ID B1X3N8_PAUCH Unreviewed; 1274 AA.
AC B1X3N8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN Name=infB {ECO:0000313|EMBL:ACB42557.1};
GN OrderedLocusNames=PCC_0105 {ECO:0000313|EMBL:ACB42557.1};
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore {ECO:0000313|EMBL:ACB42557.1}.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717 {ECO:0000313|EMBL:ACB42557.1};
RN [1] {ECO:0000313|EMBL:ACB42557.1}
RP NUCLEOTIDE SEQUENCE.
RA Gloeckner G., Nowack E., Melkonian M.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB42557.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(2008).
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; CP000815; ACB42557.1; -; Genomic_DNA.
DR RefSeq; YP_002048767.1; NC_011087.1.
DR AlphaFoldDB; B1X3N8; -.
DR GeneID; 6481425; -.
DR GO; GO:0009536; C:plastid; 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; 1.10.10.2480; -; 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; 2.
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 ECO:0000313|EMBL:ACB42557.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000313|EMBL:ACB42557.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 766..938
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 159..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 137647 MW; E62FEFA88F4CB2CF CRC64;
MTSTGKVRIY ELSRDLGLEN KDVLDAAEKL SIPAKSHSSS ISEVEAAKIR DLVRNDQTNL
SLERPATDSF NLTLPKHILA TPIKPIVSTL GKVNTSLPIT NKFLSKSASS AVRPMSIPLK
PLTNKPNASV QQPSEPQIIK DNSVKTIKAT APVARPTLIP LKPLTNKPNL PVQQPNGPQI
NQDDSIKAVS SPLKPTAPVT RPTPIKPLTN KPNPPIQQLN GPQITQDDSI KAANSKSTAP
VIRATPTTVK PILEKNTVSP RPGIFSKVEV IQKNPKKTIS SPSKPTAPVL RPSSIKVLID
KPDLPDDVID KQDVTQKSQI KSSVVKLTPP AFRPNTPNKP EIVQKAPVKL AAPVPRPVNT
PIISNDQRSV QVCDDSLKST GVTPSRRPVI PPPQRINPIG SKLNLTEGTK QQLVNRPQSH
KSGAPNSKAG NNSPPISRPS LNIQQKSTLK HPDTANAVNA NNRPTVNTLE LVGKPIRRDS
TSKRPPVEAP KRQSNAGQGM RKPMAPGELM QLQKPGSRST APPPRRADGS IAGVNSNSEI
KAIPPGPRPT AMPPSAPRRP GFRNPAPGGG TRRPSRPDWD DSAKLEALRS KTPQKQRKKV
HIIGDNDDPL TTQTGGYAGE QDAVVLQASL ARPSKPKIQK QGGTAKPIVA MRKRKKETTR
QRQRRRAMEL RASREAKQAR PDMLIVPEGN LTVQELADKL GTESSEIIKS LFFKGIIATV
TQTLDLSTIE TVSEEFGVPV LEDDVEEAAK KTVEMIEESD FKHLIRRPPV VTVMGHVDHG
KTSLLDAIRK TRVAAGEAGG ITQHIGAYQI EVTHSDQQRK ITFLDTPGHE AFTAMRARGA
KVTDVAVLVV AADDGVRPQT LEAISHARAA EVPIIVAINK IDKEGAQIDR VKQELSDQNL
LAEEWGGNTV MVPVSAIRGE NIDKLLEMIL LVTEVEDLQA NPDRMAKGTV IEAHLDKAKG
PVATLLIQNG TLRAGDVVAA GPILGKVRAM MDHAGKRVKE AGPSCAVEAL GFSEVPTAGD
EFEVYLDEKA ARAVVGERAN EARATRLAQQ MASRRVSLAT MSGQASEGEL KELNLILKAD
VQGSVEAILG ALEQLPKDEV QVRVLLSAPG EITETDVDLA AASGAVIIGF NTSMASGAKR
AADTNGVDVR EYDVIYKLLE DIQMAMEGLL EPESVEETLG EAEVRAVFSI GKSAVAGCYV
LSGKIQRNTK IRVRRGKQLI FEGDLNSLRR NKDDIKEVAT GFECGIGCDR FANWEDGDRI
EVYKMVTQRR TLNI
//
