ID   EFTS_COPC7              Reviewed;         333 AA.
AC   A8N2Z9;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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};
DE   Flags: Precursor;
GN   Name=TSF1 {ECO:0000255|HAMAP-Rule:MF_03135}; ORFNames=CC1G_06571;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
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DR   EMBL; AACS02000001; EAU92560.1; -; Genomic_DNA.
DR   RefSeq; XP_001829234.1; XM_001829182.1.
DR   AlphaFoldDB; A8N2Z9; -.
DR   SMR; A8N2Z9; -.
DR   STRING; 5346.XP_001829234.1; -.
DR   EnsemblFungi; EAU92560; EAU92560; CC1G_06571.
DR   GeneID; 6005661; -.
DR   KEGG; cci:CC1G_06571; -.
DR   VEuPathDB; FungiDB:CC1G_06571; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   HOGENOM; CLU_047155_4_1_1; -.
DR   InParanoid; A8N2Z9; -.
DR   OMA; FAKWTVG; -.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000001861; 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; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT   CHAIN           18..333
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402343"
SQ   SEQUENCE   333 AA;  35470 MW;  F64C1E6D7F4604FA CRC64;
     MLRTLRPTLP SRCLRLYSTA PEKPSLKLVA ELRKRTEVSI VKAREALSAS NNDIEAALQW
     LAKDLETTGA KKAAKVGGRT TNEGLVSVSI LSNFTASGLQ RGIRAAMIEL NCETDFVGRN
     ELFGRLAGDI AHTAAVVAEP GASVFQNLSL EFLQEAPLVS RSDPTSAPSG TVATTIRDTI
     AKVGENITLR RALVVAAEPP AADAAQALRL GQYVHGTIHQ PTEGRIGTLA LLGLKYPSPK
     GFTQETTEKL ASLERALARQ IVGFPTQSIK GSEETALYSQ PFMMLPGELN SRPVGEALQA
     WSVQQGIVGS EGDAGAVEVL EFAKWSVGEP LES