| Identifier | TRYPANRDTASE [View Relations] [View Alignment]
|
| Accession | PR00470 |
| No. of Motifs | 6 |
| Creation Date | 03-MAR-1996 (UPDATE 07-JUN-1999) |
| Title | Trypanothione reductase signature |
| Database References |
INTERPRO; IPR001864
PDB; 1TYT; 1TYP
SCOP; 1TYT; 1TYP
CATH; 1TYP
|
| Literature References | 1. SULLIVAN, F.X. AND WALSH, C.T.
Cloning, sequencing, overproduction and purification of trypanothione
reductase from Trypanosoma cruzi.
MOL.BIOCHEM.PARASITOL. 44 145-147 (1991).
2. LANTWIN, C.B., SCHLICHTING, I., KABSCH, W., PAI, E.F. AND
KRAUTH-SIEGEL, R.L.
The structure of Trypanosoma cruzi trypanothione reductase in the oxidized
and NADPH reduced state.
PROTEINS 18 161-173 (1994).
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| Documentation | Trypanothione reductase from leishmania, and African and South American
trypanosomes, has been purified and characterised [1]. The enzymes have
similar physical, mechanistic and kinetic properties, and are members of
the flavoprotein disulphide oxidoreductase family. Trypanothione is the
parasite analogue of glutathione, hence this enzyme is equivalent to
glutathione reductase. It catalyses the reaction:
NADPH + trypanothione = NADP(+) + reduced trypanothione
Trypanothione reductase shows pronounced specificty for its disulphide
substrates, trypanothione disulphide or glutathionylspermidine disulphide.
The 3D structure of the enzyme has been determined and its mode of
substrate binding revealed in detail [2], offering hope for the design of
drugs to combat Chagas disease. The structure belongs to the alpha+beta
class, i.e. with mainly anti-parallel beta-sheets separated by alpha and
beta regions. It contains an alpha-beta sandwich characteristic of
FAD/NAD-linked reductases and a C-terminal dimerisation domain.
TRYPANRDTASE is a 5-element fingerprint that provides a signature for
trypanothione reductase. The fingerprint was derived from an initial
alignment of 8 sequences: the motifs were drawn from conserved regions
within the N-terminal half of the alignment, i.e. away from the domains
that characterise the rest of the flavoprotein disulphide oxidoreductase
family. Two iterations on OWL27.0 were required to reach convergence, at
which point a true set comprising 10 sequences was identified.
An update on SPTR57.15_40.15f identified a true set of 13 sequences, and
a single partial match (Q95PT6_LEIDO), which is a trypanothione reductase
from Leishmania donovani that fails to match motif 3.
|
| Summary Information | 5 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
|
| Composite Feature Index | | 6 | 5 | 5 | 5 | 5 | 5 | 5 | | 5 | 0 | 0 | 0 | 0 | 0 | 0 | | 4 | 0 | 0 | 0 | 0 | 0 | 0 | | 3 | 0 | 0 | 0 | 0 | 0 | 0 | | 2 | 0 | 0 | 0 | 0 | 0 | 0 | | 1 | 2 | 3 | 4 | 5 | 6 |
|
| True Positives | TYTR_CRIFA TYTR_LEIDO TYTR_TRYBB TYTR_TRYCO
TYTR_TRYCR |
| Sequence Titles | TYTR_CRIFA TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTATHIONYL)SPERMIDINE REDUCTASE) - CRITHIDIA FASCICULATA.
TYTR_LEIDO TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTATHIONYL)SPERMIDINE REDUCTASE) - LEISHMANIA DONOVANI.
TYTR_TRYBB TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTATHIONYL)SPERMIDINE REDUCTASE) - TRYPANOSOMA BRUCEI BRUCEI.
TYTR_TRYCO TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTATHIONYL)SPERMIDINE REDUCTASE) - TRYPANOSOMA CONGOLENSE.
