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Database: UniProt
Entry: J9J459_9SPIT
LinkDB: J9J459_9SPIT
Original site: J9J459_9SPIT 
ID   J9J459_9SPIT            Unreviewed;       627 AA.
AC   J9J459;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=OXYTRI_18266 {ECO:0000313|EMBL:EJY83998.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY83998.1};
RN   [1] {ECO:0000313|EMBL:EJY83998.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY83998.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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}.
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:EJY83998.1}.
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DR   EMBL; AMCR01004447; EJY83998.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9J459; -.
DR   EnsemblProtists; EJY83998; EJY83998; OXYTRI_18266.
DR   OrthoDB; 5473535at2759; -.
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; cd16260; EF4_III; 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; 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; 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|HAMAP-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|HAMAP-Rule:MF_03137};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137}.
FT   DOMAIN          1..200
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT   BINDING         147..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ   SEQUENCE   627 AA;  70794 MW;  F9CDA40E046A8E92 CRC64;
     MFVPNLPSSK QFSNMNETNG EFKILINDTK TGGQQRILIT NIQGTINKLT KEDHHQVLDT
     LKVERDRGIT VIAQTATMIY KYQGVDYLMN LIDTPGHVDF TYQVSRSIRA CEGALLVVDA
     TKGIQAQTIS NFYQAFDAGL TIIPIINKID LPAADVDATR QQLIEQFDFK EEEILYISAK
     EGRNVMEVLN QTIERVSSPF PEKSRDELAK LPLKAFLFDA RFVQSRGVSC LIKIMQGTLD
     MQKLRNLMSY HRSKRYDLFE LGIVQPNMVP IGILNPGQVG YFLSNMKSVQ DAHIGDTFYD
     EKYQKDSIEP FPGYATPQPM VFAGIYPEDP DDYEDLEKSL QKLCLTDGSV SFNYESSAAL
     GSGFRCGFLG MLHLDVFRQR LDDEHDMVSI ITAPTVSYRV QLRGKDKDMK VVDNPLEAPP
     DESIDKWFEA IMIATIITPI DYAKGVTILC EEKRGQMKSQ EFLNNSTVVH FTYEIPLAEL
     VTDFFDKLKS ISSGYASLDY EFVRYEEASV VKVIFHLNGD PIDALTFLVH DSRAVDFAKR
     YCAKLKDLLP AQLFKIAIQG KIGGKVIARE DIKALRKDVT AKCYGGDITR KKKLLEKQKA
     GKKKMKARML GQIPVDSEVF LGLLKQS
//
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