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PR00999

Identifier
FUNGALYSIN  [View Relations]  [View Alignment]  
Accession
PR00999
No. of Motifs
10
Creation Date
21-DEC-1998  (UPDATE 07-JUN-1999)
Title
Fungalysin metallopeptidase (M36) signature
Database References

PROSITE; PS00142 ZINC_PROTEASE
BLOCKS; BL00142
PFAM; PF00099 zn-protease
INTERPRO; IPR001842
Literature References
1. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of metallopeptidases.
METHODS ENZYMOL. 248 183-228 (1995).
 
2. RAWLINGS, N.D. AND BARRETT, A.J.
MEROPS - Peptidase Database
http://www.bi.bbsrc.ac.uk/merops/merops.htm
 
3. RAWLINGS, N.D. AND BARRETT, A.J.
Family M36 - Clan MA - Fungalysin
http://www.bi.bbsrc.ac.uk/merops/famcards/m36.htm
 
4. BARRETT, A.J., RAWLINGS, N.D. AND WOESSNER, J.F.
Fungalysin.
IN HANDBOOK OF PROTEOLYTIC ENZYMES, ACADEMIC PRESS, 1998, CHAPTER 514, 
PP.1498-1499.

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]. The 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 [1,2].
 
Fungalysin is a zinc-containing metallopeptidase that belongs to the M36 
family of clan MA [3]. It is produced by fungi (Apergillus and other
species) to aid degradation of host lung cell walls on infection. The
enzyme is a 42kDa single chain protein, with a pH optimum of 7.5-8.0 and
optimal temperature of 60 celcius [4].
 
FUNGALYSIN is a 10-element fingerprint that provides a signature for
fungalysin (M36) metallopeptidases. The fingerprint was derived from an
initial alignment of 3 sequences: the motifs were drawn from conserved
regions spanning virtually the full alignment length - motif 8 includes
the region encoded by PROSITE pattern ZINC_PROTEASE (PS00142), which
describes the HEXXH active site; and motif 9 contains the zinc-binging Glu,
and active site Tyr and Asp residues. A single iteration on OWL31.1 was 
required to reach convergence, no further sequences being identified
beyond the starting set. 
 
An update on SPTR37_9f identified a true set of 2 sequences.
Summary Information
2 codes involving 10 elements
0 codes involving 9 elements
0 codes involving 8 elements
0 codes involving 7 elements
0 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
102222222222
90000000000
80000000000
70000000000
60000000000
50000000000
40000000000
30000000000
20000000000
12345678910
True Positives
ELM1_ASPFU    ELM2_ASPFU    
Sequence Titles
ELM1_ASPFU  EXTRACELLULAR ELASTINOLYTIC METALLOPROTEINASE PRECURSOR (EC 3.4.24.-) - ASPERGILLUS FUMIGATUS (SARTORYA FUMIGATA). 
ELM2_ASPFU EXTRACELLULAR ELASTINOLYTIC METALLOPROTEINASE PRECURSOR (EC 3.4.24.-) - ASPERGILLUS FUMIGATUS (SARTORYA FUMIGATA).
Scan History
OWL31_1    1  30   NSINGLE    
SPTR37_9f 2 3 NSINGLE
Initial Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
ATFRVVDDHYVGDNGVAHV ELM2_ASPFU 82 82 -
ATFRVVDDHYVGDNGVAHV ELM1_ASPFU 82 82 -
ATFRMVTDHYVGSNGIAHV A41504 84 84 -

Motif 2 width=23
Element Seqn Id St Int Rpt
LTKRDEKDPVDALKDTVDVLSLP A41504 144 41 -
LTKRDFSDPVTALKGTTNTLQLP ELM2_ASPFU 144 43 -
LTKRDFSDPVTALKGTTNTLQLP ELM1_ASPFU 144 43 -

Motif 3 width=19
Element Seqn Id St Int Rpt
YVFKGVSGTVSDPKAKLVY ELM2_ASPFU 183 16 -
YTFTGTKGTVSKPEAKLTY A41504 182 15 -
YVFKGVSGTVSDPKPKLVY ELM1_ASPFU 183 16 -

Motif 4 width=23
Element Seqn Id St Int Rpt
WRVETDIDSNWLLTYIDAKSGEE ELM1_ASPFU 213 11 -
WRVETDIDSNWLLTYIDAKSGEE ELM2_ASPFU 213 11 -
WRVETDIVDNWLLTYVNAAKTDE A41504 212 11 -

