ID I1L4K9_SOYBN Unreviewed; 1135 AA.
AC I1L4K9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
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=100804285 {ECO:0000313|EnsemblPlants:KRH39329};
GN Synonyms=EFTS {ECO:0000256|HAMAP-Rule:MF_03135};
GN ORFNames=GLYMA_09G193300 {ECO:0000313|EMBL:KRH39329.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH39329};
RN [1] {ECO:0000313|EMBL:KRH39329.1, ECO:0000313|EnsemblPlants:KRH39329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH39329};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH39329.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH39329}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH39329};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH39329.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH39329.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000842; KRH39329.1; -; Genomic_DNA.
DR RefSeq; XP_003534213.1; XM_003534165.3.
DR AlphaFoldDB; I1L4K9; -.
DR SMR; I1L4K9; -.
DR STRING; 3847.I1L4K9; -.
DR PaxDb; 3847-GLYMA09G32600-1; -.
DR EnsemblPlants; KRH39329; KRH39329; GLYMA_09G193300.
DR GeneID; 100804285; -.
DR Gramene; KRH39329; KRH39329; GLYMA_09G193300.
DR KEGG; gmx:100804285; -.
DR eggNOG; KOG1071; Eukaryota.
DR HOGENOM; CLU_012395_0_0_1; -.
DR InParanoid; I1L4K9; -.
DR OMA; VAEINCE; -.
DR OrthoDB; 5937at2759; -.
DR Proteomes; UP000008827; Chromosome 9.
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; 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:UP000008827}.
FT DOMAIN 144..213
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 258..327
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 76..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 122731 MW; 64E2F82C2AECDE1C CRC64;
MNPVIPCSIG NVSIIPGFTY STRKNNTLTR LNLSRSTVKP GSSSWRFLLP SFVASGAFPQ
NKRILSFHKK SRTSISATET DVAVEEPGPV ADEDSGELPS NEVGVSEDSF TKSDANPDPA
KARRSRPARK SEMPPVKNED LLPGATFTGK VKSVQPFGAF VDIGAFTDGL VHISMLSDSY
VKDVASVVSV GQEVKVKLIE VNTETQRISL SMRENVDTGK QRKDAPTKTE KAGPGKRNNS
KPSPKKDNVT KSTKFAIGQQ LVGSVKNLAR SGAFISLPEG EEGFLPVSEE PDDGFDNVMG
NTTLEVGQEV NVRVLRITRG QVTLTMKKEE DTAGLDSTFN QGVVHVATNP FVVAFRKNKD
IASFLDDREK TQTEVLKPST ASTLEEIKGT VNQGETVLDV PDVQGEPESS KLTDDVPSAE
DDISENVGTS ATNGSSTAIV DDESNLVSNV SSPKTGIDSA IEKEEEVAFG SLIPEEDLST
VNPIIEEATQ TDVTTIDLKT DAPVEIANEN VIETGVDQIV AEDEKQSQTP NAMEEFAAAV
LTDSDVVEPS PDKNDAITES DITSSAPAPQ ESAGDDVGAI TENIDSDTSL SGQSDELSPE
GSLTTDATEE TDQVPSPESS ATEVVKTSID DPEEEAKKQT PATENENSFT SQVEDKEVAI
ASDKNSSLSN SDGQTGATSG ESLSKATISP ALVKQLREET GAGMMDCKNA LSETGGDIIK
AQEYLRKKGL SSADKKASRV TAEGRIGSYI HDSRIGVLVE VNCETDFVSR GEIFKELVDD
IAMQVAACPQ VEFLVTEDVP EEIVNKEKEI EMQKEDLLSK PEQIRSKIVE GRIRKRLEEL
ALLEQSYIKD DKVAVKDFVK QTIATIGENI KVKRFVRFNL GEGLEKKSQD FAAEVAAQTA
AKPAPILVKE EPAVADAEAK ETEPKQITVA VSASLVKQLR EETGAGMMDC KKALAETGGD
LEKAQEYLRK KGLSSADKKS SRLAAEGRIG SYIHDSRIGV LIEVNCETDF VGRGEKFKEL
VDDLAMQVVA CPQVQFVSIE DIPETIVNKE KELEMQREDL LSKPENIREK IVEGRISKRL
GELALLEQPF IKDDSVLVKD LVKQTVAALG ENIKVRRFVR FTLGETSEKE TTVPA
//
