WORKLIST ENTRIES (1):
THERMOPTASE View alignment Thermophilic metalloprotease (M29) signature
Type of fingerprint: COMPOUND with 8 elements
Links:
PRINTS; PR00756 ALADIPTASE; PR00791 PEPDIPTASEA; PR00730 THERMOLYSIN
PRINTS; PR00787 NEUTRALPTASE; PR00782 LSHMANOLYSIN; PR00931 MICOLLPTASE
PRINTS; PR00997 FRAGILYSIN; PR00786 NEPRILYSIN; PR00765 CRBOXYPTASEA
PRINTS; PR00932 AMINO1PTASE; PR00789 OSIALOPTASE; PR00933 BLYTICPTASE
PRINTS; PR00934 XHISDIPTASE; PR00998 CRBOXYPTASET; PR00768 DEUTEROLYSIN
PRINTS; PR00999 FUNGALYSIN; PR01000 SREBPS2PTASE
INTERPRO; IPR000787
Creation date 21-JUN-1998; UPDATE 10-JUN-1999
1. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of metallopeptidases.
METHODS ENZYMOL. 248 183-228 (1995).
2. BAIROCH, A. AND RAWLINGS, N.
Classification of peptidase families and index of peptidase entries in
SWISS-PROT.
http://expasy.hcuge.ch/cgi-bin/lists?peptidas.txt
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].
The thermophilic metallo-aminopeptidases (M29) are homo-dimeric enzymes that
fall into the latter group, in which the metal-binding residues remain
unknown.
THERMOPTASE is an 8-element fingerprint that provides a signature for
thermophilic metalloproteases (M29). The fingerprint was derived from an
initial alignment of 4 sequences: the motifs were drawn from conserved
regions spanning virtually the full alignment length. A single ieteration
on OWL30.1 was required to reach convergence, no further sequences being
identified beyond the starting set.
An update on SPTR37_9f identified a true set of 4 sequences, and 1
partial match.
SUMMARY INFORMATION
4 codes involving 8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
1 codes involving 3 elements
0 codes involving 2 elements
COMPOSITE FINGERPRINT INDEX
8| 4 4 4 4 4 4 4 4
7| 0 0 0 0 0 0 0 0
6| 0 0 0 0 0 0 0 0
5| 0 0 0 0 0 0 0 0
4| 0 0 0 0 0 0 0 0
3| 0 0 0 1 1 1 0 0
2| 0 0 0 0 0 0 0 0
--+-----------------------------------------
| 1 2 3 4 5 6 7 8
True positives..
AMPT_THETH AMPT_THEAQ AMP2_BACST AMPS_BACSU
Subfamily: Codes involving 3 elements
Subfamily True positives..
O51096
PROTEIN TITLES
AMPT_THETH AMINOPEPTIDASE T (EC 3.4.11.-) (AP-T) (HEAT STABLE AMINOPEPT
AMPT_THEAQ AMINOPEPTIDASE T (EC 3.4.11.-) (AP-T) (HEAT STABLE AMINOPEPT
AMP2_BACST AMINOPEPTIDASE II (EC 3.4.11.-) (AP-II) - BACILLUS STEAROTHE
AMPS_BACSU AMINOPEPTIDASE AMPS (EC 3.4.11.-) - BACILLUS SUBTILIS.
O51096 AMINOPEPTIDASE II - BORRELIA BURGDORFERI (LYME DISEASE SPIRO
SCAN HISTORY
OWL30_1 1 50 NSINGLE
SPTR37_9f 2 5 NSINGLE
INITIAL MOTIF SETS
THERMOPTASE1 Length of motif = 18 Motif number = 1
Thermophilic aminopeptidase motif I - 1
PCODE ST INT
AVKVGVNIQPGQTLFVNA AMP2_BACST 15 15
AVEVGVNVQKGQYVVVNA AMPS_BACSU 15 15
AIRVGLNLEEGQEIVATA AMPT_THEAQ 15 15
AIRVGLNLEKGQEVIATA AMPT_THETH 15 15
THERMOPTASE2 Length of motif = 20 Motif number = 2
Thermophilic aminopeptidase motif II - 1
PCODE ST INT
YPMLRARAMEELAEQGAAFL AMP2_BACST 80 47
YPEWEAKGREELAKNGAAFI AMPS_BACSU 80 47
APAWLYEGMAKAFHEGAARL AMPT_THEAQ 80 47
APAWLYEGMARAFREGAARL AMPT_THETH 80 47
THERMOPTASE3 Length of motif = 23 Motif number = 3
Thermophilic aminopeptidase motif III - 1
PCODE ST INT
VFGDLRDEEAIDKLWEAIFRITR AMP2_BACST 156 56
VFPGKSEEEAIHLLWEEIFKATR AMPS_BACSU 156 56
VFPGLPEEEAVQRLWQAIFQATR AMPT_THEAQ 156 56
VFPGLPEEEAVRRLWEAIFQATR AMPT_THETH 156 56
THERMOPTASE4 Length of motif = 20 Motif number = 4
Thermophilic aminopeptidase motif IV - 1
