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PR00129

Identifier
CUTINASE  [View Relations]  [View Alignment]  
Accession
PR00129
No. of Motifs
5
Creation Date
26-FEB-1994  (UPDATE 14-JUN-1999)
Title
Cutinase signature
Database References

PROSITE; PS00155 CUTINASE_1; PS00931 CUTINASE_2
BLOCKS; BL00155
PFAM; PF01083 Cutinase
INTERPRO; IPR000675
PDB; 1CUS
SCOP; 1CUS
Literature References
1. ETTINGER, W.F., THUKRAL, S.K. AND KOLATTUKUDY, P.E.
Structure of cutinase gene, cDNA, and the derived amino acid sequence from
phytopathogenic fungi.
BIOCHEMISTRY 26(24) 7883-7892 (1987).
 
2. SWEIGARD, J.A., CHUMLEY, F.G. AND VALENT, B.
Cloning and analysis of cut1, a cutinase gene from Magnaporthe grisea.
MOL.GEN.GENET. 232(2) 174-182 (1992).
 
3. MARTINEZ, C., DE GEUS, P., LAUWEREYS, M., MATTHYSSENS, G. AND
CAMBILLAU, C.
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine 
accessible to solvent.
NATURE 356 615-618 (1992).

Documentation
Aerial plant organs are protected by a cuticle composed of an insoluble
polymeric structural compound, cutin, which is a polyester composed of
hydroxy and hydroxyepoxy fatty acids [1]. Plant pathogenic fungi produce
extracellular degradative enzymes [2] that play an important role in
pathogenesis: they include cutinase, which hydrolyses cutin, facilitating
fungus penetration through the cuticle [1,2]. Inhibition of the enzyme can
prevent fungal infection through intact cuticles [1]. Cutin monomers
released from the cuticle by small amounts of cutinase on fungal spore
surfaces can greatly increase the amount of cutinase secreted by the spore,
the mechanism for which process is as yet unknown [1,2].
 
Cutinase is a serine esterase containing the classical Ser, His, Asp triad
of serine hydrolases [1]. The protein belongs to the alpha-beta class,
with a central beta-sheet of 5 parallel strands covered by 5 helices on
either side of the sheet [3]. The active site cleft is partly covered by 2
thin bridges formed by amino acid side chains, by contrast with the hydro-
phobic lid possessed by other lipases [3]. The protein also contains 2
disulphide bridges, which are essential for activity, their cleavage 
resulting in complete loss of enzymatic activity [1].
 
CUTINASE is a 5-element fingerprint that provides a signature for the
cutinases. The fingerprint was derived from an initial alignment of 5
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, motifs 4 and 5 including the regions encoded by
PROSITE patterns CUTINASE_1 (PS00155) and CUTINASE_2 (PS00931), which
contain the Ser residue, and the Asp and His residues of the catalytic triad
respectively. Two iterations on OWL22.1 were required to reach convergence,
at which point a true set comprising 8 sequences was identified.
 
An update on SPTR37_9f identified a true set of 8 sequences, and 1
partial match.
Summary Information
   8 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
1 codes involving 2 elements
Composite Feature Index
588888
400000
300000
200011
12345
True Positives
CUTI_ALTBR    CUTI_ASCRA    CUTI_ASPOR    CUTI_COLCA    
CUTI_COLGL CUTI_FUSSC CUTI_FUSSO CUTI_MAGGR
True Positive Partials
Codes involving 2 elements
CUTI_BOTCI
Sequence Titles
CUTI_ALTBR  CUTINASE PRECURSOR (EC 3.1.1.-) - ALTERNARIA BRASSICICOLA. 
CUTI_ASCRA CUTINASE PRECURSOR (EC 3.1.1.-) - ASCOCHYTA RABIEI.
CUTI_ASPOR CUTINASE PRECURSOR (EC 3.1.1.-) (L1) - ASPERGILLUS ORYZAE.
CUTI_COLCA CUTINASE PRECURSOR (EC 3.1.1.-) - COLLETOTRICHUM CAPSICI (ANTHRACNOSE FUNGUS).
CUTI_COLGL CUTINASE PRECURSOR (EC 3.1.1.-) - COLLETOTRICHUM GLOEOSPORIOIDES (ANTHRACNOSE FUNGUS) (GLOMERELLA CINGULATA).
CUTI_FUSSC CUTINASE PRECURSOR (EC 3.1.1.-) - FUSARIUM SOLANI (SUBSP. CUCURBITAE) (NECTRIA IPOMOEAE).
CUTI_FUSSO CUTINASE PRECURSOR (EC 3.1.1.-) - FUSARIUM SOLANI (SUBSP. PISI) (NECTRIA HAEMATOCOCCA).
CUTI_MAGGR CUTINASE PRECURSOR (EC 3.1.1.-) - MAGNAPORTHE GRISEA (RICE BLAST FUNGUS).