TYTR_TRYCR TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTATHIONYL)SPERMIDINE REDUCTASE) - TRYPANOSOMA CRUZI.
|
| Scan History | OWL27_0 2 50 NSINGLE
SPTR37_9f 2 7 NSINGLE
|
| Initial Motifs | Motif 1 width=20
Element Seqn Id St Int Rpt
KKVAVVDVQATHGPPALVAL TYTR_LEIDO 29 29 -
KRVAVIDLQKHHGPPHYAAL TYTR_CRIFA 29 29 -
KRVAVIDVQMVHGPPFFSAL TYTR_TRYCR 30 30 -
KRVAVVDVQTVHGPPFFAAL TYTR_TRYCO 29 29 -
KRVAVIDVQMVHGPPFFSAL TRBTRYREDA 22 22 -
KRVAVIDLQKHHGPPHYAAL TRFTRPREDB 29 29 -
KRVAVIDVQMVHGPPFFSAL TCTRYRED 30 30 -
KRVAVIDLQKHHGPPHYAAL TRFTRPREDC 29 29 -
Motif 2 width=21
Element Seqn Id St Int Rpt
VTGANYMDTIRESAGFGWELD TRFTRPREDB 64 15 -
VTGAQYMEHLRESAGFGWEFD TCTRYRED 65 15 -
VTGAQYMEHLRESAGFGWEFD TRBTRYREDA 57 15 -
VTGANYMDTIRESAGFGWELD TRFTRPREDC 64 15 -
VTGAQYMDQLRESAGFGWEFD TYTR_TRYCO 64 15 -
VTGAQYMEHLRESAGFGWEFD TYTR_TRYCR 65 15 -
VTGANYMDTIRESAGFGWELD TYTR_CRIFA 64 15 -
VTGAQYMDLIRESGGFGWEMD TYTR_LEIDO 64 15 -
Motif 3 width=19
Element Seqn Id St Int Rpt
INDSYEGMFADTEGLTFHQ TRFTRPREDC 106 21 -
INESYKSMFADTEGLSFHM TYTR_LEIDO 106 21 -
INDSYEGMFADTEGLTFHQ TYTR_CRIFA 106 21 -
INKSYEEMFRDTEGLEFFL TYTR_TRYCR 107 21 -
INKSYEDMFKDTEGLEFFL TYTR_TRYCO 106 21 -
INKSYDEMFRDTEGLEFFL TCTRYRED 107 21 -
INKSYDEMFRDTEGLEFFL TRBTRYREDA 99 21 -
INDSYEGMFADTEGLTFHQ TRFTRPREDB 106 21 -
Motif 4 width=20
Element Seqn Id St Int Rpt
AYKARGGQVDLAYRGDMILR TRFTRPREDC 209 84 -
AYKPVGGKVTLCYRNNPILR TYTR_TRYCO 209 84 -
AYKPKDGQVTLCYRGEMILR TYTR_TRYCR 210 84 -
AYKARGGQVDLAYRGDMILR TYTR_CRIFA 209 84 -
GYKPCGGYVDLCYRGDLILR TYTR_LEIDO 209 84 -
AYKPKDGQVTLCYRGEMILR TCTRYRED 210 84 -
AYKPKDGQVTLCYRGEMILR TRBTRYREDA 202 84 -
AYKARGGQVDLAYRGDMILR TRFTRPREDB 209 84 -
Motif 5 width=21
Element Seqn Id St Int Rpt
LRQELTKQLVANGIDIMTNEN TYTR_TRYCO 234 5 -
LRKQLTEQLRANGINVRTHEN TRFTRPREDC 234 5 -
LRKQLTEQLRANGINVRTHEN TRFTRPREDB 234 5 -
LREELTKQLTANGIQILTKEN TRBTRYREDA 227 5 -
LREELTKQLTANGIQILTKEN TYTR_TRYCR 235 5 -
