ID Q4DX02_TRYCC Unreviewed; 778 AA.
AC Q4DX02;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=Tc00.1047053510533.120 {ECO:0000313|EMBL:EAN97056.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN97056.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN97056.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN97056.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN97056.1}.
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DR EMBL; AAHK01000117; EAN97056.1; -; Genomic_DNA.
DR RefSeq; XP_818907.1; XM_813814.1.
DR AlphaFoldDB; Q4DX02; -.
DR SMR; Q4DX02; -.
DR STRING; 353153.Q4DX02; -.
DR PaxDb; 353153-Q4DX02; -.
DR EnsemblProtists; EAN97056; EAN97056; Tc00.1047053510533.120.
DR GeneID; 3551253; -.
DR KEGG; tcr:510533.120; -.
DR eggNOG; KOG1145; Eukaryota.
DR InParanoid; Q4DX02; -.
DR OMA; DHPLREY; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
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 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 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:SF20; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EAN97056.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT DOMAIN 198..370
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 85855 MW; FD33EC1985D5A2C6 CRC64;
MWRLSSGVRQ LAVSWIGASC GCGAASAMAQ TTVRRWQSQS SRGQPGLHWD EGVVDPRYSS
EGNMRRFNPD TVAHYVKATI QNDRREMGLG EVYDWHEFAK DAVYIPTRSG PLWVGSDDPR
CAKFMRRREK MKKSPQQKAR PKPGPDPAKQ LEDHTLREFF TTATNLRDPL STANNLHRAG
LIREYDIKHV AAKIQYVPRP PIVSIMGHVD HGKTTLLDYL RNTNVASEEA GGITQNVGAF
QVKISDGHFV TFIDTPGHAA FTAMREVGVA ANDLIVLVVS AVDGVQPQTK EVIGLARDAG
IALVVACTKI DRQPKVDPIK QQLRDCGVEL EEDGGDTQFV SVCGRDGTGI PELLEAISLQ
AELCEISTPE PSRCEVTVIE SRSSDVKNEV AGIVRCGKLK PGQVLVAGMT YGVVRKVMDN
NGNVLQEAGP SMPVIMQGFR VHPKPGVVLM QVSSESHAQK YYLFMKDVYK VEGRREDYLQ
LLNQEQHGMI YARKPDNNLV RTYSTKAFVL SCKAATFGML QALMKTLYEL PRLEGVSTEI
KVTEVGGLKD YDIALIGSSG QPGCILLYGE SKDTNTLDVP NHVKVIRFNV LYHGIDALKE
TLVESLPKIS KTRVTAEAEC IQVFRASQAG RNGNAGGMRV TKGSIIGSHL TFRVLRKSSR
SKLTGGDNSP KKATGDEDDT EDARTVVYEG QIKELRRFKE IVPSVEMGLE CGVILHDEFQ
FRLGDILQQF EVYEEPRDVA EEYEAAERRE KIMRETAALQ AQMEEEKAGG NADGAGTV
//
