ID A0A0D9XD69_9ORYZ Unreviewed; 901 AA.
AC A0A0D9XD69;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR09G05730.3, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR09G05730.3, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR09G05730.3, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR09G05730.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D9XD69; -.
DR EnsemblPlants; LPERR09G05730.3; LPERR09G05730.3; LPERR09G05730.
DR Gramene; LPERR09G05730.3; LPERR09G05730.3; LPERR09G05730.
DR Proteomes; UP000032180; Chromosome 9.
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; 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 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:UP000032180}.
FT DOMAIN 405..623
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 11..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 96513 MW; 6245B8056DC8F471 CRC64;
MVITNLINEK GVQFSSSSSS SRVSVSVKPD DENDLLLKPP QKPVLRPNGL PSPERSMNAA
ASPSSGGGRP VLEDRDKVRE SLDEVLEKAE KLNASTSGNG NGDGSSSGGL RRQNGAYKPD
NSSATAAASA EGVNSRKTKT LKSVWRKGNP VSTVHKVVRD HPRSESRNQS TVSAAKPSIP
PPTQPGPQLL SKPSVAPPPR RPVKPDISKE KKGPILIDKF ASSNRPVVDP AVAAALLEPV
KPVRGPPTKV RDDRRKKLST PAGTRRRQTN DDRLADEDTA DVPISGVPVR KGRRWNKAKR
RAARLQLEAS LVEEPVRVEI LEVGEEGMLI EDLAYELAIG ESEILRFLSV RGVMLDNVQR
LDKDLVKMVC MEYDVEVLES GPVKVEEMAK KKEFLDEEDL DKLEARPPIV TIMGHVDHGK
TTLLDYIRKS KVVASEAGGI TQGIGAYHVL VPVYGKPQTC VFLDTPGHEA FGAMRARGAR
VTDICIVVVA ADDGVRPQTN EAIAHAKAAG VPIVIAINKI SALSGEGVDE LLETAVLVAE
LQELKANPHR NAKGTVIEAC LDKAKGPLAT LVVQNGTLNR GDIVVCGEAF GKIRAMYDDG
GMLIDKAGPS NAVQVIGLNN VPLAGDEFES VDNLDVARER ANARADAMRI ERISAKAGEG
KVTLSSIAAS VSSGKQVGID THELNVILKV DFQGSIEAIR QAIQVLPQEN VSLRVLLQAP
GDVSVSDIDL AVASEGIIFG FNVKAPGSVK TYAKKKSVEI RLYKVIYDLI DDLRNAMEGL
LEPAEDEVPL GSAKVRAVFS SGSGKVAGCM ITTGKVVQDC KVRVLRKGKE VYVGTLDSLR
RVKETVKEVG AGLECGIGVD DFDEWEEGDV VEAFNTVKKT RTLEEASASM TAALKDAGVQ
L
//