CUTI_BOTCI CUTINASE PRECURSOR (EC 3.1.1.-) - BOTRYTIS CINEREA (BOTRYOTINIA FUCKELIANA).
Scan History
OWL22_1    2  100  NSINGLE    
OWL26_0 1 100 NSINGLE
SPTR37_9f 2 50 NSINGLE
Initial Motifs
Motif 1  width=11
Element Seqn Id St Int Rpt
SAGPIVADALE CUTI_COLGL 66 66 -
SAGPAVASALE CUTI_ASCRA 66 66 -
SAGPIVADALE CUTI_COLCA 69 69 -
SAGTNVASRLE CUTI_MAGGR 3 3 -
TLGPSIASNLE CUTI_FUSSO 66 66 -

Motif 2 width=18
Element Seqn Id St Int Rpt
VWVQGVGGPYLADLASNF CUTI_COLGL 84 7 -
IWVQGVGGPYTADLPSNF CUTI_ASCRA 83 6 -
VWVQGVGGPYSADLASNF CUTI_COLCA 87 7 -
IWVQGVGDPYDAALSPNF CUTI_MAGGR 20 6 -
VWIQGVGGAYRATLGDNA CUTI_FUSSO 84 7 -

Motif 3 width=21
Element Seqn Id St Int Rpt
LPDGTSSAAINEARRLFTLAN CUTI_COLGL 102 0 -
LPGGTSQSAINEAVRLFNEAN CUTI_ASCRA 101 0 -
IPEGTSRVAINEAKRLFTLAN CUTI_COLCA 106 1 -
LPAGTTQGAIDEAKRMFTLAN CUTI_MAGGR 38 0 -
LPRGTSSAAIREMLGLFQQAN CUTI_FUSSO 102 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
TKCPNAAIVSGGYSQGTAVM CUTI_COLGL 123 0 -
TKCPSTPIVAGGYSQGTAVM CUTI_ASCRA 122 0 -
TKCPNSAVVAGGYSQGTAVM CUTI_COLCA 127 0 -
TKCPNAAVVAGGYSQGTAVM CUTI_MAGGR 59 0 -
TKCPDATLIAGGYSQGAALA CUTI_FUSSO 123 0 -

Motif 5 width=26
Element Seqn Id St Int Rpt
VYCDIADAVCYGTLFILPAHFLYQTD CUTI_COLGL 185 42 -
VYCEVGDLVCDGTLIITVSHFLYLEE CUTI_ASCRA 183 41 -
VYCALADAVCYGTLFILPAHFLYQAD CUTI_COLCA 189 42 -
VYCNASDAVCFGTLFLLPAHFLYTTE CUTI_MAGGR 121 42 -
VFCNTGDLVCTGSLIVAAPHLAYGPD CUTI_FUSSO 185 42 -
Final Motifs
Motif 1  width=11
Element Seqn Id St Int Rpt
SAGPIVADALE CUTI_COLGL 66 66 -
SAGPAVASALE CUTI_ASCRA 66 66 -
SAGPIVADALE CUTI_COLCA 69 69 -
LVGPFTANALE CUTI_ALTBR 49 49 -
SAGTNVASRLE CUTI_MAGGR 3 3 -
TLGPSIASNLE CUTI_FUSSC 66 66 -
TLGPSIASNLE CUTI_FUSSO 66 66 -
STGPAVCNRLK CUTI_ASPOR 57 57 -

Motif 2 width=18
Element Seqn Id St Int Rpt
VWVQGVGGPYLADLASNF CUTI_COLGL 84 7 -
IWVQGVGGPYTADLPSNF CUTI_ASCRA 83 6 -
VWVQGVGGPYSADLASNF CUTI_COLCA 87 7 -
VWVQGVGGPYTAGLVENA CUTI_ALTBR 67 7 -
IWVQGVGDPYDAALSPNF CUTI_MAGGR 20 6 -
VWIQGVGGAYRATLGDNA CUTI_FUSSC 84 7 -
VWIQGVGGAYRATLGDNA CUTI_FUSSO 84 7 -
VACQGVGPRYTADLPSNA CUTI_ASPOR 74 6 -

Motif 3 width=21
Element Seqn Id St Int Rpt
LPDGTSSAAINEARRLFTLAN CUTI_COLGL 102 0 -
LPGGTSQSAINEAVRLFNEAN CUTI_ASCRA 101 0 -
IPEGTSRVAINEAKRLFTLAN CUTI_COLCA 106 1 -
LPAGTSQAAIREAQRLFNLAA CUTI_ALTBR 85 0 -
LPAGTTQGAIDEAKRMFTLAN CUTI_MAGGR 38 0 -
LPRGTSSAAIREMLGLFQQAN CUTI_FUSSC 102 0 -
LPRGTSSAAIREMLGLFQQAN CUTI_FUSSO 102 0 -
LPEGTSQAAIAEAQGLFEQAV CUTI_ASPOR 92 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
TKCPNAAIVSGGYSQGTAVM CUTI_COLGL 123 0 -
TKCPSTPIVAGGYSQGTAVM CUTI_ASCRA 122 0 -
TKCPNSAVVAGGYSQGTAVM CUTI_COLCA 127 0 -
SKCPNTPITAGGYSQGAAVM CUTI_ALTBR 106 0 -
TKCPNAAVVAGGYSQGTAVM CUTI_MAGGR 59 0 -
TKCPDATLIAGGYSQGAALA CUTI_FUSSC 123 0 -
TKCPDATLIAGGYSQGAALA CUTI_FUSSO 123 0 -
SKCPDTQIVAGGYSQGTAVM CUTI_ASPOR 113 0 -

Motif 5 width=26
Element Seqn Id St Int Rpt
VYCDIADAVCYGTLFILPAHFLYQTD CUTI_COLGL 185 42 -
VYCEVGDLVCDGTLIITVSHFLYLEE CUTI_ASCRA 183 41 -
VYCALADAVCYGTLFILPAHFLYQAD CUTI_COLCA 189 42 -
IYCETGDLVCNGTLIITPAHLLYSDE CUTI_ALTBR 168 42 -
VYCNASDAVCFGTLFLLPAHFLYTTE CUTI_MAGGR 121 42 -
VFCNVGDLVCTGSLIVAAPHLAYGPD CUTI_FUSSC 185 42 -
VFCNTGDLVCTGSLIVAAPHLAYGPD CUTI_FUSSO 185 42 -
VYCAVGDLVCLGTLIVAPPHFSYLSD CUTI_ASPOR 175 42 -