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PR00768

Identifier
DEUTEROLYSIN  [View Relations]  [View Alignment]  
Accession
PR00768
No. of Motifs
5
Creation Date
30-JAN-1997  (UPDATE 07-JUN-1999)
Title
Deuterolysin metalloprotease (M35) family signature
Database References

PROSITE; PS00142 ZINC_PROTEASE
BLOCKS; BL00142
INTERPRO; IPR001384
Literature References
1. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of metallopeptidases.
METHODS ENZYMOL. 248 183-228 (1995).
 
2. TATSUMI, H., MURAKAMI, S., TSUJI, R.F., ISHIDA, Y., MURAKAMI, K., MASAKI,
A., KAWABE, H., ARIMURA., H., NAKANO, E. AND MOTAI, H.
Cloning and expression in yeast of a cDNA clone encoding Aspergillus oryzae
neutral protease II, a unique metalloprotease.
MOL.GEN.GENET. 228 97-103 (1991).
 
3. MATSUMOTO, K., YAMAGUCHI, M. AND ICHISHIMA, E.
Molecular cloning and nucletide sequence of the complementary DNA for
penicillinolysin gene plnC, and 18kDa metalloendopeptidase gene from 
Penicillium citrinum.
BIOCHIM.BIOPHYS.ACTA 1218(3) 469-472 (1994).

Documentation
Metalloproteases are the most diverse of the four main types of protease,
with more than 30 families identified to date [1]. Of these, around
half contain the HEXXH motif, which has been shown in crystallographic
studies to form part of the metal-binding site [1]. This HEXXH motif is 
relatively common, but can be more stringently defined for metallo-
proteases as abXHEbbHbc, where a is most often valine or threonine and 
forms part of the S1' subsite in thermolysin and neprilysin, b is an
uncharged residue, and c a hydrophobic residue. Proline is never found
in this site, possibly because it would break the helical structure
adopted by this motif in metalloproteases [1].
 
Metalloproteases can be split into five groups on the basis of their metal-
binding residues: the first three contain the HEXXH motif, the other two
do not [1]. In the first group, a glutamic acid completes the active site -
these are termed HEXXH+E: all families in this group show some sequence
relationship and have been assigned to clan MA [1]. The second group, which
have a third histidine as the extra metal-binding residue, are termed
HEXXH+H and are grouped into clan MB on the basis of their inter-relation-
ship [1]. In the third group, the additional metal-binding residues are
unidentified. The fourth group is diverse - the metal-binding residues are
known but do not form the HEXXH motif. And the fifth group comprises the
remaining families where the metal-binding residues are as yet unknown [1].
 
Deuterolysin is a microbial zinc-containing metalloprotease that shows 
some similarity to thermolysin [2]. The protein is expressed with a
possible 19-residue signal sequence, a 155-residue propeptide, and an
active peptide of 177 residues [3]. The latter contains an HEXXH motif
towards the C-terminus, but the other zinc ligands are as yet undetermined
[2,3].
 
DEUTEROLYSIN is a 5-element fingerprint that provides a signature for the
deuterolysin (M35) family of metalloproteases. The fingerprint was derived
from an initial alignment of 3 sequences: the motifs were drawn from
virtually the full length of the active peptide, motif 1 containing a
conserved Glu residue that may contribute to zinc binding, and motif 4
including the region encoded by PROSITE pattern ZINC_PROTEASE (PS00142),
which contains the HEXXH motif. Two iterations on OWL29.3 were required to
reach convergence, at which point a true set comprising 4 sequences was
identified.
 
An update on SPTR37_9f identified a true set of 4 sequences.
Summary Information
4 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
544444
400000
300000
200000
12345
True Positives
ME24_ASPFL    NPII_ASPOR    PLNC_PENCI    Q09016        
Sequence Titles
ME24_ASPFL  24 KD METALLOPROTEINASE PRECURSOR (EC 3.4.24.39) (DEUTEROLYSIN) - ASPERGILLUS FLAVUS. 
NPII_ASPOR NEUTRAL PROTEASE II PRECURSOR (EC 3.4.24.39) (DEUTEROLYSIN) (NPII) - ASPERGILLUS ORYZAE.
PLNC_PENCI PENICILLOLYSIN PRECURSOR (EC 3.4.24.39) (DEUTEROLYSIN) - PENICILLIUM CITRINUM.
Q09016 MEP20 - ASPERGILLUS FUMIGATUS (SARTORYA FUMIGATA).
Scan History
OWL29_3    2  100  NSINGLE    
SPTR37_9f 2 5 NSINGLE
Initial Motifs
Motif 1  width=30
Element Seqn Id St Int Rpt
LKNTVSLANQAASAAQSGSSSRFQEYFKTT ME24_ASPFL 211 211 -
LSNTVKLANAAATAARSGSASKFSEYFKTT PLNC_PENCI 192 192 -
LSNAAKLANQAAEAAESGDESKFEEYFKTT NPII_ASPOR 193 193 -

