ID A0A176WAV9_MARPO Unreviewed; 1456 AA.
AC A0A176WAV9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AXG93_2789s1260 {ECO:0000313|EMBL:OAE29216.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE29216.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE29216.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE29216.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE29216.1}.
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DR EMBL; LVLJ01001507; OAE29216.1; -; Genomic_DNA.
DR OrthoDB; 5937at2759; -.
DR Proteomes; UP000077202; 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 CDD; cd00164; S1_like; 1.
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; 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; 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:UP000077202}.
FT DOMAIN 241..310
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 370..437
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 153969 MW; B051F5E18DB75728 CRC64;
MAVRGGSQEP GAERSGILPS LAGDERIRGQ RTRLTRDGGG RGRTGSRREG VCGRASRLRY
IFNPSICAQV SQAPTPRLRD HLKVSCLDAC LEDLGTVQSL CQTTASASKI WQAKRSVSSG
SGLRRASAES QIEGASLKSS LPSSVYESRR RVGVRHVARS GSSRRVFTAA VEGSVAVEEP
STEAEVVETP ESTTTEAVAE PEQDSTPAAA PQRRGGKSKP RGNARSKRED ATVPVEALVQ
GAVFTGKVTT IQPFGAFVNF GAFTDGLVHI SKLSSGYVSN VGDIVSVGQE VQVTVIDVDN
TAGRIALSMA EKEERTEGSG RQGGEVGGDK SRLQEGNGGR PVNKGKSAGR GNQSNRRDEP
KKPQTKLVKG QVVEGTVKNT ARGGVYVILP EEEEAFLKYS EVPGGENMAP ESGLQAGQKI
TATVLRIDRG KITLSMKPVV DIKSVNSSIN KGAGGGATNP FEIAFRAMDL IPEPVVEPPV
EETVEEAPAA ETEQSNTAAV ADVAEEITED MESVQINEKS EQVAPIVDDP TPAPPAAELS
EETKPEEVPA EVTAEVPAPE IVEEEVEEVV ETPAAEAAVS APVEESAEEI TETPAAEAAI
PSPVEEKAEE VVEAPPAEAA IGAPAEEKVE EVTETPAAEA AIPAPVEEKV EEVVETPAAE
AAIPSPVEEK AEEVVATPAA EAAIPAAAEE EKVEEVVETP AAETAIPSPV EEKVEEVIET
PAVEAAIPAS VEEKVEDVVE TPAAEAAIPA PVEEKVEEVI ETPAAEASIP EAVEEKVEEV
TETPAAEAAI PEAVEEKVEE VIETPAAAAA IPAPVEEKVE EVIDTPVAEA AIPTPVEEKV
EEVIETPAAE AAIPAPVEEK VEEVVEPPAA EAATPAPVEE KVEELVQTPE AAIPEAVEEK
VEEVVETPAA EAAIPSPVEE KVEEAVETPA AEAVIPETVE EKVEEVTETP AVEAASPAPV
EEQTKELEAP KQEVTASAAA VEEKKGGISA ALVKKLRDET GAGMMDCKKA LTECKGDFDS
ARDALRKKGL ASADKKASRI ASEGLIGSYI HDSRIGVLVE VNCETDFVAR GPVFKQLVSD
IGMQVVACPQ VKYVAVEDIP AEIVNKETEL EMQREDLVNK PEAVRAKIVE GRVSKRMNES
VLLEQPYIRD DSILVKDLVK QTVATVGENI KVRRFERYTL GEGLDKKSED FAAEVAAQTA
QTVEAPKVEE KPAKVDSVEE ASPKVAVSAG AVEEASPKVA VSAGAVKELR NSTGAGMMDC
KKALAATGND MEKAVEFLRK KGLASADKKA SRLASEGLVG SYVHNGVIGV MVEINCETDF
VARSEKFKEL VNNVAMQIAA CPLVTAVSIE DVPASFVEEE RAIELGKEDL ANKPEAVRAR
IVEGRLNKRL SELALLEQPF IKDDTKLMKD VIKETVAALG ENIQVRRFCR FNLGEGIEKK
VVDFAAEVAA QTGQTS
//
