ID A0A448YK15_BRENA Unreviewed; 680 AA.
AC A0A448YK15;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=DEKNAAC102772 {ECO:0000313|EMBL:VEU21269.1};
GN ORFNames=BRENAR_LOCUS2004 {ECO:0000313|EMBL:VEU21269.1};
OS Brettanomyces naardenensis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU21269.1, ECO:0000313|Proteomes:UP000290900};
RN [1] {ECO:0000313|EMBL:VEU21269.1, ECO:0000313|Proteomes:UP000290900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tiukova I., Dainat J.;
RL Submitted (DEC-2018) 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: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}.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03137}.
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DR EMBL; CAACVR010000012; VEU21269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448YK15; -.
DR STRING; 13370.A0A448YK15; -.
DR InParanoid; A0A448YK15; -.
DR Proteomes; UP000290900; 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; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 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; 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; 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_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; 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 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|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03137};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|HAMAP-Rule:MF_03137};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03137}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137};
KW Reference proteome {ECO:0000313|Proteomes:UP000290900}.
FT DOMAIN 84..265
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 93..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ SEQUENCE 680 AA; 77041 MW; 24BEB08F7F49D127 CRC64;
MIAERLFQLR SRLLSNVTSF NHVLTSSSAK FCTSASRSNW QYPKTPGTDE YKGYIKYQFD
TKNNPTKVLT NIELAERMSK IPLKNYRNFI IVAHVDHGKS TLSDRLLEIT GVVDPEAPNK
QVLDKLDVER ERGITVKAQT VSMIYHYKGE DYLFHLVDSP GHVDFRLEVS RSYASCQGAL
LLVDASEGVK AQTVANFYLA YSMDLKLIPV INKVDLDTAD VPRTEEQIES MFELSRNDII
HVSAKSGLNV KYLLPKIIEN IPPPLHCRPD EPFRAQIVDS WYDSYLGVIM LINVADGSVK
KGSKIVSFKT RQKYEVKEVG IMYPDRTPLP HLVAGQVAYI IPGIKDPNTV FVGDTLYEAG
TSVEPLEGFE EPKPMVFVGA FPAQGTDFKK MEERLEHLFL NDRSVTLQHA TSSALGQGWR
LGFLGSLHAS IFKERLEKEY GESLIITSPT VPYKVHYKDG REVTVSNPDD FPDSLKKTTI
SYFSEPYVDA FMSFPKEYVG KVMQLCTANR GEQEEIQYMS NDQVLMTYSI PTSQLIDDFF
GKLKGITKGY ASLDYEDAGY KPSDVYKLEI LVNGESIDAL STVMHKSQIE KNSKEFVKRL
KEFLRIQQFE VAIQAQANGK IVARETIRAR RKDVLAKLHA SDESRRKKLL VRQKEGKKLL
RSIGKVKIPP QAYQSFLKAR
//
