GUF1_CULQU
ID GUF1_CULQU Reviewed; 647 AA.
AC B0WXB8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=CPIJ012086;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS232161; EDS36379.1; -; Genomic_DNA.
DR RefSeq; XP_001862040.1; XM_001862005.1.
DR AlphaFoldDB; B0WXB8; -.
DR SMR; B0WXB8; -.
DR STRING; 7176.CPIJ012086-PA; -.
DR GeneID; 6044536; -.
DR KEGG; cqu:CpipJ_CPIJ012086; -.
DR VEuPathDB; VectorBase:CPIJ012086; -.
DR VEuPathDB; VectorBase:CQUJHB000100; -.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_3_1; -.
DR InParanoid; B0WXB8; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; B0WXB8; -.
DR Proteomes; UP000002320; 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 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..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 35..647
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402837"
FT DOMAIN 46..227
FT /note="tr-type G"
FT BINDING 55..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 120..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 174..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 647 AA; 72008 MW; 04DC644A1E89093F CRC64;
MLSFLRLSQL GRIGVQQRFK PLIHRTLSTS CRRFSVDIAY DEIPVSRIRN FSIIAHVDHG
KSTLADRLLE LTGTIKKNAT NKQVLDSLQV EKERGITVKA QTASLLYRYE GSDYLLNLID
TPGHVDFANE VSRSLAACDG VILLVDANEG VQAQTVANYH LARGKELVIV PVLNKIDLKN
ARPDAVTQEL FTLFGIDPDG VLRISAKQGT GCEQVLVEIV KRLPAPDVRR GEQFRALIFD
SWFDRYRGAL NLVYVKDGEV RVGQEIVSCH TGKVYEVKSL AMLRPDEQKI ERLVAGQVGL
LGCNMRTSKE SNIGDTLYLK KNKNCEPLPG FKPQQPMVFA GVYPADQSQH PYLKGAIEKL
VLNDSAVTVV PDSSPALGQG WRLGFLGLLH LDVFSQRLQQ EYDAEPILTA PSVTYKIKLK
GIKMIAAHGG KDTIFVSNPA LFPDPNSVEE YYEPYVLGTI IAPTECTGPI IGLCVERRAV
QKTSINIDND RIMTTYLMPL NEIVLDFHDQ LKSISSGYAS FDYEDHGYVA SALVRMDVLL
NGTLVDELCT VVHISKAQSH ARELVLKLKE LIPRQMVQIA IQATVGGKVV ARETLKAYRK
DVTAKLYGGD VTRRMKLLKQ QAEGKKKMRA IANINVPRDT FINVLKR
