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Conserved domains on  [gi|489495605|ref|WP_003400522|]
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M10 family metallopeptidase [Pseudomonas syringae]

Protein Classification

M10 family metallopeptidase( domain architecture ID 11560623)

M10 family metallopeptidase similar to serralysin and Pseudomonas aeruginosa alkaline protease, which include an N-terminal peptidase domain and a C-terminal calcium-binding domain

Gene Ontology:  GO:0005509|GO:0004222|GO:0008270|GO:0006508
PubMed:  10361285|32860773|7674922

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-214 5.89e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


:

Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 177.99  E-value: 5.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  38 THLTYSFHKADSVYATDYSRSQEPGDAYSLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDnvGDIRFGGFKGLQGTEFG 117
Cdd:cd04277    2 TTLTYSFSNTGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSG--ADIRFGNSSDPDGNTAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 118 QAYAPGT---LGRSGDVWIGPNVNAADPAKGTDDYLTFMHETGHALGLKHSFEASQYNDVLLDAKFEDARYTIMSYTNNY 194
Cdd:cd04277   80 YAYYPGSgsgTAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNSGY 159

                        170       180
                 ....*....|....*....|....*..
gi 489495605 195 SFK-------PTTPMLLDVAAMQFIYG 214
Cdd:cd04277  160 GNGasagggyPQTPMLLDIAALQYLYG 186
Peptidase_M10_C super family cl23859
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 215-335 2.65e-19

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


The actual alignment was detected with superfamily member pfam08548:

Pssm-ID: 451582 [Multi-domain]  Cd Length: 222  Bit Score: 86.66  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  215 ANTHYHTGDDVYKW-------------APGQSVFeTIWDAGGKDTIDASNQEASVKINLNEGEFSTIGkafldynanpda 281
Cdd:pfam08548   1 ANLTTRTGDTVYGFnsntgrdfytatdASSKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVG------------ 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495605  282 ptSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDT 335
Cdd:pfam08548  68 --GLKGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 263-513 2.49e-05

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 46.05  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 263 GEFSTIGKAFLDYNANPDAPTSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDTYVIDQAG 342
Cdd:COG2931    1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 343 ELDLVQEKADQGVDTLKITYDNTSPIAQVINLNAGTLANFENVHLKGEGAFTVLGNDRNNTLTGNDADNVLFGGAGNDKL 422
Cdd:COG2931   81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 423 VGGQGADIMTGGSGADRFVFNDLSEMGKGHNSDVITDFNSQQGDKLSFLKMDANVDTKALDAFSFIGSGEFTGAGQLRFA 502
Cdd:COG2931  161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                        250
                 ....*....|.
gi 489495605 503 DHVLSGNVNGD 513
Cdd:COG2931  241 GGGGGGDDGLG 251
 
Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-214 5.89e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 177.99  E-value: 5.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  38 THLTYSFHKADSVYATDYSRSQEPGDAYSLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDnvGDIRFGGFKGLQGTEFG 117
Cdd:cd04277    2 TTLTYSFSNTGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSG--ADIRFGNSSDPDGNTAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 118 QAYAPGT---LGRSGDVWIGPNVNAADPAKGTDDYLTFMHETGHALGLKHSFEASQYNDVLLDAKFEDARYTIMSYTNNY 194
Cdd:cd04277   80 YAYYPGSgsgTAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNSGY 159

                        170       180
                 ....*....|....*....|....*..
gi 489495605 195 SFK-------PTTPMLLDVAAMQFIYG 214
Cdd:cd04277  160 GNGasagggyPQTPMLLDIAALQYLYG 186
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 215-335 2.65e-19

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 86.66  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  215 ANTHYHTGDDVYKW-------------APGQSVFeTIWDAGGKDTIDASNQEASVKINLNEGEFSTIGkafldynanpda 281
Cdd:pfam08548   1 ANLTTRTGDTVYGFnsntgrdfytatdASSKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVG------------ 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495605  282 ptSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDT 335
Cdd:pfam08548  68 --GLKGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 36-214 1.57e-12