Motif 2 width=26
Element Seqn Id St Int Rpt
RTSVAARFRAVASEASSTSSGSTTYY ME24_ASPFL 245 4 -
RSVVAARLEAVAKEAQSASSGSTTYY PLNC_PENCI 226 4 -
RTTVAERLRAVAKEAGSTSGGSTTYH NPII_ASPOR 227 4 -

Motif 3 width=30
Element Seqn Id St Int Rpt
CTDTYGYCSSNVPGVHLPAYNIIANCDIYY ME24_ASPFL 271 0 -
CSDTLGYCETNVLAYTLPARNIIANCDIYY PLNC_PENCI 252 0 -
CNDPYGYCEPNVLAYTLPSKNEIANCDIYY NPII_ASPOR 253 0 -

Motif 4 width=29
Element Seqn Id St Int Rpt
LTRTCHAQDQATTTLHEFTHAPGVYSPGT ME24_ASPFL 306 5 -
LAGTCHQQDQATTTLHEFTHAPGVYSPGT PLNC_PENCI 287 5 -
LAQKCHAQDQATTTLHEFTHAPGVYQPGT NPII_ASPOR 288 5 -

Motif 5 width=30
Element Seqn Id St Int Rpt
DDLGYGYDAATALSSSQALNNVDTYALFAN ME24_ASPFL 335 0 -
DDLGYGYSAATSLSSSQAVLNADSYALYAN PLNC_PENCI 316 0 -
EDLGYGYDAATQLSAQDALNNADSYALYAN NPII_ASPOR 317 0 -
Final Motifs
Motif 1  width=30
Element Seqn Id St Int Rpt
LKNTVSLANQAASAAQSGSSSRFQEYFKTT ME24_ASPFL 211 211 -
LSNTVKLANAAATAARSGSASKFSEYFKTT PLNC_PENCI 192 192 -
LSNAAKLANQAAEAAESGDESKFEEYFKTT NPII_ASPOR 193 193 -
LRNAGSLANAAASAASSGSSTRFQEYFKTT Q09016 190 190 -

Motif 2 width=26
Element Seqn Id St Int Rpt
RTSVAARFRAVASEASSTSSGSTTYY ME24_ASPFL 245 4 -
RSVVAARLEAVAKEAQSASSGSTTYY PLNC_PENCI 226 4 -
RTTVAERLRAVAKEAGSTSGGSTTYH NPII_ASPOR 227 4 -
PENVGGRFRAVGREASSQSSGKTTYY Q09016 223 3 -

Motif 3 width=30
Element Seqn Id St Int Rpt
CTDTYGYCSSNVPGVHLPAYNIIANCDIYY ME24_ASPFL 271 0 -
CSDTLGYCETNVLAYTLPARNIIANCDIYY PLNC_PENCI 252 0 -
CNDPYGYCEPNVLAYTLPSKNEIANCDIYY NPII_ASPOR 253 0 -
CNDPYGYCDSNTLAYTLPSSNLIANCDIYY Q09016 249 0 -

Motif 4 width=29
Element Seqn Id St Int Rpt
LTRTCHAQDQATTTLHEFTHAPGVYSPGT ME24_ASPFL 306 5 -
LAGTCHQQDQATTTLHEFTHAPGVYSPGT PLNC_PENCI 287 5 -
LAQKCHAQDQATTTLHEFTHAPGVYQPGT NPII_ASPOR 288 5 -
LTSSCHAQDQATTTLHEFTHAPAVYSPGT Q09016 284 5 -

Motif 5 width=30
Element Seqn Id St Int Rpt
DDLGYGYDAATALSSSQALNNVDTYALFAN ME24_ASPFL 335 0 -
DDLGYGYSAATSLSSSQAVLNADSYALYAN PLNC_PENCI 316 0 -
EDLGYGYDAATQLSAQDALNNADSYALYAN NPII_ASPOR 317 0 -
DDYAYGYRASTALSASQALLNADTYALFAN Q09016 313 0 -