PCODE ST INT
NIPTEEVFTMPHKDGVNGTV AMP2_BACST 245 66
NMPTEEVFTLPQKDGVDGVV AMPS_BACSU 245 66
NLPTEEVFTAPHRERVEGVV AMPT_THEAQ 245 66
NLPTEEVFTAPHRERVEGVV AMPT_THETH 245 66
THERMOPTASE5 Length of motif = 21 Motif number = 5
Thermophilic aminopeptidase motif V - 1
PCODE ST INT
LKHLLDTDDGARRLGEVALVP AMP2_BACST 301 36
LKELVETDEGSHYLGEVALVP AMPS_BACSU 301 36
LKKLLDTDEGARRLGEVALVP AMPT_THEAQ 301 36
LRRLLDTDEGARRLGEVALVP AMPT_THETH 301 36
THERMOPTASE6 Length of motif = 22 Motif number = 6
Thermophilic aminopeptidase motif VI - 1
PCODE ST INT
SPVSLSNLIFYNTLFDENAACH AMP2_BACST 324 2
SPISQSNILFYNTLFDENASNH AMPS_BACSU 324 2
NPIAKTGLVFFDTLFDENAASH AMPT_THEAQ 324 2
NPIAKTGLVFFDTLFDENAASH AMPT_THETH 324 2
THERMOPTASE7 Length of motif = 23 Motif number = 7
Thermophilic aminopeptidase motif VII - 1
PCODE ST INT
SKEELDRRGVNDSLVHVDFMIGS AMP2_BACST 363 17
SREELVKEGLNESITHVDFMIGS AMPS_BACSU 363 17
SGEEFRRRGGNESMVHVDWMIGS AMPT_THEAQ 361 15
SGEAFRKRGGNESLVHVDWMIGS AMPT_THETH 361 15
THERMOPTASE8 Length of motif = 20 Motif number = 8
Thermophilic aminopeptidase motif VIII - 1
PCODE ST INT
NIDGVTKDGKREPIFRSGNW AMP2_BACST 389 3
NIDGITADGKREPIFRNGNW AMPS_BACSU 389 3
DVDGLLEDGTRVPLMRRGRW AMPT_THEAQ 387 3
DVDGLYEDGTRTPLMRRGRW AMPT_THETH 387 3
FINAL MOTIF SETS
THERMOPTASE1 Length of motif = 18 Motif number = 1
Thermophilic aminopeptidase motif I - 2
PCODE ST INT
AIRVGLNLEKGQEVIATA AMPT_THETH 15 15
AIRVGLNLEEGQEIVATA AMPT_THEAQ 15 15
AVKVGVNIQPGQTLFVNA AMP2_BACST 15 15
AVEVGVNVQKGQYVVVNA AMPS_BACSU 15 15
THERMOPTASE2 Length of motif = 20 Motif number = 2
Thermophilic aminopeptidase motif II - 2
PCODE ST INT
APAWLYEGMARAFREGAARL AMPT_THETH 80 47
APAWLYEGMAKAFHEGAARL AMPT_THEAQ 80 47
YPMLRARAMEELAEQGAAFL AMP2_BACST 80 47
YPEWEAKGREELAKNGAAFI AMPS_BACSU 80 47
THERMOPTASE3 Length of motif = 23 Motif number = 3
Thermophilic aminopeptidase motif III - 2
PCODE ST INT
VFPGLPEEEAVRRLWEAIFQATR AMPT_THETH 156 56
VFPGLPEEEAVQRLWQAIFQATR AMPT_THEAQ 156 56
VFGDLRDEEAIDKLWEAIFRITR AMP2_BACST 156 56
VFPGKSEEEAIHLLWEEIFKATR AMPS_BACSU 156 56
THERMOPTASE4 Length of motif = 20 Motif number = 4
Thermophilic aminopeptidase motif IV - 2
PCODE ST INT
NLPTEEVFTAPHRERVEGVV AMPT_THETH 245 66
NLPTEEVFTAPHRERVEGVV AMPT_THEAQ 245 66
NIPTEEVFTMPHKDGVNGTV AMP2_BACST 245 66
NMPTEEVFTLPQKDGVDGVV AMPS_BACSU 245 66
THERMOPTASE5 Length of motif = 21 Motif number = 5
Thermophilic aminopeptidase motif V - 2
PCODE ST INT
LRRLLDTDEGARRLGEVALVP AMPT_THETH 301 36
LKKLLDTDEGARRLGEVALVP AMPT_THEAQ 301 36
LKHLLDTDDGARRLGEVALVP AMP2_BACST 301 36
LKELVETDEGSHYLGEVALVP AMPS_BACSU 301 36
THERMOPTASE6 Length of motif = 22 Motif number = 6
Thermophilic aminopeptidase motif VI - 2
PCODE ST INT
NPIAKTGLVFFDTLFDENAASH AMPT_THETH 324 2
NPIAKTGLVFFDTLFDENAASH AMPT_THEAQ 324 2
SPVSLSNLIFYNTLFDENAACH AMP2_BACST 324 2
SPISQSNILFYNTLFDENASNH AMPS_BACSU 324 2
THERMOPTASE7 Length of motif = 23 Motif number = 7
Thermophilic aminopeptidase motif VII - 2
PCODE ST INT
SGEAFRKRGGNESLVHVDWMIGS AMPT_THETH 361 15
SGEEFRRRGGNESMVHVDWMIGS AMPT_THEAQ 361 15
SKEELDRRGVNDSLVHVDFMIGS AMP2_BACST 363 17
SREELVKEGLNESITHVDFMIGS AMPS_BACSU 363 17
THERMOPTASE8 Length of motif = 20 Motif number = 8
Thermophilic aminopeptidase motif VIII - 2
PCODE ST INT
DVDGLYEDGTRTPLMRRGRW AMPT_THETH 387 3
DVDGLLEDGTRVPLMRRGRW AMPT_THEAQ 387 3
NIDGVTKDGKREPIFRSGNW AMP2_BACST 389 3
NIDGITADGKREPIFRNGNW AMPS_BACSU 389 3
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