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 65.33  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605   36 SGTHLTYSFhkadSVYATDYSRSQEPGdaysltdaqavAAKSALDAWSAVADIKFTEVQDTPDNVgDIRFGG-------- 107
Cdd:pfam00413   3 RKKNLTYRI----LNYTPDLPRAEVRR-----------AIRRAFKVWSEVTPLTFTEVSTGEADI-MIGFGRgdhgdgyp 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  108 FKGLQGTeFGQAYAPGTlGRSGDV-------WigpnVNAADPAKGTDDYLTFMHETGHALGLKHSfeasqyndvlldakf 180
Cdd:pfam00413  67 FDGPGGV-LAHAFFPGP-GLGGDIhfdddetW----TVGSDPPHGINLFLVAAHEIGHALGLGHS--------------- 125

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 489495605  181 eDARYTIM----SYTNNYSFKPTTPmllDVAAMQFIYG 214
Cdd:pfam00413 126 -SDPGAIMyptySPLDSKKFRLSQD---DIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 63-215 1.71e-11

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 61.98  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605    63 DAYSLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDNvgDIRFGgfKGLQGTEFGQAYAPGtlgrsGDVWIgpnvnaaDP 142
Cdd:smart00235  15 DSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADI--YISFG--SGDSGCTLSHAGRPG-----GDQHL-------SL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495605   143 AKGTDDYLTFMHETGHALGLKHSfeaSQYNDvlldakfedaRYTIMS-YTNNYSFKPTTPMLLDVAAMQFIYGA 215
Cdd:smart00235  79 GNGCINTGVAAHELGHALGLYHE---QSRSD----------RDNYMYiNYTNIDTRNFDLSEDDSLGIPYDYGS 139
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 263-513 2.49e-05

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 46.05  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 263 GEFSTIGKAFLDYNANPDAPTSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDTYVIDQAG 342
Cdd:COG2931    1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 343 ELDLVQEKADQGVDTLKITYDNTSPIAQVINLNAGTLANFENVHLKGEGAFTVLGNDRNNTLTGNDADNVLFGGAGNDKL 422
Cdd:COG2931   81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 423 VGGQGADIMTGGSGADRFVFNDLSEMGKGHNSDVITDFNSQQGDKLSFLKMDANVDTKALDAFSFIGSGEFTGAGQLRFA 502
Cdd:COG2931  161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                        250
                 ....*....|.
gi 489495605 503 DHVLSGNVNGD 513
Cdd:COG2931  241 GGGGGGDDGLG 251
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
405-440 3.00e-05

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 40.88  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489495605  405 TGNDADNVLFGGAGNDKLVGGQGADIMTGGSGADRF 440
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
 
Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-214 5.89e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 177.99  E-value: 5.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  38 THLTYSFHKADSVYATDYSRSQEPGDAYSLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDnvGDIRFGGFKGLQGTEFG 117
Cdd:cd04277    2 TTLTYSFSNTGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSG--ADIRFGNSSDPDGNTAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 118 QAYAPGT---LGRSGDVWIGPNVNAADPAKGTDDYLTFMHETGHALGLKHSFEASQYNDVLLDAKFEDARYTIMSYTNNY 194
Cdd:cd04277   80 YAYYPGSgsgTAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNSGY 159

                        170       180
                 ....*....|....*....|....*..
gi 489495605 195 SFK-------PTTPMLLDVAAMQFIYG 214
Cdd:cd04277  160 GNGasagggyPQTPMLLDIAALQYLYG 186
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 215-335 2.65e-19

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 86.66  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  215 ANTHYHTGDDVYKW-------------APGQSVFeTIWDAGGKDTIDASNQEASVKINLNEGEFSTIGkafldynanpda 281
Cdd:pfam08548   1 ANLTTRTGDTVYGFnsntgrdfytatdASSKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVG------------ 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495605  282 ptSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDT 335
Cdd:pfam08548  68 --GLKGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 74-213 5.52e-15

