GUF1_TALMQ
ID GUF1_TALMQ Reviewed; 663 AA.
AC B6QW35;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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; ORFNames=PMAA_014420;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995906; EEA19182.1; -; Genomic_DNA.
DR RefSeq; XP_002153567.1; XM_002153531.1.
DR AlphaFoldDB; B6QW35; -.
DR SMR; B6QW35; -.
DR STRING; 441960.B6QW35; -.
DR EnsemblFungi; EEA19182; EEA19182; PMAA_014420.
DR GeneID; 7030925; -.
DR KEGG; tmf:PMAA_014420; -.
DR VEuPathDB; FungiDB:PMAA_014420; -.
DR HOGENOM; CLU_009995_3_1_1; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; B6QW35; -.
DR Proteomes; UP000001294; 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 Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 52..663
FT /note="Translation factor guf1, mitochondrial"
FT /id="PRO_0000402898"
FT DOMAIN 65..245
FT /note="tr-type G"
FT BINDING 74..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 138..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 192..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 663 AA; 74375 MW; 4C2F4E7C2926B011 CRC64;
MRGCLQVLRW LSTSTARRPV SSRPLHEIFP KSEFRRPFTS TILRQAQASR NVSDLEKRIA
DIPIERFRNF CIVAHVDHGK STLSDRLLEL TGVIQPGSNK QVLDKLDVER ERGITVKAQT
CTMLYNHNGE DYLLHLIDTP GHVDFRAEVS RSYASCGGAL LLVDASQGVQ AQTVANFYLA
FAQGLELVPV LNKVDLPSAD PERALEQMRS SFELDTDNAI KVSAKTGLNV AQLLPTVIER
IPAPVGDHTK PLRMLLVDSW YSTYKGVILL VRVFDGEIRA GDQVVSFATG LKYFVGEVGI
MYPDQTPQTT LRAGQVGYIY FNPGMKRSKE AKIGDTFTKV GFEKKVEPLP GFEEPKSMVF
VAAYPSDADH FEHLEDSVNQ LVLNDRSITV QKESSEALGA GFRLGFLGTL HCSVFEDRLR
HEHGASILIT PPTVPVKVIY KDGKEVTITN PAHFPDEDDI RAKVAELREP YVMATLTFPD
EYLGKVIELC EANRGIQHTL EYFTPTQVIL KYELPLGQLV EDFFGKLKGS TKGYATLDYE
EAGWKVSNIV KLQLLVNKKS VDAVARIVHY SQAERLGKQW VTKFKEHVDR QMFEIIIQAA
VGRKIVARET IKPYRKDVLA KLHAADIGRK RKLLEKQKEG RKRLNAVGNV VIDHSAFQAF
LSK
