ID   A0A2U1PS28_ARTAN        Unreviewed;       661 AA.
AC   A0A2U1PS28;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   10-JUN-2026, entry version 26.
DE   RecName: Full=Translation factor GUF1 homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03137};
DE            EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_03137};
DE   AltName: Full=Elongation factor 4 homolog {ECO:0000256|HAMAP-Rule:MF_03137};
DE            Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_03137};
DE   AltName: Full=GTPase GUF1 homolog {ECO:0000256|HAMAP-Rule:MF_03137};
DE   AltName: Full=Ribosomal back-translocase {ECO:0000256|HAMAP-Rule:MF_03137};
GN   ORFNames=CTI12_AA119750 {ECO:0000313|EMBL:PWA88522.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA88522.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA88522.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA88522.1};
RX   PubMed=29703587; DOI=.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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:0000256|HAMAP-Rule:MF_03137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03137};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03137}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03137}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03137}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. LepA
CC       subfamily. {ECO:0000256|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:0000256|ARBA:ARBA00005454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWA88522.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PKPP01000808; PWA88522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1PS28; -.
DR   OrthoDB; 1074at2759; -.
DR   Proteomes; UP000245207; 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; cd03699; EF4_II; 1.
DR   CDD; cd16260; EF4_III; 1.
DR   CDD; cd01890; LepA; 1.
DR   CDD; cd03709; lepA_C; 1.
DR   FunFam; 2.40.30.10:FF:000015; Translation factor GUF1, mitochondrial; 1.
DR   FunFam; 3.30.70.240:FF:000007; Translation factor GUF1, mitochondrial; 1.
DR   FunFam; 3.30.70.2570:FF:000001; Translation factor GUF1, mitochondrial; 1.
DR   FunFam; 3.30.70.870:FF:000004; Translation factor GUF1, mitochondrial; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.30.10; Translation factors; 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; IPR004161; EFTu-like_2.
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.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR01393; lepA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_03137};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03137};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03137};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03137};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03137};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03137};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03137}; Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT   DOMAIN          86..245
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         95..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT   BINDING         160..164
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT   BINDING         192..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ   SEQUENCE   661 AA;  73883 MW;  73DD811A8D6B2B66 CRC64;
     MSMATTSLKL TLSSKPPPQH NHHHHLPVHF SNRTFHTLQS FNPSKLNLNN KTRRRRYKVF
     SKAVDVQDAE ATALAGRDRL LKVPIERIRN FSIIAHIDHG KSTLADKLLQ VTGTVQSREM
     KEQFLDNMDL ERERGITIKL QAARMRFAFE GQPYCLNLID TPGHVDFSYE VSRSLAACEG
     ALLVVDASQV LNKIDLPGAE PSRVIQEIEE VIGLDCSNAI YCSAKEGIGI NEILSAIVQR
     IPPPPNSAGR PLRALIFDSY YDAYRGVIVY FRVIDGTVKK GDRILFMASG KDYYADEVGV
     LSPNQLQVDE LYAGEVGYIS ASIRSVADAR VGDTITHYSR KAEESLPGYK EATPMVFCGL
     FPIDADQFPD LRDALDKLQL NDAALKFEPE TSSAMGFGFR CGFLGLLHME IVQERLEREY
     NLSLITTAPS VVYKVFCTNG EIVDCSNPSA LPEQGKRKSI EEPIVKIEML TPKDYIGSLM
     ELSQDRRGEF KEMKFITENR ASLTYEMPLA EMVGDFFDQL KSRSKGYASM EYSFIGYKES
     DLIKLDVLIN GEGVEPLSTI VHKDKAYSVG RALTQKLKEL IPRQMFKVPI QACIGTKVIA
     SEALSAIRKD VLAKCYGGDI SRKKKLLKKQ AAGKKRMKAI GKVDVPQEAF MAVLKLEKEV
     L
//