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Database: UniProt
Entry: G0UPX2_TRYCI
LinkDB: G0UPX2_TRYCI
Original site: G0UPX2_TRYCI 
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
//
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