LRKQLTEQLRANGINVRTHEN TYTR_CRIFA 234 5 -
VRKSLTKQLGANGIRVRTNLN TYTR_LEIDO 234 5 -
LREELTKQLTANGIQILTKEN TCTRYRED 235 5 -
Motif 6 width=11
Element Seqn Id St Int Rpt
NHVHFNDGTEE TYTR_LEIDO 266 11 -
RHVVFESGAEA TRFTRPREDC 266 11 -
RHVVFESGAEA TRFTRPREDB 266 11 -
KSVTFESGKKM TRBTRYREDA 259 11 -
KHVTFESGKTL TYTR_TRYCO 266 11 -
KSVTFESGKKM TYTR_TRYCR 267 11 -
RHVVFESGAEA TYTR_CRIFA 266 11 -
KSVTFESGKKM TCTRYRED 267 11 -
|
| Final Motifs | Motif 1 width=20
Element Seqn Id St Int Rpt
KRVAVVDVQTVHGPPFFAAL TYTR_TRYCO 29 29 -
KRVAVIDVQTHHGPPHYAAL TYTR_TRYBB 29 29 -
KRVAVIDVQMVHGPPFFSAL TYTR_TRYCR 30 30 -
KRVAVIDLQKHHGPPHYAAL TYTR_CRIFA 29 29 -
KKVAVVDVQATHGPPALVAL TYTR_LEIDO 29 29 -
Motif 2 width=21
Element Seqn Id St Int Rpt
VTGAQYMDQLRESAGFGWEFD TYTR_TRYCO 64 15 -
VTGAQYMDHLRESAGFGWEFD TYTR_TRYBB 64 15 -
VTGAQYMEHLRESAGFGWEFD TYTR_TRYCR 65 15 -
VTGANYMDTIRESAGFGWELD TYTR_CRIFA 64 15 -
VTGAQYMDLIRESGGFGWEMD TYTR_LEIDO 64 15 -
Motif 3 width=19
Element Seqn Id St Int Rpt
INKSYEDMFKDTEGLEFFL TYTR_TRYCO 106 21 -
INKSYEGMFNDTEGLDFFL TYTR_TRYBB 106 21 -
INKSYEEMFRDTEGLEFFL TYTR_TRYCR 107 21 -
INDSYEGMFADTEGLTFHQ TYTR_CRIFA 106 21 -
INESYKSMFADTEGLSFHM TYTR_LEIDO 106 21 -
Motif 4 width=20
Element Seqn Id St Int Rpt
AYKPVGGKVTLCYRNNPILR TYTR_TRYCO 209 84 -
AYKPPGGKVTLCYRNNLILR TYTR_TRYBB 209 84 -
AYKPKDGQVTLCYRGEMILR TYTR_TRYCR 210 84 -
AYKARGGQVDLAYRGDMILR TYTR_CRIFA 209 84 -
GYKPCGGYVDLCYRGDLILR TYTR_LEIDO 209 84 -
Motif 5 width=21
Element Seqn Id St Int Rpt
LRQELTKQLVANGIDIMTNEN TYTR_TRYCO 234 5 -
IREEVTKQLTANGIEIMTNEN TYTR_TRYBB 234 5 -
LREELTKQLTANGIQILTKEN TYTR_TRYCR 235 5 -
LRKQLTEQLRANGINVRTHEN TYTR_CRIFA 234 5 -
VRKSLTKQLGANGIRVRTNLN TYTR_LEIDO 234 5 -
Motif 6 width=11
Element Seqn Id St Int Rpt
KHVTFESGKTL TYTR_TRYCO 266 11 -
KHVTFESGKTL TYTR_TRYBB 266 11 -
KSVTFESGKKM TYTR_TRYCR 267 11 -
RHVVFESGAEA TYTR_CRIFA 266 11 -
NHVHFNDGTEE TYTR_LEIDO 266 11 -
|