位置:首页 > 蛋白库 > EFTS2_THAPS
EFTS2_THAPS
ID   EFTS2_THAPS             Reviewed;         390 AA.
AC   B8CAZ5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Elongation factor Ts 2, mitochondrial;
DE            Short=EF-Ts 2 {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-TsMt 2 {ECO:0000255|HAMAP-Rule:MF_03135};
DE   Flags: Precursor;
GN   ORFNames=THAPSDRAFT_9318;
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Schmutz J., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T.,
RA   Bruce D., Pitluck S., Rokhsar D., Armbrust V.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED89227.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000648; EED89227.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002293491.1; XM_002293455.1.
DR   AlphaFoldDB; B8CAZ5; -.
DR   SMR; B8CAZ5; -.
DR   STRING; 35128.Thaps9318; -.
DR   EnsemblProtists; EED89227; EED89227; THAPSDRAFT_9318.
DR   GeneID; 7452970; -.
DR   KEGG; tps:THAPSDRAFT_9318; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   InParanoid; B8CAZ5; -.
DR   Proteomes; UP000001449; Chromosome 13.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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.
DR   TIGRFAMs; TIGR00116; tsf; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT   CHAIN           25..390
FT                   /note="Elongation factor Ts 2, mitochondrial"
FT                   /id="PRO_0000402342"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  41560 MW;  83886B87101575C6 CRC64;
     MMIFSTAVLR LCATSRIGAV TKRASSTFLS SASSSSSSSS PTQSMPPQRY THHQFQRHSY
     STTTTTLQQQ QQPSPPLSTA QLVKQLRLLT GAPMLECKKA LASPDVNNDL ALAQEWLRKH
     SSQKIGSKVA GREALEGLVG VCIDNCDGGS RGVLVKVASE TDFASRSEVF TGLVQEIADA
     AAAAAGDGGD IVDIPTFLSN TQSITTGKLL SECLNDAVLS IRENIQLDSI VTIGTTPSSR
     SVIAGYVHGR APNSTCGTSA ALVEVEVLPK DGGGGDDAVL SEEEKSVAME AAKKLAMHVV
     ASNPLYLNPE SVPVDVVEKE REILMEKMTD SNKPPEIIEK IISGQLRKFY EGICLTEQSH
     LVEEGNPKIS KVMKGLGLVV KDFRLVGMSK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024