ID A0A0D3A3L4_BRAOL Unreviewed; 1011 AA.
AC A0A0D3A3L4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 Synonyms=106304797 {ECO:0000313|EnsemblPlants:Bo1g016860.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g016860.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g016860.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g016860.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013596647.1; XM_013741193.1.
DR AlphaFoldDB; A0A0D3A3L4; -.
DR STRING; 109376.A0A0D3A3L4; -.
DR EnsemblPlants; Bo1g016860.1; Bo1g016860.1; Bo1g016860.
DR GeneID; 106304797; -.
DR Gramene; Bo1g016860.1; Bo1g016860.1; Bo1g016860.
DR KEGG; boe:106304797; -.
DR eggNOG; KOG1071; Eukaryota.
DR HOGENOM; CLU_012395_0_0_1; -.
DR OMA; MQVAAYP; -.
DR OrthoDB; 5937at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; 2.
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; 1.
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:UP000032141}.
FT DOMAIN 137..206
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 245..316
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 86..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 110190 MW; 6A9CD0F30F2DD33D CRC64;
MATVTPSSIS KPWLVPGAAF TVKKNDCSIK CCFSRKAGKH IPPSTQRLVL PLSTSLKLFP
THGRHFVLHP HRTRATTETD LVAAAVEGQD SPPVPETDAN DKSDDSAPPA APTSRGTARP
GRKSEMPAVK NEELVAGATF TGKVRAIQPF GAFIDFGAFT DGLVHVSQLS DTFVKDVASV
VSIGQEVKVR LVEADIEAKR ISLTMRSNDD PPKRQSGGGD NKPRPGGKRG GQKKEDGFSS
KYVKGQMLDG TVKNLTRSGA FITIGEGEEG FLPTNEEADD GIGSMMMGGG SSLQAGQEVK
VRVLRIARGR VTLTMKEEDD GKFDETLSQG VVHTATNPFV LAFRKNEEIA AFLDKREEEA
EKPVEPVKES EEAITSEKVD ESLSLSPEEV LSETPKVEEE EEEEEEVIET KAEEETEEQT
ETLAAAAAEV EEVEKVEETP DVPPVPETKS EEEVSENSIP QSSATDEVSS PEAVVSEDVE
KKQEVVAEVP VTETVPDEVP SSEAVATEDV EKKEEVVAGV PVAEAIPDEV SSPEAVASED
VEKVAEVPVA EAETPAAVVT EASTEESGIK AGISPALVKQ LREETGAGMM DCKNALLESE
GDMVKAQEYL RKKGLASADK KASRATAEGR IGSYIHDSRI GVLLEVNCET DFVSRGDIFK
ELVDDLAMQV AAYPQVEYLV PEDVSEEIVK KEKEIEMQKE DLLSKPEQIR EKIVEGRIKK
RVDALALLEQ PYIKDDKVIV KDLVKQRIAT IGENIKVKRF IRYTLGEGLE KKSQDFAAEV
AAQTAAKPKA EPEKEQPKAE ELPKEAVPSP PTAVVSAGLV KQLREETGAG MMDCKKALAE
TGGDLEKAQE YLRKKGLSTA DKKSSRLAAE GRIGSYIHDA RIGVLIEVNC ETDFVGRSEK
FKELVDDLAM QAVANPQVQY VSIEDIPEEI KQKEKEIEMQ REDLESKPEN IKEKIVEGRI
SKRLGEMALL EQPFIKDDSV LVKDLVKQTV ATLGENIKVR RFVKFTLGED N
//
