IF2C_PHAVU
ID IF2C_PHAVU Reviewed; 1012 AA.
AC P57997;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic;
DE AltName: Full=PvIF2cp;
DE Flags: Precursor;
GN Name=IF2CP;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11356831; DOI=10.1074/jbc.m100605200;
RA Campos F., Garcia-Gomez B.I., Solorzano R.M., Salazar E., Estevez J.,
RA Leon P., Alvarez-Buylla E.R., Covarrubias A.A.;
RT "A cDNA for nuclear-encoded chloroplast translational initiation factor 2
RT from a higher plant is able to complement an infB Escherichia coli null
RT mutant.";
RL J. Biol. Chem. 276:28388-28394(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By light.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF324244; AAK09431.1; -; Genomic_DNA.
DR STRING; 3885.XP_007149252.1; -.
DR PRIDE; P57997; -.
DR eggNOG; KOG1145; Eukaryota.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; GTP-binding; Initiation factor; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..1012
FT /note="Translation initiation factor IF-2, chloroplastic"
FT /id="PRO_0000014478"
FT DOMAIN 488..661
FT /note="tr-type G"
FT REGION 75..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..504
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 522..526
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 601..604
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 637..639
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 547..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 601..604
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1012 AA; 108791 MW; 33A639712A30D07C CRC64;
MLILVGSKQG TMSSLASPVS LGSLMGVSSS GRSHSGVRRV SFSRGNCKGR KRWHCLSLSV
CRYSVTTTDF IADQGNSVSL DSNSNSSSSS KSGGDDGTGF VLKPPPKPVL KAPDNRMTHL
GPSRTTGDVE ERNKVIESLG EVLEKAEKLG SSKVNGDKNN GSVNKPVRNN ANASPRTERP
VNSAASLKSK TLKSVWRKGD SVASVQKVVK EVPKPSYNKN EEEKSQTRGG EKVVSQTRAP
QPPSKPQPLK PQQPSKPQPA LLSKPSIAPP PVKKPVVLRD KGAAETSVKS KEKKSPILID
KFASKKPVVD PLIAQAVLAP PKPGKAPSPG KFKDDFRKKG ALAGGGRRRR ILDDEDVIQD
ASELNVSIPG AATARKGRKW SKASRKAARL QAARDAAPVK VEILEVGDSG MLVEELAYCL
ATSEGEILGY LYSKGIKPDG VQTIDKDMVK MICKEYDVEV IDADPVKVEG LVKKREILDE
DDLDKLKDRP PVITIMGHVD HGKTTLLDYI RKSKVAASEA GGITQGIGAY KVQVPFDGKT
LPCVFLDTPG HEAFGAMRAR GASVTDIAVI VVAADDGIRS QTNEAIAHAK AAGVPIVIAI
NKIDKDGANP ERVMQELSSI GLMPEDWGGN TPMVPISALK GKNVDDLLET VMLVAELQEL
KANPDRSAKG TVIEAGLDKS KGPLATFIVQ NGSLRRGDIV VCWRSFWKGR ALFDDGGKRV
DEATPSIPVQ VIGLNNVPIA GDVFEVVESL DAARERAETR AESLRNERIS AKAGDGKITL
SSLASAVSSG KLSGLDLHQL NIILKVDLQG SIEAVRKALQ VLPQENVTLK FLLEATGDVN
TSDVDLAVAS KAIIMGFNAX TPGSVKSYAD NKAVEIRLYR VIYELIDDVR KAMEGLLEPV
EEQLTIGSAV VRAVFSSGSG RVAGCMVTEG KVLKDCGIRV KRKGKIVHVG IIDSLRRVKE
IVKEVNAGLE CGLGLEDFDD WEEGDIIEPS TQLRRRGPLK RPQHQWQLLW RE