Motif 5 width=20
Element Seqn Id St Int Rpt
EFTWLSDGSNNYTTTRGNNG A41504 275 40 -
EFTWISDGSTNYTTSRGNNG ELM2_ASPFU 275 39 -
EFTWISDGSTNYTTSRGNNG ELM1_ASPFU 276 40 -

Motif 6 width=21
Element Seqn Id St Int Rpt
SSLSFKYPYSVSSSPPSSYID ELM1_ASPFU 316 20 -
PSLKFEYDYSTSTTTPTTYRD A41504 315 20 -
SSLSFKYPYSVSSSPPSSYID ELM2_ASPFU 315 20 -

Motif 7 width=21
Element Seqn Id St Int Rpt
GNDYVILNAQDGSGTNNANFA ELM2_ASPFU 375 39 -
GNDMVILNAQDGSGTNNANFA A41504 375 39 -
GNDYVILNAQDGSGTNNANFA ELM1_ASPFU 376 39 -

Motif 8 width=21
Element Seqn Id St Int Rpt
STPQRDCSFDAGVVIHEYTHG A41504 413 17 -
STPYRNGSFEAGIVIHEYTHG ELM1_ASPFU 414 17 -
STPYRDGSFEAGIVIHEYTHG ELM2_ASPFU 413 17 -

Motif 9 width=23
Element Seqn Id St Int Rpt
PANSGCLPGGESGGMGEGWGDFM A41504 442 8 -
PANSNSLYALESGGMGEGWSDFM ELM1_ASPFU 443 8 -
PANSNCLNALESGGMGEGWSDFM ELM2_ASPFU 459 25 -

Motif 10 width=23
Element Seqn Id St Int Rpt
QARDAIIDADTALTKGANKCEIW A41504 581 116 -
QARDAILDADTALTGGENQCEIW ELM2_ASPFU 597 115 -
QARDAILDADTALTGGENQCEIW ELM1_ASPFU 582 116 -
Final Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
ATFRVVDDHYVGDNGVAHV ELM1_ASPFU 82 82 -
ATFRVVDDHYVGDNGVAHV ELM2_ASPFU 82 82 -

Motif 2 width=23
Element Seqn Id St Int Rpt
LTKRDFSDPVTALKGTTNTLQLP ELM1_ASPFU 144 43 -
LTKRDFSDPVTALKGTTNTLQLP ELM2_ASPFU 144 43 -

Motif 3 width=19
Element Seqn Id St Int Rpt
YVFKGVSGTVSDPKPKLVY ELM1_ASPFU 183 16 -
YVFKGVSGTVSDPKAKLVY ELM2_ASPFU 183 16 -

Motif 4 width=23
Element Seqn Id St Int Rpt
WRVETDIDSNWLLTYIDAKSGEE ELM1_ASPFU 213 11 -
WRVETDIDSNWLLTYIDAKSGEE ELM2_ASPFU 213 11 -

Motif 5 width=20
Element Seqn Id St Int Rpt
EFTWISDGSTNYTTSRGNNG ELM1_ASPFU 276 40 -
EFTWISDGSTNYTTSRGNNG ELM2_ASPFU 275 39 -

Motif 6 width=21
Element Seqn Id St Int Rpt
SSLSFKYPYSVSSSPPSSYID ELM1_ASPFU 316 20 -
SSLSFKYPYSVSSSPPSSYID ELM2_ASPFU 315 20 -

Motif 7 width=21
Element Seqn Id St Int Rpt
GNDYVILNAQDGSGTNNANFA ELM1_ASPFU 376 39 -
GNDYVILNAQDGSGTNNANFA ELM2_ASPFU 375 39 -

Motif 8 width=21
Element Seqn Id St Int Rpt
STPYRNGSFEAGIVIHEYTHG ELM1_ASPFU 414 17 -
STPYRDGSFEAGIVIHEYTHG ELM2_ASPFU 413 17 -

Motif 9 width=23
Element Seqn Id St Int Rpt
PANSNSLYALESGGMGEGWSDFM ELM1_ASPFU 443 8 -
PANSNCLNALESGGMGEGWSDFM ELM2_ASPFU 459 25 -

Motif 10 width=23
Element Seqn Id St Int Rpt
QARDAILDADTALTGGENQCEIW ELM1_ASPFU 582 116 -
QARDAILDADTALTGGENQCEIW ELM2_ASPFU 597 115 -