ID   GUF11_TRYCC             Reviewed;         748 AA.
AC   Q4DKF7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation factor GUF1 homolog 1, mitochondrial;
DE            EC=3.6.5.-;
DE   AltName: Full=Elongation factor 4 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03137};
DE            Short=EF-4 1 {ECO:0000255|HAMAP-Rule:MF_03137};
DE   AltName: Full=GTPase GUF1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03137};
DE   AltName: Full=Ribosomal back-translocase 1 {ECO:0000255|HAMAP-Rule:MF_03137};
DE   Flags: Precursor;
GN   ORFNames=Tc00.1047053503697.90;
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener;
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., 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: Promotes mitochondrial protein synthesis. May act as a
CC       fidelity factor of the translation reaction, by catalyzing a one-codon
CC       backward translocation of tRNAs on improperly translocated ribosomes.
CC       Binds to mitochondrial ribosomes in a GTP-dependent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_03137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03137};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. LepA subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAHK01000385; EAN93010.1; -; Genomic_DNA.
DR   RefSeq; XP_814861.1; XM_809768.1.
DR   AlphaFoldDB; Q4DKF7; -.
DR   SMR; Q4DKF7; -.
DR   STRING; 5693.XP_814861.1; -.
DR   PaxDb; Q4DKF7; -.
DR   EnsemblProtists; EAN93010; EAN93010; Tc00.1047053503697.90.
DR   GeneID; 3546474; -.
DR   KEGG; tcr:503697.90; -.
DR   eggNOG; KOG0462; Eukaryota.
DR   OMA; HIDFNHE; -.
DR   OrthoDB; 165663at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd03709; lepA_C; 1.
DR   Gene3D; 3.30.70.2570; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00071; LepA; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   InterPro; IPR035654; LepA_IV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43512; PTHR43512; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT   CHAIN           30..748
FT                   /note="Translation factor GUF1 homolog 1, mitochondrial"
FT                   /id="PRO_0000402861"
FT   DOMAIN          94..276
FT                   /note="tr-type G"
FT   BINDING         103..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT   BINDING         167..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT   BINDING         221..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ   SEQUENCE   748 AA;  82466 MW;  5BCABB6D4C7B65D9 CRC64;
     MRVGCCLLLK PIRQRLCTAS ISSRHIMRWC ATSSSNINST ETAAKMPDDD VSGSLSAPSL
     LKYKIEPSTA TMGAPRPPHD DDRAFCTLAS FPPSHIRNFA VVAHVDHGKT TLSDAILRRT
     GVLSGSQVGT YTDRLLVERE RGITIKAQTC SIFVVRDGEE FLLNLIDTPG HVDFQYEVSR
     SLSASDAALL LVDAAQGIEA QTMAHFHMAL DRGLTILPVL TKMDAVLSDA PVDRALQDLE
     DSTGLLRREV LFTSAKEQVG IEALLHAIIE RVPPPTGLLG LSDLQQLPPL LPGSAERAAM
     EEKMVPLRAL LFDSWTSECG GGLRRPAPRG GEKVNSGNDN DSNLICLVRI IDGTLTAKTV
     VTFYQSQRRC EALEVGIIHP ELRPTAALTA GMVGYVVFSR VRGEEFFVGE TLYTLPTRKF
     AREDIVPVPG FRRVQPVVFA GFYPDEGEYI TQLREAVEKL RVNEPAVTME PLDCPALGSG
     LQLGFLGMLH MQVFQERLLA EFGQRVLVTP PLVQYKYREA GSDEEEPLKP LTVHTWKWIH
     EGAACYLEPY VTATIITRRE HFQAIDSEAL RRFRGEQLDM RVLDDARVLV RYKMPLADLA
     RGFFAVVKSL SHGYASLDYG DPVYEEADLV KVDVLVQKSR ISALSVICPR SEAPSIGKRI
     VSSLKSNLTR TAVDIPLQAM VGSKIVARET VKAYRKDVTA KIHAGDISRK QKKWNDQKKG
     KERMARRTVG AVTLDQSILA AAMGAISL