ID A0A3B6MML9_WHEAT Unreviewed; 1007 AA.
AC A0A3B6MML9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Elongation factor Ts, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03135};
DE Short=EF-Ts {ECO:0000256|HAMAP-Rule:MF_03135};
DE Short=EF-TsMt {ECO:0000256|HAMAP-Rule:MF_03135};
GN Name=EFTS {ECO:0000256|HAMAP-Rule:MF_03135};
GN ORFNames=CFC21_076470 {ECO:0000313|EMBL:KAF7071060.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G105500.1};
RN [1] {ECO:0000313|EMBL:KAF7071060.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7071060.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G105500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G105500.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G105500.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7071060.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7071060.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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:0000256|HAMAP-Rule:MF_03135, ECO:0000256|RuleBase:RU000642}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03135}.
CC -!- SIMILARITY: Belongs to the EF-Ts family.
CC {ECO:0000256|ARBA:ARBA00005532, ECO:0000256|HAMAP-Rule:MF_03135,
CC ECO:0000256|RuleBase:RU000642}.
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DR EMBL; CM022225; KAF7071060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6MML9; -.
DR SMR; A0A3B6MML9; -.
DR STRING; 4565.A0A3B6MML9; -.
DR PaxDb; 4565-Traes_5DS_1BE0927E1-2; -.
DR EnsemblPlants; TraesCS5D02G105500.1; TraesCS5D02G105500.1; TraesCS5D02G105500.
DR Gramene; TraesCAD_scaffold_059213_01G000200.1; TraesCAD_scaffold_059213_01G000200.1; TraesCAD_scaffold_059213_01G000200.
DR Gramene; TraesCLE_scaffold_138189_01G000200.1; TraesCLE_scaffold_138189_01G000200.1; TraesCLE_scaffold_138189_01G000200.
DR Gramene; TraesCS5D02G105500.1; TraesCS5D02G105500.1; TraesCS5D02G105500.
DR Gramene; TraesCS5D03G0248900.1; TraesCS5D03G0248900.1.CDS; TraesCS5D03G0248900.
DR Gramene; TraesPAR_scaffold_124903_01G000200.1; TraesPAR_scaffold_124903_01G000200.1; TraesPAR_scaffold_124903_01G000200.
DR Gramene; TraesROB_scaffold_056872_01G000200.1; TraesROB_scaffold_056872_01G000200.1; TraesROB_scaffold_056872_01G000200.
DR Gramene; TraesWEE_scaffold_083479_01G000200.1; TraesWEE_scaffold_083479_01G000200.1; TraesWEE_scaffold_083479_01G000200.
DR OMA; VAEINCE; -.
DR Proteomes; UP000019116; Chromosome 5D.
DR Proteomes; UP000815260; Chromosome 5D.
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 CDD; cd14275; UBA_EF-Ts; 2.
DR Gene3D; 1.10.286.20; -; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.479.20; Elongation factor Ts, dimerisation domain; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_00050; EF_Ts; 2.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR NCBIfam; TIGR00116; tsf; 3.
DR PANTHER; PTHR11741; ELONGATION FACTOR TS; 1.
DR PANTHER; PTHR11741:SF10; POLYPROTEIN OF EF-TS, CHLOROPLASTIC; 1.
DR Pfam; PF00889; EF_TS; 3.
DR Pfam; PF00575; S1; 2.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF54713; Elongation factor Ts (EF-Ts), dimerisation domain; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF46934; UBA-like; 2.
DR PROSITE; PS01126; EF_TS_1; 2.
DR PROSITE; PS01127; EF_TS_2; 2.
DR PROSITE; PS50126; S1; 2.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_03135}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03135};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03135}; Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 143..212
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 257..325
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 86..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 109065 MW; 35FCD40CA226F3C9 CRC64;
MTPVVHCSVG TISLFHIGSF RPSREIQIRR FRGSERYSRV TSPSRHGLLQ PQTPFHLISI
YKRSWSSANN RLRTLSAAAV GTDVTVEGSA SPSGETSEAA PAAAETTGQA VASKSPASSP
PKLGRNPRKS EMPPLKDGDL VPGASFTGKV RSIKPFGVFV DIGAFTEGLV HISRVSDGFV
EDISTLFTVG QEVSVKLVEV NKETRRISLT MRTGGDYVKE APTAPSGGRS PTAAAPRSSP
RQTKDFKKID EAKYTRGQSL TGTVKNTTRT GSFVTLPDGE EGFLPREEEA AALFTLIGHS
ALEVGQEVTV KVLNVARGQV TLTMKGGEDD DDELSSLNTN LKQGWSRGTN AFELAFRRSK
EISAFLDQRE KVTAPEVKTE VETETSVSTS GVESAIDDKL VEPPTEVESK EDSSLTETVT
GTVEPPTVSA TEVETKEEDS ASTEAVTGAI EPPTVSATEV ETKEEDSPST EAVTGAVEEI
TPVDKAEEPE ESVQEVPTTA SSESAVVTEE VAASDEKTTE VSAAAAAEAS TTTATISPAL
VKQLRDATGA GMMDCKKALA ESSGDIDKAQ EFLRKKGLAA ADKRAGRATA EGRIGSYIHD
SRIGILIELN CETDFVSRGD VFKELVDDLA MQAAACPQVN YISIDDVPEE VVKKETELEM
QREDLLSKPE QIRAKIVEGR VKKRLGEFAL LEQPFIKNDK VTTGEWVKQT IATIGENMKV
RRFVRYNLGE GLEKKSQDFA AEVAAQTAAK PPPAAPVKDD KPEESVEAAE KKPAVAISAA
LVKQLRDETG AGMMDCKKAL AETGGDLQGA QEFLRKKGLS SADKKSSRLT AEGLIGSYIH
DNRIGCMIEI NSETDFVARN EKFKELVNDL AMQVVACPQV EYVSMEDIPE SVVSKEKEIE
MQREDLQSKP ENIREKIVEG RISKRLGVMA LLEQPFIKDD SKTVKDLVKE TIAGLGENIK
VRRFVRLNSI PKIYMLQTRC STTCSCELQE LPHPAQFRQP ACSPARR
//