EFTS1_POSPM
ID EFTS1_POSPM Reviewed; 290 AA.
AC B8PE34;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Elongation factor Ts, mitochondrial 1 {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-Ts 1 {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-TsMt 1 {ECO:0000255|HAMAP-Rule:MF_03135};
GN Name=TSF1-1 {ECO:0000255|HAMAP-Rule:MF_03135}; ORFNames=POSPLDRAFT_106662;
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Dacryobolaceae; Postia.
OX NCBI_TaxID=561896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R;
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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; EQ966329; EED80885.1; -; Genomic_DNA.
DR RefSeq; XP_002473925.1; XM_002473880.1.
DR AlphaFoldDB; B8PE34; -.
DR SMR; B8PE34; -.
DR STRING; 561896.B8PE34; -.
DR EnsemblFungi; EED80885; EED80885; POSPLDRAFT_106662.
DR KEGG; ppl:POSPLDRAFT_106662; -.
DR HOGENOM; CLU_047155_4_1_1; -.
DR InParanoid; B8PE34; -.
DR OMA; TCIRSPS; -.
DR Proteomes; UP000001743; 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..290
FT /note="Elongation factor Ts, mitochondrial 1"
FT /id="PRO_0000402347"
SQ SEQUENCE 290 AA; 31435 MW; 14BADA6CDED3714B CRC64;
MDVSKALLWL EKQQTESAVK KAAKVADRTA NEGLIGTTVL SSGVANGRRV GVRAAMVELN
CETDFVARNE LFANLLEDIT HTAAFISEPA NAETFMQPFS METLQNAPLL SQTKPSQNGK
ATVSEAMRDL TGRVGEKISL RRALTVVRDP FTSSQPDLAL RVAARVHQSV FNPTQGRIGS
LALLALKSKR LSEVIASQTF QDDLDKLCQA LGRQVIGFPT TCIRSPSGTT DEGALYDQPF
SMFIGPGNDQ SVGAFLQSWA QERSLVNEDE EQSAGVEVLE FAKWSVGEVV