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Conserved domains on  [gi|402493|gb|AAA99432|]
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matrilysin [Rattus norvegicus]

Protein Classification

matrilysin family metalloendoprotease( domain architecture ID 12021146)

matrilysin family metalloendoprotease may play a role in the degradation and remodeling of the extracellular matrix, such as mammalian matrilysin (matrix metallolproteinase-7 or MMP-7), which degrades casein, type I, III, IV, and V gelatin, as well as fibronectin, and which activates procollagenase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-262 9.57e-96

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: 277.96  E-value: 9.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493     106 KWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWGTADIIIGFARGDHGDNFPFDGPGNTLGHAFAP 185
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402493     186 GPGLGGDAHFDKDEYWTDGEDS--GVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSEDFSLTKDDIAGIQKLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-85 1.32e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.51  E-value: 1.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 402493      34 QWEQAQNYLRKF-YLHDSKTKKATSA-VDKLREMQKFFGLPETGKLSPRVMEIM 85
Cdd:pfam01471   4 DVKELQRYLNRLgYYPGPVDGYFGPStEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-262 9.57e-96

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: 277.96  E-value: 9.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493     106 KWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWGTADIIIGFARGDHGDNFPFDGPGNTLGHAFAP 185
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402493     186 GPGLGGDAHFDKDEYWTDGEDS--GVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSEDFSLTKDDIAGIQKLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-262 9.92e-82

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: 242.49  E-value: 9.92e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   106 KWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWG-TADIIIGFARGDHGDNFPFDGPGNTLGHAFA 184
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402493   185 PGpGLGGDAHFDKDEYWTDG-EDSGVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSeDFSLTKDDIAGIQKLYG 262
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 103-263 1.70e-40

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: 136.71  E-value: 1.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493      103 NSPKWHSRTVTYRIVSYTTDlprFLVDQIVKRALRMWSMQIPLNFKRVSwGTADIIIGFARGDHGdnfPFdgpgntLGHA 182
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493      183 FAPGpglgGDAHFDkDEYWTDGEDsgvnflfVATHELGHSLGLGHSSVPSS---VMYPTYQGDHSEDFSLTKDDIAGIQK 259
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 402493      260 LYGK 263
Cdd:smart00235 136 DYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-85 1.32e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.51  E-value: 1.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 402493      34 QWEQAQNYLRKF-YLHDSKTKKATSA-VDKLREMQKFFGLPETGKLSPRVMEIM 85
Cdd:pfam01471   4 DVKELQRYLNRLgYYPGPVDGYFGPStEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-261 1.15e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.14  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   132 VKRALRMWSMQIPLNfkRVSWGT-ADIIIgfARGDHGDNFPFDG-PGNTLGHAfAPGPGLGGDAHFDKDEYWTDGEDSGV 209
Cdd:COG5549 106 VLQAIAEWNAYLPLE--VVENPEnADIII--VRSNPPLTASPNPeTGARSAET-TYEFYDTGNILSHRFTILLSPNQTGK 180

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 402493   210 NFLFVATHELGHSLGL-GHSSVPSSVMYPtyQGDhSEDFSLTKDDIAGIQKLY 261
Cdd:COG5549 181 YLLATARHELGHALGIwGHSPSPTDAMYF--SQV-RNPPPISPRDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
215-236 4.04e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 4.04e-05
                         10        20
                 ....*....|....*....|..
gi 402493    215 ATHELGHSLGLGHSSVPSSVMY 236
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 215-236 1.10e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.85  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|..
gi 402493    215 ATHELGHSLGLGHSSVPSSVMY 236
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 192-230 5.73e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 37.30  E-value: 5.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 402493    192 DAHFDKDEYWTDGEDSG-VNFLFVATHELGHSLGLGhSSV 230
Cdd:NF038122 115 SSFFNFDFDPSDGISAGtYDFVGVAAHEIGHALGFV-SGV 153
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-262 9.57e-96

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: 277.96  E-value: 9.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493     106 KWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWGTADIIIGFARGDHGDNFPFDGPGNTLGHAFAP 185
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402493     186 GPGLGGDAHFDKDEYWTDGEDS--GVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSEDFSLTKDDIAGIQKLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-262 9.92e-82

