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PR00998

Identifier
CRBOXYPTASET  [View Relations]  [View Alignment]  
Accession
PR00998
No. of Motifs
9
Creation Date
21-DEC-1998  (UPDATE 07-JUN-1999)
Title
Carboxypeptidase Taq (M32) metallopeptidase signature
Database References

PROSITE; PS00142 ZINC_PROTEASE
BLOCKS; BL00142
PFAM; PF00099 zn-protease
INTERPRO; IPR001333
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 M32 - Carboypeptidase Taq
http://www.bi.bbsrc.ac.uk/merops/famcards/m32.htm
 
4. BARRETT, A.J., RAWLINGS, N.D. AND WOESSNER, J.F.
Carboxypeptidase Taq.
IN HANDBOOK OF PROTEOLYTIC ENZYMES, ACADEMIC PRESS, 1998, CHAPTER 504, 
PP.1469-1471.

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].
 
Carboxypeptidase Taq is a zinc-containing thermostable metallopeptidase that
belongs to the M32 family [3]. It does not share any significant sequence
similarity with other carboypeptidases or metalloproteases, so has not been
assigned to a clan. It was originally discovered and purified from Thermus
aquaticus; optimal enzymatic activity occurs at 80 celcius. Although very
little is known about this enzyme, it is thought either to be associated 
with a membrane or to be particle bound [4].
 
CRBOXYPTASET is a 9-element fingerprint that provides a signature for 
the thermostable carboxypeptidase Taq (M32) family of 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 4 includes the region encoded by PROSITE pattern 
ZINC_PROTEASE (PS00142), which describes the HEXXH active site. 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 3 sequences.
Summary Information
3 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
9333333333
8000000000
7000000000
6000000000
5000000000
4000000000
3000000000
2000000000
123456789
True Positives
CTAQ_THEAQ    O58210        YPWA_BACSU    
Sequence Titles
CTAQ_THEAQ  THERMOSTABLE CARBOXYPEPTIDASE 1 (EC 3.4.17.19) (CARBOXYPEPTIDASE TAQ) - THERMUS AQUATICUS. 
O58210 515AA LONG HYPOTHETICAL THERMOSTABLE CARBOXYPEPTIDASE - PYROCOCCUS HORIKOSHII.
YPWA_BACSU HYPOTHETICAL 58.2 KD PROTEIN IN KDGT-XPT INTERGENIC REGION - BACILLUS SUBTILIS.
Scan History
OWL31_1    1  50   NSINGLE    
SPTR37_9f 2 4 NSINGLE
Initial Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
PPYGELYDALLDGYEPGARAR CTAQ_THEAQ 159 159 -
GYQEHPYDALLDLFEPGVTVK YPWA_BACSU 148 148 -
GYEEEPYDALLDLYEEGLRTR C71158 166 166 -

Motif 2 width=17
Element Seqn Id St Int Rpt
RLDVSAHPFTTEFGIRD C71158 248 61 -
RLDPTAHPFEIAIGPGD CTAQ_THEAQ 239 59 -
RLDETVHPFATTLNRGD YPWA_BACSU 228 59 -

Motif 3 width=20
Element Seqn Id St Int Rpt
VRVTTRYDEKDFRTAIFGTI YPWA_BACSU 245 0 -
VRITTRYEGFDFRRALLSTI C71158 265 0 -
VRITTRYYEDFFNAGIFGTL CTAQ_THEAQ 256 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
HECGHAIYEQNIDEALSGTN YPWA_BACSU 265 0 -
HEMGHALYEQGLPEAHWGTP CTAQ_THEAQ 276 0 -
HEFGHALYELQQDERFMFTP C71158 285 0 -

Motif 5 width=17
Element Seqn Id St Int Rpt
GVHESQSRTWENLVGRS CTAQ_THEAQ 303 7 -
GIHESQSRFWENIIGRS C71158 312 7 -
GIHESQSLFYENFIGRN YPWA_BACSU 292 7 -

