GUF12_TRYCC
ID GUF12_TRYCC Reviewed; 748 AA.
AC Q4DZ91;
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 2, mitochondrial;
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03137};
DE Short=EF-4 2 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=GTPase GUF1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase 2 {ECO:0000255|HAMAP-Rule:MF_03137};
DE Flags: Precursor;
GN ORFNames=Tc00.1047053504105.210;
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}.
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DR EMBL; AAHK01000081; EAN97856.1; -; Genomic_DNA.
DR RefSeq; XP_819707.1; XM_814614.1.
DR AlphaFoldDB; Q4DZ91; -.
DR SMR; Q4DZ91; -.
DR STRING; 5693.XP_819707.1; -.
DR PaxDb; Q4DZ91; -.
DR EnsemblProtists; EAN97856; EAN97856; Tc00.1047053504105.210.
DR GeneID; 3552196; -.
DR KEGG; tcr:504105.210; -.
DR eggNOG; KOG0462; Eukaryota.
DR OMA; MVQIAIQ; -.
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 2, mitochondrial"
FT /id="PRO_0000402862"
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; 82482 MW; 68B849FF7CEEFB29 CRC64;
MRVGCCLLLK PLRQRLCTAS ISSRHIMRWC ATSSSNINST ETAAKMPDDD VSGSLSAPSL
LKYKIEPSTA TMGAPRPPHD DDRAFCTLAS FPPSHIRNVA VVAHVDHGKT TLSDAILRRT
GVLSGSQVGT YTDRLLVERE RGITIKAQTC SIFVVWDGEE FLLNLIDTPG HVDFQYEVSR
SLSASDAALL LVDAAQGIEA QTMAHFHMAL DRGLTILPVL TKMDAVLSDA PVDRALQDLE
DSTGLLRREV LFTSAKEQLG IEALLHAIIE RVPPPTGLLG LSDLQQLPPL LPGSAERVAM
EEKMVPLRAL LFDSWTSECG GGLRRPAPRG GEKVNSGNDN DRNLICLVRI IDGTLTAKTV
VTFYQSQRRC EALEVGIIHP ELRPTAALTA GMVGYVVFSQ VRGEEFLVGE TLYTLPTRKF
ARENIVPVPG FRRVQPVVFA GFYPDEGEYI TQLREAVEKL RVNEPAVTME PLDCPALGSG
LQLGFLGMLH MQVFQERLLA EFGQRVLVTP PLVQYKYREA GSDEEEPLKP LTVHTWKWIH
EGAACYLEPY VTATIITRRE HFQAIDGEAL RRFRGEQLDM RVLDDARVLV RYKMPLADLA
RGFFAVVKSL SHGYASLDYG DPVYEEADLV KVDVLVQKSR ISALSVICLR SEAPSIGKRI
VSSLKSNLTR TAVDIPLQAM VGSKIVARET VKAYRKDVTA KIHAGDISRK QKKWNDQKKG
KERMARRTVG AVTLDQSILA AAMGAISL