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: 242.49  E-value: 9.92e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   106 KWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWG-TADIIIGFARGDHGDNFPFDGPGNTLGHAFA 184
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402493   185 PGpGLGGDAHFDKDEYWTDG-EDSGVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSeDFSLTKDDIAGIQKLYG 262
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 103-263 1.70e-40

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: 136.71  E-value: 1.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493      103 NSPKWHSRTVTYRIVSYTTDlprFLVDQIVKRALRMWSMQIPLNFKRVSwGTADIIIGFARGDHGdnfPFdgpgntLGHA 182
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493      183 FAPGpglgGDAHFDkDEYWTDGEDsgvnflfVATHELGHSLGLGHSSVPSS---VMYPTYQGDHSEDFSLTKDDIAGIQK 259
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 402493      260 LYGK 263
Cdd:smart00235 136 DYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 110-261 2.42e-19

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: 82.57  E-value: 2.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   110 RTVTYRIVSYT----TDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWG--TADIIIGFARGDHgdnfpfdgPGNTLGHAF 183
Cdd:cd00203   1 KVIPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQDF--------DGGTGGWAY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   184 APG--PGLGGDAHFDKDEYWTDgedsgvNFLFVATHELGHSLGLGHSS--------------------VPSSVMYPTY-Q 240
Cdd:cd00203  73 LGRvcDSLRGVGVLQDNQSGTK------EGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKgS 146

                       170       180
                ....*....|....*....|.
gi 402493   241 GDHSEDFSLTKDDIAGIQKLY 261
Cdd:cd00203 147 FSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 132-262 9.39e-15

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: 69.79  E-value: 9.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   132 VKRALRMWSMQipLNFKRVSWGT----ADIIIgfargDHGDNFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEYWTDGEDS 207
Cdd:cd04279  26 VKQAAAEWENV--GPLKFVYNPEedndADIVI-----FFDRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINLGPGQP 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 402493   208 GV--NFLFVATHELGHSLGLGHSSV-PSSVMYPTYQGDHSEDFSLTKDDIAGIQKLYG 262
Cdd:cd04279  99 RGaeNLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 110-261 1.03e-14

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: 69.83  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   110 RTVTYRIVSYTtdlPRFLVDQIvKRALRMWSMQIPLNFKRVSWG-TADIIIGFARgdhgdnfpfDGPGNTLGHAFAPG-- 186
Cdd:cd04268   2 KPITYYIDDSV---PDKLRAAI-LDAIEAWNKAFAIGFKNANDVdPADIRYSVIR---------WIPYNDGTWSYGPSqv 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   187 PGLGGDAHFDkDEYWTDG--EDSGVNFLFVATHELGHSLGLGHSS----------------VPSSVMYPT-----YQGDH 243
Cdd:cd04268  69 DPLTGEILLA-RVYLYSSfvEYSGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYApsnfsIQLGD 147

                       170
                ....*....|....*...
gi 402493   244 SEDFSLTKDDIAGIQKLY 261
Cdd:cd04268 148 GQKYTIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-262 2.46e-14

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: 69.37  E-value: 2.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   132 VKRALRMWSMQIPLNFKRVSWGT-ADIIIGFargdhgdnfpFDGP-GNTLGHAFAPGPG----LGGDAHFDKDEYWTDGE 205
Cdd:cd04277  39 ARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGsgtaYGGDIWFNSSYDTNSDS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   206 DSGVNFlFVATHELGHSLGLGHSSVPS----------------SVM--------YPTYQGDHSEDFSLtkDDIAGIQKLY 261
Cdd:cd04277 109 PGSYGY-QTIIHEIGHALGLEHPGDYNggdpvpptyaldsreyTVMsynsgygnGASAGGGYPQTPML--LDIAALQYLY 185


                .
gi 402493   262 G 262
Cdd:cd04277 186 G 186
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-85 1.32e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.51  E-value: 1.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 402493      34 QWEQAQNYLRKF-YLHDSKTKKATSA-VDKLREMQKFFGLPETGKLSPRVMEIM 85
Cdd:pfam01471   4 DVKELQRYLNRLgYYPGPVDGYFGPStEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-261 1.15e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.14  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   132 VKRALRMWSMQIPLNfkRVSWGT-ADIIIgfARGDHGDNFPFDG-PGNTLGHAfAPGPGLGGDAHFDKDEYWTDGEDSGV 209
Cdd:COG5549 106 VLQAIAEWNAYLPLE--VVENPEnADIII--VRSNPPLTASPNPeTGARSAET-TYEFYDTGNILSHRFTILLSPNQTGK 180

