GUF1_BABBO
ID GUF1_BABBO Reviewed; 705 AA.
AC A7AQ93;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation factor GUF1 homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03137};
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03137};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137};
DE Flags: Precursor;
GN ORFNames=BBOV_III011750;
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo;
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
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; AAXT01000001; EDO08727.1; -; Genomic_DNA.
DR RefSeq; XP_001612295.1; XM_001612245.1.
DR AlphaFoldDB; A7AQ93; -.
DR SMR; A7AQ93; -.
DR STRING; 5865.XP_001612295.1; -.
DR EnsemblProtists; EDO08727; EDO08727; BBOV_III011750.
DR GeneID; 5480555; -.
DR KEGG; bbo:BBOV_III011750; -.
DR VEuPathDB; PiroplasmaDB:BBOV_III011750; -.
DR eggNOG; KOG0462; Eukaryota.
DR InParanoid; A7AQ93; -.
DR OMA; HIDFNHE; -.
DR Proteomes; UP000002173; Partially assembled 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 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; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
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; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 1.
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..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 21..705
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402851"
FT DOMAIN 105..288
FT /note="tr-type G"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 181..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 235..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 705 AA; 78001 MW; FA93B0F0F8393E4A CRC64;
MVCHRYLLGL GASTLCLRRL AQYPSTEYHG IASRHRSPGY YAYILGNFNI SNEEQLFSSV
HSLANNDSDV LPVEDNGTTN LTGTGEATSE TGKEEEVVNE PYNGNRMRNF CIIAHVDHGK
STLADRFLEL TKAVEPHEIQ GQYLDNMELE RERGITIKLQ SALIKYTYPK DGQVYSLNLI
DTPGHIDFNH EARRSIAACE GAILVVDGTK GIQAQTVTTS MIAIEAGLKL IPVVNKIDVP
FCDYESTVAD LTSLFDFSED EILMASAKEG FGINEILDAV VERIPPPKIN LDRPFRALVF
DSQYDPHRGV VSYVRVSDGI IKKLDDVVFL GHNLESRITA VGVMMPELRE RDVLRSGEVG
WLCSNTKDPS KVAVGDTVAL KSAVKDNNVE PLVAFAPAKP SVFAGLYPCD GSDYMRLSVA
LEKLKLNDHS IVFEPSESSI AGHGFKCGFN GLLHLDVTVQ RLQREFDVGV IVTSPSVPYK
CILKNGKEIT VSDAAHWPEE GMVKVSMEPW TNVTVRIPGD CHKKVSNLLT QMRGEFQKKS
EFAGGKSLVL EYKVPMIEII STFFDNLKSM TNGFGSFDYE GTEYREIDLC KLRVLINGEE
AGGLSMLVAR DNAYKSGRLL VETLREVIPP KQFKINLQAA IGKRVIAALS IPALRKNVTE
RCSGGDPSRK RKLLENQAKG KKYMAEIGNV SIPFDAYKAV HKALR
