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Database: UniProt
Entry: F2Q0P3_TRIEC
LinkDB: F2Q0P3_TRIEC
Original site: F2Q0P3_TRIEC 
ID   F2Q0P3_TRIEC            Unreviewed;       658 AA.
AC   F2Q0P3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=GTP-binding protein GUF1 {ECO:0000313|EMBL:EGE07711.1};
GN   ORFNames=TEQG_06694 {ECO:0000313|EMBL:EGE07711.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS995764; EGE07711.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q0P3; -.
DR   VEuPathDB; FungiDB:TEQG_06694; -.
DR   eggNOG; KOG0462; Eukaryota.
DR   HOGENOM; CLU_009995_3_1_1; -.
DR   Proteomes; UP000009169; 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; 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   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};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          70..250
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         79..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT   BINDING         143..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT   BINDING         197..200
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ   SEQUENCE   658 AA;  74062 MW;  1F82BA51CA26A92E CRC64;
     MRGCLQPARW LTTATLRRPP LSCQRFTLPT PRYKPSPFPR QFHHAPVFHA RQSNRPLSPV
     EERIDAIPIE RYRNFCIVAH VDHGKSTLSD RLLELTGTIK PGENKQVLDK LDVERERGIT
     VKAQTCTMLY NYKGEDYLLH LIDTPGHVDF RTEVSRSYAS CGGALLLVDA SQGVQAQTVA
     NFYLAFAQGL TLVPVINKVD LPSADPDRAL EQMKTSFELD VDKAVRVSAK TGLNVQELLP
     AIVENIPALL LVDSWYSSYK GVIILTRVFD GEVKAGDQLV SFATGLIYTV GEVGIMYPNQ
     TPQTVLRAGQ VGYIYFNPGM KRSQEAKIGD TFTRVGCETQ VEPLPGFEEP KSMVFVAAYP
     VDSNDFHHLE ESINQLLLND RSVTMQKESS EALGAGFRLG FLGTLHCSVF EDRLRQEHGA
     SIILTPPTVP CKVIWKDGKE TIFSNPSHFP DEDTLRVKVA ELQEPYVLAT ITFPEEYLGR
     VMELCEANRG EQVSMEFFTA TQVILKYQLP LAQLVDDFFG KLKGSTKGYA SIDYEESEWR
     KSNVVKLQLL VNKTPVDAVS RIVHSSQANR LGRQWVTKFK EHVERQMFEV IIQAAVGRNV
     LARETIKPYR KDVLAKLHAS DITRRKKLLE KQKEGRKRLK AVGNVVIDHK AFQAFLAK
//
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