ID B9RKL9_RICCO Unreviewed; 972 AA.
AC B9RKL9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
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=RCOM_1051260 {ECO:0000313|EMBL:EEF48217.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(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: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; EQ973784; EEF48217.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RKL9; -.
DR STRING; 3988.B9RKL9; -.
DR eggNOG; KOG1071; Eukaryota.
DR InParanoid; B9RKL9; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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; 1.
DR Gene3D; 1.10.286.20; -; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
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; 2.
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; 1.
DR PROSITE; PS01126; EF_TS_1; 1.
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:UP000008311}.
FT DOMAIN 151..220
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 268..337
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 91..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 105725 MW; D3E8982037707869 CRC64;
MTTVVPCSTS SISLIPGTPF RLKKNNNLTR CNLLRKSSKH VISSQRHVLP LLTSVGLFPH
YRRDCNWLHR SIVYGVSATG TDTDVVIEEP ESPVTDENSG GASDIPADAA ETSENSSIKS
DSNRAPAQTK RSRPGRKSEM PPVTNEELIP GATFTGKVRS IQPFGAFVDF GAFTDGLVHV
SRLSDNFVKD VGNVVSVGQE VTVRLVEANT ETGRISLTMR ESDDTNKSQQ QRDAPATASS
GKPRPGRRNA PKSGQRREDN KISKFVKGQE LEGTVKNLTR SGTFISLPEG EEGFLPTSEE
SDGGLESMMG GSSLEVGQEV SVRVLRISRG QVTLTMKKEE DNKLNTELLQ GVVHAATNPF
VLAFRKNRDI SSFLEEREKM EKVANQPVEP KIPVEVGEQE KQTETVSDIL EVQGQPSSSN
EGSDSVTSTV AETLVDETSP KEVAEEPSIA GDDEVPGSIE SSSPQSVEAA VQTVEKEAEE
SSGTPDPIGS VSTADNITEQ TPLTDEMGSD GKSGPYGEIS SEVSTPVSPA AEEVVENQLG
ESITNEELQT PIAENEISSI APVEDEGTGA TSPDENGSIT GSGEQADVPS LQEATEVNCE
TDFVSRGEIF KELVDDIAMQ VAACPQVKYL VTEDVPEEIV NKEKEIEMQK EDLLSKPEQI
RSKIVEGRIR KRLEELALLE QPYIKNDKIV VKDWVKQTIA TIGENIKVKR FIRFNLGEGL
EKKSQDFAAE VAAQTTAKPV AAPAKEQSVS AEAEEPVEKP PVVAVSAALV KQLREETGAG
MMDCKKALSE TGGDLEKAQE YLRKKGLSAA DKKSSRLAAE GRIGSYIHDS RIGVLIEVNC
ETDFVGRSEK FKELVDDLAM QVVACPQVQF VSTEEIPESI LNKEKELEMQ REDLASKPEN
IREKIVEGRI SKRLGELALL EQPFIKDDSV LVKDLVKQTV AAIGENIKVR RFVRFTIGEN
TEDAKTETET EA
//
