV TLSSLASAVS AKKMSGLDLH QLNIILKVDV QGSIEAVRQA LQVLPQENVT
LKFLLQATGD VSNSDVDLAS ASEAIIFGFN VKASGSVKKA AENKGVEIRL YRVIYELIDD
VRNAMEGLLE SVEEQIPIGS AEVRATFSSG SGRVAGCMVN EGKFVKDCGI RVIRKGKTVH
VGVLDSLKRV KENVKEVSAG LECGIGMDDY DDWIEGDTIE AFNAVQKRRT LEEASASMSA
AIEEAGV
//