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 72.91  E-value: 5.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  74 AAKSALDAWSAVADIKFTEVQDTpdNVGDIRFGGFKGLQGTEFGQAYAPG-TLGRSGDVWIGPNVNAADPAKGTDDYL-- 150
Cdd:cd04268   19 AILDAIEAWNKAFAIGFKNANDV--DPADIRYSVIRWIPYNDGTWSYGPSqVDPLTGEILLARVYLYSSFVEYSGARLrn 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495605 151 TFMHETGHALGLKHSFEASQYNDVLLDAKFEDARYTIMSYTNNYSFK------PTTPMLLDVAAMQFIY 213
Cdd:cd04268   97 TAEHELGHALGLRHNFAASDRDDNVDLLAEKGDTSSVMDYAPSNFSIqlgdgqKYTIGPYDIAAIKKLY 165
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 36-214 1.57e-12

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 65.33  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605   36 SGTHLTYSFhkadSVYATDYSRSQEPGdaysltdaqavAAKSALDAWSAVADIKFTEVQDTPDNVgDIRFGG-------- 107
Cdd:pfam00413   3 RKKNLTYRI----LNYTPDLPRAEVRR-----------AIRRAFKVWSEVTPLTFTEVSTGEADI-MIGFGRgdhgdgyp 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  108 FKGLQGTeFGQAYAPGTlGRSGDV-------WigpnVNAADPAKGTDDYLTFMHETGHALGLKHSfeasqyndvlldakf 180
Cdd:pfam00413  67 FDGPGGV-LAHAFFPGP-GLGGDIhfdddetW----TVGSDPPHGINLFLVAAHEIGHALGLGHS--------------- 125

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 489495605  181 eDARYTIM----SYTNNYSFKPTTPmllDVAAMQFIYG 214
Cdd:pfam00413 126 -SDPGAIMyptySPLDSKKFRLSQD---DIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 63-215 1.71e-11

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 61.98  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605    63 DAYSLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDNvgDIRFGgfKGLQGTEFGQAYAPGtlgrsGDVWIgpnvnaaDP 142
Cdd:smart00235  15 DSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADI--YISFG--SGDSGCTLSHAGRPG-----GDQHL-------SL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495605   143 AKGTDDYLTFMHETGHALGLKHSfeaSQYNDvlldakfedaRYTIMS-YTNNYSFKPTTPMLLDVAAMQFIYGA 215
Cdd:smart00235  79 GNGCINTGVAAHELGHALGLYHE---QSRSD----------RDNYMYiNYTNIDTRNFDLSEDDSLGIPYDYGS 139
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 38-214 1.86e-10

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 59.53  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  38 THLTYSFHKadsvYATDYSRSqepgdaysltDAQAVAAKsALDAWSAVADIKFTEVQDTPDnvGDIRFGGFKGL------ 111
Cdd:cd04278    5 TNLTYRILN----YPPDLPRD----------DVRRAIAR-AFRVWSDVTPLTFREVTSGQE--ADIRISFARGNhgdgyp 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 112 ---QGTEFGQAYAPGTLGrsGDV-------WIgpnvnAADPAKGTDDYLTFMHETGHALGLKHSfeasqyNDvlldakfE 181
Cdd:cd04278   68 fdgPGGTLAHAFFPGGIG--GDIhfdddeqWT-----LGSDSGGTDLFSVAAHEIGHALGLGHS------SD-------P 127

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489495605 182 DArytIMS-----YTNNYSFKPTtpmllDVAAMQFIYG 214
Cdd:cd04278  128 DS---IMYpyyqgPVPKFKLSQD-----DIRGIQALYG 157
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 87-214 2.72e-10

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 60.03  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  87 DIKFTEVQDTPDNVGDIRFGGFKGLQGTEFGQAYAPGTLG-RSG-----DVWIGPNV---NAADPAKGTDDYL--TFMHE 155
Cdd:cd04276   44 NAIIVKVLPDDADPGDIRYNVIRWIHSPNGGWAYGPSVVDpRTGeilkaDVILYSGFlrqDQLWYEDLLAASLryLLAHE 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495605 156 TGHALGLKHSFEASQY--NDVLLDAKFED---ARYTIMSYT-NNYSFK--------PTTPMLLDVAAMQFIYG 214
Cdd:cd04276  124 VGHTLGLRHNFKASSDgsNEELEDPLGTKekgATSSVMDYPpPNVAAQgedqgdyyPPTIGPYDKWAIEYGYT 196
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 66-191 5.32e-08

