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EFTS_MALGO
ID   EFTS_MALGO              Reviewed;         406 AA.
AC   A8PRT2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Elongation factor Ts, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-TsMt {ECO:0000255|HAMAP-Rule:MF_03135};
GN   Name=TSF1 {ECO:0000255|HAMAP-Rule:MF_03135}; ORFNames=MGL_0122;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC       exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC       Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_03135}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
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DR   EMBL; AAYY01000001; EDP45133.1; -; Genomic_DNA.
DR   RefSeq; XP_001732347.1; XM_001732295.1.
DR   AlphaFoldDB; A8PRT2; -.
DR   SMR; A8PRT2; -.
DR   STRING; 425265.A8PRT2; -.
DR   EnsemblFungi; EDP45133; EDP45133; MGL_0122.
DR   GeneID; 5856653; -.
DR   KEGG; mgl:MGL_0122; -.
DR   VEuPathDB; FungiDB:MGL_0122; -.
DR   InParanoid; A8PRT2; -.
DR   OMA; FAKWTVG; -.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.479.20; -; 2.
DR   HAMAP; MF_00050; EF_Ts; 1.
DR   InterPro; IPR036402; EF-Ts_dimer_sf.
DR   InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR   InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR   InterPro; IPR018101; Transl_elong_Ts_CS.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..406
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402346"
FT   REGION          387..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  42310 MW;  0500EA017179C602 CRC64;
     MRAMRPVAHL ARCFCASSSV KETRPSIQAI AELRKALPGT SMLKAREALT ASRSPDAPDT
     DNVEAAIAWL EQTRASDGAK REAKVASRVT AEGTIGLCTL SDGISSPGAR AAMVELNCET
     DFVARNDIFG ALARDIAHTA AWFPIVAASE TSAVLSDVDV AAFLECPIIP FEASEENKHD
     VISVRAAITS VVARLGEKVA LGRVASLAPT SGGSHGSALV CGSFAHGTAS APPAPQTPVA
     ATFASGRVAS LLAVQVHGPL SQRIMSRTAT TQHNDHDHDR NGDDERKRQL RALARSLARQ
     AAGFPTTSVD APSATAAVAS DASSETSGAL LTQPFVMLLP AAGLDPSVNE QKSVRDALEL
     WSNTYAGQAD GIRVAALRRW EVGETAARPS DETSFADQVK EAAGLA
 
 
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