ID G0UPX2_TRYCI Unreviewed; 770 AA.
AC G0UPX2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Putative translation initiation factor IF-2 {ECO:0000313|EMBL:CCC91433.1};
GN ORFNames=TCIL3000_7_2430 {ECO:0000313|EMBL:CCC91433.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC91433.1};
RN [1] {ECO:0000313|EMBL:CCC91433.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC91433.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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; HE575320; CCC91433.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UPX2; -.
DR VEuPathDB; TriTrypDB:TcIL3000_7_2430; -.
DR OrthoDB; 169393at2759; -.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
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:CCC91433.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 200..372
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 84869 MW; E1397D36E69036F7 CRC64;
MKVGLSVRAW RGAAVWGASG LSLIAFPSMH CANVARRWQS QSSRGQPGVQ WQDGVVDPRY
SSAGNMRRFN PDTAAHYVKA TIQNDRREMG LGEVHDWHEF AKDAVYIPTR SGPLWVGSDD
PRCAKFMRRR AKMQKTPQQK ARPKPGPDPA KALEDHPLRE YFTTETNLRD PLSTANNLHR
AGLIREYDIK FTAAKVKYVA RPPVVSIMGH VDHGKTTLLD HLRKTNVASS EAGGITQNVG
AFQVKVPGDK FITFIDTPGH AAFTTMREAG AAANDLIILV VSAVDGVQLQ TKEVIGLAHK
LGIPFVVACT KIDRQSNVED VKRQLRNCNV ELEEDGGDVQ FVPVCARDGR GVPELLDAVA
LQAELCEIST PEPSRCEVTV IETNGMSSTS EVTGIVRCGK VRPGQVLVAG MTYGVVRKVM
DEHGHIVQEA GPSKPVVLHG FRVHPKPGSV LMQVSSESHA QKFYHFMKEV YDTEGKREEY
LQLLNQEQHG MMYARKPDNN LVRAYSTQAF VLSCKAATFG MLQALMKSIY ELPRLEGVST
EIKVTEVGGL RDYDVALIGS SGQPGCILLY GDCKDANTLD VPNHIKVIRF NVLYHGLEAL
KEAFVSALPK VTKVRVTAEA ECLQVFRASQ AGKNGNAGGM RVIKGTIIAS HLTFRVLRKR
PKVKDDHDGG EEGNDATIKE GFAVAYEGQV KELRRFKDLV PSVEPGLECG VIMQDEFQFR
TGDILQQYEV YDEPRDVAEE YEKAELREKI MHDAAAAEAS KEAAEVSEVA
//