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 52.52  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  66 SLTDAQAVAAKSALDAWSAVADIKFTEVQDTPDNVgDIRFGGFKG-LQGTEFGQAYAPGT-LGRSGDVWIGPNvnaadPA 143
Cdd:cd00203   18 NLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKA-DIAILVTRQdFDGGTGGWAYLGRVcDSLRGVGVLQDN-----QS 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489495605 144 KGTDDYLTFMHETGHALGLKHSFEAS---QYNDVLLDAKFEDAR-YTIMSYT 191
Cdd:cd00203   92 GTKEGAQTIAHELGHALGFYHDHDRKdrdDYPTIDDTLNAEDDDyYSVMSYT 143
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 56-214 1.21e-06

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 48.22  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  56 SRSQEPGDAYSLTDAQAVaaKSALDAWSAVADIKFTEvQDTPDNVGDIR--FGGFKGLQGTEFGQAYApGTLGRSGDVWI 133
Cdd:cd04279    9 DPTPAPPDSRAQSWLQAV--KQAAAEWENVGPLKFVY-NPEEDNDADIVifFDRPPPVGGAGGGLARA-GFPLISDGNRK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 134 GPN---VNAADPAKGTDDYL--TFMHETGHALGLKHSFeasqyndvlldAKFEDARYTIMSYTNNYSFKPTTpmlLDVAA 208
Cdd:cd04279   85 LFNrtdINLGPGQPRGAENLqaIALHELGHALGLWHHS-----------DRPEDAMYPSQGQGPDGNPTLSA---RDVAT 150


                 ....*.
gi 489495605 209 MQFIYG 214
Cdd:cd04279  151 LKRLYG 156
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 263-513 2.49e-05

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 46.05  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 263 GEFSTIGKAFLDYNANPDAPTSMNSGLAIAYGAHIENAIGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDTYVIDQAG 342
Cdd:COG2931    1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 343 ELDLVQEKADQGVDTLKITYDNTSPIAQVINLNAGTLANFENVHLKGEGAFTVLGNDRNNTLTGNDADNVLFGGAGNDKL 422
Cdd:COG2931   81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605 423 VGGQGADIMTGGSGADRFVFNDLSEMGKGHNSDVITDFNSQQGDKLSFLKMDANVDTKALDAFSFIGSGEFTGAGQLRFA 502
Cdd:COG2931  161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                        250
                 ....*....|.
gi 489495605 503 DHVLSGNVNGD 513
Cdd:COG2931  241 GGGGGGDDGLG 251
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
405-440 3.00e-05

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 40.88  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489495605  405 TGNDADNVLFGGAGNDKLVGGQGADIMTGGSGADRF 440
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
117-192 7.39e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 43.95  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495605  117 GQAYA--PGTLGRSGDVWIGPNVNAADPAKGTDDYlTFMHETGHALGLKHSFEASQYND-VLLDAKFEDAR-YTIMSYTN 192
Cdd:pfam13688 105 GLAWLgqLCNSGSAGSVSTRVSGNNVVVSTATEWQ-VFAHEIGHNFGAVHDCDSSTSSQcCPPSNSTCPAGgRYIMNPSS 183
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 148-194 1.13e-04

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 44.16  E-value: 1.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489495605  148 DYLTF--MHETGHALGLKHSFEASQYNDV--LLDAKFEDARYT---IMSYT-NNY 194
Cdd:pfam16313  11 ALLRFvsAHEVGHTLGLRHNFAASSAYPVdsLRDKSFTRKYGTtpsIMDYArFNY 65
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
397-431 1.49e-04

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 38.96  E-value: 1.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 489495605  397 GNDRNNTLTGNDADNVLFGGAGNDKLVGGQGADIM 431
Cdd:pfam00353   2 GGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
301-335 2.41e-03

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 35.49  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 489495605  301 IGSAFNDTLIGNDLDNVLNGRGGLDTMIGGLGNDT 335
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDT 35
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 136-195 8.56e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 37.60  E-value: 8.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495605  136 NVNAADPAKGTDDYLTFMHETGHALGLKHSFEasqYNDVLLDAKFEDARY-TIMSYTNNYS 195
Cdd:pfam13583 123 NAKASGVARSRDEWDIFAHEIGHTFGAVHDCS---SQGEGLSSSTEDGSGqTIMSYASTAS 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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