ID A0A0N4ZTJ0_PARTI Unreviewed; 872 AA.
AC A0A0N4ZTJ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
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};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001181800.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001181800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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}.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR AlphaFoldDB; A0A0N4ZTJ0; -.
DR STRING; 131310.A0A0N4ZTJ0; -.
DR WBParaSite; PTRK_0001181800.1; PTRK_0001181800.1; PTRK_0001181800.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd14275; UBA_EF-Ts; 1.
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; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
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 PANTHER; PTHR47248; PROTEIN CBG06772; 1.
DR PANTHER; PTHR47248:SF7; PROTEIN CBG19214; 1.
DR Pfam; PF00889; EF_TS; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00131; KU; 2.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF54713; Elongation factor Ts (EF-Ts), dimerisation domain; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS01127; EF_TS_2; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}.
FT DOMAIN 332..388
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 490..547
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 689..744
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 872 AA; 97777 MW; F02D174696B8486A CRC64;
MLRYSSIFSK QAIRSLCVSA PSTGASTITP TKKALMKLRK ITGYSYVNCK KAVDKFGIDN
LEEATSWLRE LAKKEGWAKA AKLSHKQTTE GLFSVLSKNN LGAVVELNCQ TDFVARGDDF
KNLISDITKS VLQHAETLSD TVNVNDNELV VVPVTVDDIK TSNGTTIKET LAMAVGKLGE
NITCPTLSMI FGQKDIMIKG HSHPKEKFNN CEIGRFVSLV GLKRDPFKAT SFPSEKLGEQ
ICQHIIGMRP ELLGEPPEEK NEIVEEKTND GKDEDDINDF YRGKTTELNE DETSLLRQPF
MLNPSQSVFS YLNSHGAAIV NYLRMEVVLP AEGPCTLGTN EEAKNYKCTT EGYYELVQCN
DEYCVCVDPY TGSEAGDTRT DRKYTPTCGN CLKSYAKAAA LNKNQFELPQ CNKMNGKFEK
MRYNDNEMYC VDENTGEKID NKPKQYKGLY TCDDYSKYEN APKTTINYPD DVKETQPLIK
EEMPVVNVGC AIPKDLGETC SPSDHKKSSR LLYFFDTETS QCLPFMYKGC GGNINRYNSA
SECSSACIPM DYSSCSGHFQ SATDSQGNHI LCNMGRGNPM GTNKKTKDEC PPNYTCIMSA
FFGSCCHKPT EDLFNRNYSP SCNETKFESS TPVKHEKYGF STTLLGRECS DNFCPTGSTC
SYSLPAIEYE SWMIQRMPPR TRFTHVAECT LPPDIGEICD NTDVKGGIFY FFDPETLECY
PMKFKGCKGN QNKFLDKDEC KSYCLGSNYD GCRGGIEPAE KMCGYHSDCS GENLNKTEDY
MCSNNYMLVI GKKYDHCCYK ETELYLQGKE DLVRCMGGNF IKGTPVRLDK KGYHPAWLLG
RSCDHDFCPL GTVCQQRDIF AYCCYPNNNS IH
//
