ID A0A0B2R6J7_GLYSO Unreviewed; 1020 AA.
AC A0A0B2R6J7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=glysoja_025564 {ECO:0000313|EMBL:KHN27759.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN27759.1};
RN [1] {ECO:0000313|EMBL:KHN27759.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN27759.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-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; KN653085; KHN27759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2R6J7; -.
DR Proteomes; UP000053555; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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 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; 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 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 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 Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KHN27759.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 486..664
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 74..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 750..777
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 108912 MW; AFC3908D2B1FE224 CRC64;
MLILVGNVQG TMSSLASPVS LGSLMGVSSS GRAHSMVRRV SLSRGNCRGR KRWHCVSLSV
CRYSVTTTDF VADQGNSVSL DSNSSSSSSK GGDDGAGFVL KPPPKPVLKS PENKSDPILG
PSRTIGDPGD VEEKNKVIES LGEVLEKAEK LGSSKVNGER NNGSMNKPVR SNADASPRAD
KLVNSAAYQK SKTMKSVWRK GDTVASVQKV VKEVPKPNSN KNEGEKTQTR GGEEVVSQTR
APQLPLKPQP PSQPQPALLS KPSIAPPPVK KPVVLRDKGV SETTSVKPKE KKSPILIDKF
ASKKPVVDPL IAQAVLAPPK PGKGPPPGKF KDDFRKKGAT TGGPRRRILE DDVIHDEDAS
ELNVSIPGAA TARKGRKWSK ASRRAARLQA ARDAAPVKVE ILEVGDKGML VEELAYCLAT
SEGEILGYLY SKGIKPDGVQ TIDKDMVKMI CKEYDVEVID ADPFKVEGLV KKKEILDKDD
LDKLKDRPPV ITIMGHVDHG KTTLLDYIRK SKVAASEAGG ITQGIGAYKV EVPVDGKNLP
CVFLDTPGHE AFGAMRARGA SVTDIAIIVV AADDGIRPQT NEAIAHAKAA GVPIIIAINK
ACQHEIDKDG ANPERVMQEL SSIGLMPEDW GGDIPMVPIS ALKGKNIDDL LETVMLVAEL
QELKANPDRS AKGTVVEAGL DKSKGPFASF IVQNGTLRRG DIVVCGEAFG KVRALFDDGG
KRVDEATPSI PVQVIGLNNV PIAGDEFEVI ESLDTARERA ETRAESLRNE RISAKAGDGK
VTLSSLASAV SSGKLSGLDL HQLNIILKVD LQGSIEAVRK ALEILPQDNV TLKFLLEATG
DVSTSDVDLA VASKAIILGF NVKAPGSVKS YAENKAVEIR LYKVIYELID DVRNAMEGLL
EPVEEHVTIG SAVVRAVFSS GSGRVAGCMV TEGKILQDCG IRVKRKGKVV HVGILDSLRR
VKEIVKEVNA GLECGLGLED FDDWEEGDIL EVFNTVQKRR TLEEASASMA AAVEGVGVAL
//
