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Database: UniProt
Entry: A0A445M362_GLYSO
LinkDB: A0A445M362_GLYSO
Original site: A0A445M362_GLYSO 
ID   A0A445M362_GLYSO        Unreviewed;      1133 AA.
AC   A0A445M362;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=D0Y65_001554 {ECO:0000313|EMBL:RZC29986.1};
OS   Glycine soja (Wild soybean).
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=3848 {ECO:0000313|EMBL:RZC29986.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZC29986.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC29986.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-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}.
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:RZC29986.1}.
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DR   EMBL; QZWG01000001; RZC29986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445M362; -.
DR   SMR; A0A445M362; -.
DR   OrthoDB; 5937at2759; -.
DR   Proteomes; UP000289340; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:UP000289340}.
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          63..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..116
FT                   /note="Polar residues"
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        375..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..459
FT                   /note="Polar 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..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  122609 MW;  C3883F883114CA06 CRC64;
     MNPVIPCSIG NVSIIPVFIY STRKNNTLTR FNLSRSTVKP GSSSWRFLLP SFVASGAFPQ
     NKGIRSFHKK SSTSISATET DVTVEEPSPV ADEDSGEITS NEVGISEDSS SKSDANPDPA
     KGRRSRPARK SEMPPVKNED LIPGATFTGK VKSVQPFGAF VDIGAFTDGL VHISMLSDSY
     VKDVTSVVSV GQEVKVKLIE VNTETQRISL SMRENADTGK QRKDAPVKTE KAGPGKRNSS
     KPSSKKDNVT KSTKFAIGQQ LVGSVKNLAR SGAFISLPEG EEGFLPVSEE PDDGFDNVMG
     NTTLEVGQEV NVRVLRITRG QVTLTMKKEE DTAGLDSTFN HGVVHVATNP FVLAFRKNKD
     IASFLDEREK TQNEVQKPTT ASTSEEIKGT VNQGETVLDV PDVQGEPESS KLTDDDVPSA
     EDDISENVGT SATNGSSTAI VDDESNLVSN VSSPTTGIDS AIEKEEEVAS GSLIPEEDLS
     TVNPIIEEVT QTDVTNDLKT DTPVEIANEN VIETGVDQIV TEDEKQSQTP DAIEEFAAAV
     LTDSDVVEPS PDKNDTITES DITSSAPALQ ESADDDVGAI TENIDSDTSL GGQSDELSPV
     GSLTTDATEE TDQVPSPESS ATEVVKPSVD DPEEEAQKLT PATENENSFT SQVEDKEVAI
     ACEENNSLSN SDGQTGATSG EGLSKATISP ALVKQLREET GAGMMDCKKA LSETGGDIIK
     AQEYLRKKGL SSADKKASRV TAEGRIGSYI HDSRIGVLVE VNCETDFVSR GEIFKELVDD
     IAMQVAACPQ VEYLVTEDVP EEIVNKEKEI EMQKEDLLSK PEQIRSKIVE GRIRKRLEEL
     ALLEQSYIKD DKVAVKDFIK QTIATIGENI KVKRFVRFNL GEGLEKKSQD FAAEVAAQTA
     AKPAPMPAKE QPAVPEAKET EPKQSTVAVS ASLVKQLREE TGAGMMDCKK ALAETGGDLE
     KAQEYLRKKG LSTADKKSSR LAAEGRIGSY IHDSRIGVLI EVNCETDFVG RGEKFKELVD
     DLAMQVVACP QVQFVSIEDI PETIVNKEKE LEMQREDLLS KPENIREKIV EGRILKRLGE
     LALLEQPFIK DDSVLVKDLV KQTVAALGEN IKVRRFVRFT LGETSEKETT VPA
//
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