GUF1_PARBP
ID GUF1_PARBP Reviewed; 658 AA.
AC C0SHD5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Translation factor GUF1, 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 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137};
DE Flags: Precursor;
GN Name=GUF1 {ECO:0000255|HAMAP-Rule:MF_03137}; ORFNames=PABG_07090;
OS Paracoccidioides brasiliensis (strain Pb03).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=482561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb03;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN305545; EEH17003.1; -; Genomic_DNA.
DR AlphaFoldDB; C0SHD5; -.
DR SMR; C0SHD5; -.
DR PRIDE; C0SHD5; -.
DR EnsemblFungi; EEH17003; EEH17003; PABG_07090.
DR VEuPathDB; FungiDB:PABG_07090; -.
DR HOGENOM; CLU_009995_3_1_1; -.
DR InParanoid; C0SHD5; -.
DR Proteomes; UP000002740; 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; IPR031157; G_TR_CS.
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; 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 Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 41..658
FT /note="Translation factor GUF1, mitochondrial"
FT /id="PRO_0000402896"
FT DOMAIN 60..240
FT /note="tr-type G"
FT BINDING 69..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 133..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 187..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 658 AA; 73404 MW; F51F4F2EDB43D65A CRC64;
MRGCLQTVRW LTSAWQRPPS YPPLSRAAPC RFFNVSIPRN AQSRKPVSDL ERRIAAIPID
RFRNFCIVAH VDHGKSTLSD RLLELTGTIQ PGGNKQVLDK LDVERERGIT VKAQTCTMLY
NYRGEDYLLH LVDTPGHVDF RAEVSRSYAS CGGALLLVDA SQGVQAQTVA NFYLAFAEGL
KLVPVINKVD LPSADPVRAL DQMANTFELD PKTAVLVSAK TGLNVEQLLP TVVEQIPAPV
GDHTKPLRML LVDSWYSTYK GVILLVRIFD GEVRAGDHVG SLATGLKYHV GEVGIMYPGQ
TAQSVLRAGQ VGYIYFNPAM KRSQEAKVGD TYTKVGSEKL IEPLPGFEEP KSMVFVAAYP
VDASDFPHLE DSINQLLLND RSITLQKESS EALGAGFRLG FLGTLHCSVF EDRLRQEHGA
SIIITPPTVP FKVIWKDGKE EIITNPALFP EEDALRAKVV ELQEPFVLAT LTFPEEYLGR
VIELCESNRG EQKSLEFFTA TQVILKYELP LAQLVDDFFG KLKGSTKGYA SLDYEESGWR
RSSIAKLQLL VNKVPVDAVS RVVHSSQVQK LGRVWVSKFK EHVDRQMFEV VIQAAVGRNI
VARETIKPFR KDVLQKLHAA DVTRRRKLLE KQKEGRKKLK AVGNVVIEHK AFQAFLAK
