ID A0A067DZF7_CITSI Unreviewed; 996 AA.
AC A0A067DZF7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=CISIN_1g0017452mg {ECO:0000313|EMBL:KDO44387.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO44387.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO44387.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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}.
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DR EMBL; KK785307; KDO44387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067DZF7; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; cd03692; mtIF2_IVc; 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; 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 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; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 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:UP000027120};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..996
FT /note="Translation initiation factor IF-2, chloroplastic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001635941"
FT DOMAIN 489..662
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 82..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 106417 MW; 96028F6C69C327BB CRC64;
MLVLVGTMPS LASLVSLGSI SVTGTTSCCS ESSCCSLVKR VSLTKRNFKG KKRWVCKYSV
TTQTTTTTTD FIEQGNGSAV SFDSNTFRGR NSDNDSDGDD NGIVLKPAPR PVLKSLGVKG
GASVSGVNSM GWDPSRVGED SDEEERNKVI ESLDEVLEKA EKLETRNESG NVSVNKATLP
NVSADTKNGR PMNSVGAKKS KTLKSVWKKG DSVASIQKVV KETPKTKVKK EEPKMGGDMK
MESQLNIPPR PVQPPLRPQP KLQTKPSVAS TPVIKKPVVL KDVGAGQKLS TIGEADSAVK
NKERKPILID KFASKKPAVD PLISQAVLAP TKPGKGPAGK FKDDYRKKGG PRKRIVDDDD
EIPDEEASEL IPGAARKGRK WTKASRKAAK LKAAKDAAPV KVEILEVGEK GMLIEELARN
LAIGEGEILG SLYSKGIKPE GVQTLDKDMV KMICKDYEVE VLDADPVKME EMARKKDLFD
EEDLDKLEDR PPVLTIMGHV DHGKTTLLDH IRKTKVAAAE AGGITQGIGA YKVQVPVDGK
LQPCVFLDTP GHEAFGAMRA RGARVTDIAV IVVAADDGIR PQTNEAIAHA KAAGVPIVIA
INKIDKDGAN PERVMQELSS IGLMPEDWGG DIPMVQISAL KGEKVDDLLE TIMLVAELQE
LKANPHRNAK GTVIEAGLHK SKGPVATFIL QNGTLKKGDV VVCGEAFGKI IGLNGVPIAG
DEFEVVDSLD VAREKAEARA FSLRNERISA KAGDGKVTLS SLASAVSAGK LSGLDLHQLN
VIMKVDVQGS IEAVRQALQV LPQDNVTLKF LLQATGDISA SDVDLAVASK AIILGFNVKA
PGSVKTYADN KGVEIRLYRV IYDLIDDMRN AMEGLLETVE EQVPIGSAEV RAIFSSGSGR
VAGCMVSEGK LVKGCGIRVI RDGKTVHVGV LDSLRRVKEN VKEVNAGLEC GVGAADYDDL
EEGDIIEAFN SIQRKRTLEE ASASMASALE GAGIEL
//
