ID G3IMP1_CRIGR Unreviewed; 421 AA.
AC G3IMP1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=GTP-binding protein GUF1-like {ECO:0000313|EMBL:EGW14502.1};
GN ORFNames=I79_025182 {ECO:0000313|EMBL:EGW14502.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW14502.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(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:0000256|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; 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}.
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DR EMBL; JH004924; EGW14502.1; -; Genomic_DNA.
DR AlphaFoldDB; G3IMP1; -.
DR STRING; 10029.G3IMP1; -.
DR PaxDb; 10029-XP_007632360-1; -.
DR eggNOG; KOG0462; Eukaryota.
DR InParanoid; G3IMP1; -.
DR Proteomes; UP000001075; 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 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; 1.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
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 NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF7; TRANSLATION FACTOR GUF1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
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|HAMAP-Rule:MF_03137};
KW Hydrolase {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|HAMAP-Rule:MF_03137};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT DOMAIN 7..188
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ SEQUENCE 421 AA; 46712 MW; 0462F76F94960BDD CRC64;
MSRFPAEDIR NFSIIAHVDH GKSTLADRLL ELTGTIDKTK KNQQVLDKLQ VERERGITVK
AQTATLFYSF KGKQYLLNLI DTPGHVDFSY EVSRSLSACQ GVLLVVDANE GIQAQTVANF
FLAFEAQLSV IPVINKIDLK NADPERVEKQ IEKVFDIPSD ECIKISAKLG TNVDSVLQAV
IERIPPPKVH RENPLRALVF DSTFDQYRGV IANIALFDGV VSKGDKIVSA HTKKTYEVNE
VGILNPNEQP THKLYAGQVG FLIAGMKDVT EAQIGDTLYL HNHPVEPLPG FKSAKPMVFA
GVYPVDQSEY NNLKSAIEKL TLNDSSVTVH RDSSLALGAG WRLGFLGLLH MEVFNQRLEQ
EYNASVILTT PTVPYKAVLS SAKLIKVPHL LLVCISLKGK ISQRSVHLYT KCRRKVLVIG
K
//