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 402493   210 NFLFVATHELGHSLGL-GHSSVPSSVMYPtyQGDhSEDFSLTKDDIAGIQKLY 261
Cdd:COG5549 181 YLLATARHELGHALGIwGHSPSPTDAMYF--SQV-RNPPPISPRDINTLKRIY 230
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 121-227 5.26e-06

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 45.83  E-value: 5.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   121 TDLPRFLVDQIVKRAlRMWSMQIPLNFKRVSWGTADIIIGFARGDhgDNFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEy 200
Cdd:cd04327  15 GGPDAFLKDKVRAAA-REWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWFTDDTPDP- 90

                        90       100
                ....*....|....*....|....*..
gi 402493   201 wtdgedsgvNFLFVATHELGHSLGLGH 227
Cdd:cd04327  91 ---------EFSRVVLHEFGHALGFIH 108
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
215-236 4.04e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 4.04e-05
                         10        20
                 ....*....|....*....|..
gi 402493    215 ATHELGHSLGLGHSSVPSSVMY 236
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 155-238 6.80e-05

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 42.28  E-value: 6.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   155 ADIIIGFARGD---HGDNFPF---DGPGNTLGHAFAPgpglggdahfDKDEYWTDGEDSGVNF---LFVATHELGHSLGL 225
Cdd:cd11375  68 ADCVLGVTDVDlyePGLNFVFglaDGGSGVAVVSTAR----------LRPEFYGLPPDEGLFLerlLKEAVHELGHLFGL 137

                        90
                ....*....|...
gi 402493   226 GHSSVPSSVMYPT 238
Cdd:cd11375 138 DHCPYYACVMNFS 150
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
214-238 1.76e-04

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 1.76e-04
                        10        20
                ....*....|....*....|....*
gi 402493   214 VATHELGHSLGLGHSSVPSSVMYPT 238
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHFS 150
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 176-248 2.18e-04

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 41.25  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402493   176 GNTLGHAFAPGPGlggdahfdkDEYWTDG--EDSGVNFL--FVATHELGHSLGLGHS----------SVPSSVMYPTYQG 241
Cdd:cd04267 103 GDILGLAYVGSMC---------NPYSSVGvvEDTGFTLLtaLTMAHELGHNLGAEHDggdelafecdGGGNYIMAPVDSG 173


                ....*..
gi 402493   242 DHSEDFS 248
Cdd:cd04267 174 LNSYRFS 180
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 205-238 9.40e-04

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 39.53  E-value: 9.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 402493   205 EDSGVNFLFVATHELGHSLGLGH---------SSVPSSVMYPT 238
Cdd:cd04273 134 EDTGLSSAFTIAHELGHVLGMPHdgdgnscgpEGKDGHIMSPT 176
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 215-236 1.10e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.85  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|..
gi 402493    215 ATHELGHSLGLGHSSVPSSVMY 236
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 173-227 1.81e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 38.86  E-value: 1.81e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 402493   173 DGPGNTLGHAFAPGPGLGGDAHFD----KDEYWTDGEDSGVNFLFVATHELGHSLGLGH 227
Cdd:cd04275  95 FLGGGLLGYATFPDSLVSLAFITDgvviNPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 116-176 3.79e-03

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 37.64  E-value: 3.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402493   116 IVSYTTDLPrflvDQIVKRALRMwSMQIPLNFKRVSWGTADIIIgfargDHG--DNFP---FDGPG 176
Cdd:cd07207 136 VVFSAETTP----DMPVAKAVRA-SMSIPFVFKPVRLAKGDVYV-----DGGvlDNYPvwlFDGWE 191
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 192-230 5.73e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 37.30  E-value: 5.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 402493    192 DAHFDKDEYWTDGEDSG-VNFLFVATHELGHSLGLGhSSV 230
Cdd:NF038122 115 SSFFNFDFDPSDGISAGtYDFVGVAAHEIGHALGFV-SGV 153
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 213-248 9.00e-03

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: 36.85  E-value: 9.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402493     213 FVATHELGHSLGLGH-----SSVP----------------SSVM-YPTY----QGDHSEDFS 248
Cdd:pfam16313  15 FVSAHEVGHTLGLRHnfaasSAYPvdslrdksftrkygttPSIMdYARFnyvaQPEDQIDLS 76
 
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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