Motif 6 width=20
Element Seqn Id St Int Rpt
EDFHFAVNAVEPSLIRVEAD CTAQ_THEAQ 343 23 -
EDVYLYFNMVRPDFIRTEAD C71158 352 23 -
DDFVRAINESKPSFIRVEAD YPWA_BACSU 333 24 -

Motif 7 width=18
Element Seqn Id St Int Rpt
DLPEMWNDEMERLLGIRP C71158 398 26 -
DLPSLWNQKYQDYLGITP YPWA_BACSU 379 26 -
DLPEAWREKYRAYLGVAP CTAQ_THEAQ 389 26 -

Motif 8 width=22
Element Seqn Id St Int Rpt
GILQDIHWAHGSIGYFPTYSIG C71158 421 5 -
GILQDVHWAGGDFGYFPSYALG YPWA_BACSU 402 5 -
GVMQDVHWSGGMFGYFPTYTLG CTAQ_THEAQ 412 5 -

Motif 9 width=19
Element Seqn Id St Int Rpt
KGEFEPIKSWLREKIHRWG C71158 466 23 -
RGEFTPFLDWTRRKIHAEG CTAQ_THEAQ 457 23 -
RGEFHPIKQWLTEKVHIHG YPWA_BACSU 447 23 -
Final Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
GYQEHPYDALLDLFEPGVTVK YPWA_BACSU 148 148 -
GYEEEPYDALLDLYEEGLRTR O58210 166 166 -
PPYGELYDALLDGYEPGARAR CTAQ_THEAQ 159 159 -

Motif 2 width=17
Element Seqn Id St Int Rpt
RLDETVHPFATTLNRGD YPWA_BACSU 228 59 -
RLDVSAHPFTTEFGIRD O58210 248 61 -
RLDPTAHPFEIAIGPGD CTAQ_THEAQ 239 59 -

Motif 3 width=20
Element Seqn Id St Int Rpt
VRVTTRYDEKDFRTAIFGTI YPWA_BACSU 245 0 -
VRITTRYEGFDFRRALLSTI O58210 265 0 -
VRITTRYYEDFFNAGIFGTL CTAQ_THEAQ 256 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
HECGHAIYEQNIDEALSGTN YPWA_BACSU 265 0 -
HEFGHALYELQQDERFMFTP O58210 285 0 -
HEMGHALYEQGLPEAHWGTP CTAQ_THEAQ 276 0 -

Motif 5 width=17
Element Seqn Id St Int Rpt
GIHESQSLFYENFIGRN YPWA_BACSU 292 7 -
GIHESQSRFWENIIGRS O58210 312 7 -
GVHESQSRTWENLVGRS CTAQ_THEAQ 303 7 -

Motif 6 width=20
Element Seqn Id St Int Rpt
DDFVRAINESKPSFIRVEAD YPWA_BACSU 333 24 -
EDVYLYFNMVRPDFIRTEAD O58210 352 23 -
EDFHFAVNAVEPSLIRVEAD CTAQ_THEAQ 343 23 -

Motif 7 width=18
Element Seqn Id St Int Rpt
DLPSLWNQKYQDYLGITP YPWA_BACSU 379 26 -
DLPEMWNDEMERLLGIRP O58210 398 26 -
DLPEAWREKYRAYLGVAP CTAQ_THEAQ 389 26 -

Motif 8 width=22
Element Seqn Id St Int Rpt
GILQDVHWAGGDFGYFPSYALG YPWA_BACSU 402 5 -
GILQDIHWAHGSIGYFPTYSIG O58210 421 5 -
GVMQDVHWSGGMFGYFPTYTLG CTAQ_THEAQ 412 5 -

Motif 9 width=19
Element Seqn Id St Int Rpt
RGEFHPIKQWLTEKVHIHG YPWA_BACSU 447 23 -
KGEFEPIKSWLREKIHRWG O58210 466 23 -
RGEFTPFLDWTRRKIHAEG CTAQ_THEAQ 457 23 -