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Conserved domains on  [gi|4505219|ref|NP_002414|]
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matrilysin preproprotein [Homo sapiens]

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 ...
 103-259 7.31e-97

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: 280.66  E-value: 7.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219    103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAP 182
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505219    183 GTGLGGDAHFDEDERWTDGS--SLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 1.69e-09

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: 52.52  E-value: 1.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505219     31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
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 ...
 103-259 7.31e-97

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: 280.66  E-value: 7.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219    103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAP 182
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505219    183 GTGLGGDAHFDEDERWTDGS--SLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-259 1.57e-85

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: 252.12  E-value: 1.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWG-TADIMIGFARGAHGDSYPFDGPGNTLAHAFA 181
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505219  182 PGtGLGGDAHFDEDERWTDGS-SLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPqNFKLSQDDIKGIQKLYG 259
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 100-260 8.31e-35

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: 122.07  E-value: 8.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219     100 NSPKWTSKVVTYRIvsYTRDLPHiTVDRLVSKALNMWGKEIPLHFRKVVwGTADIMIGFARGAHGdsyPFdgpgntLAHA 179
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219     180 FAPGtglgGDAHFDeDERWTDGSslGInflyaATHELGHSLGMGHSSDPNA---VMYPTYGNGDPQNFKLSQDDIKGIQK 256
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINT--GV-----AAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 4505219     257 LYGK 260
Cdd:smart00235 136 DYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 1.69e-09

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: 52.52  E-value: 1.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505219     31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPvdGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 129-258 2.51e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 53.15  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  129 VSKALNMWGKEIPLhfrKVVWGT--ADIMIGFAR---GAHGD----------SYPFDGPGNTLAHAFAPGTGlggdahfd 193
Cdd:COG5549 106 VLQAIAEWNAYLPL---EVVENPenADIIIVRSNpplTASPNpetgarsaetTYEFYDTGNILSHRFTILLS-------- 174

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505219  194 ederwtdgSSLGINFLYAAT-HELGHSLG-MGHSSDPNAVMYPTYGNGDPQnfkLSQDDIKGIQKLY 258
Cdd:COG5549 175 --------PNQTGKYLLATArHELGHALGiWGHSPSPTDAMYFSQVRNPPP---ISPRDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
212-233 1.08e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 41.84  E-value: 1.08e-04
                         10        20
                 ....*....|....*....|..
gi 4505219   212 ATHELGHSLGMGHSSDPNAVMY 233
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 212-233 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|..
gi 4505219   212 ATHELGHSLGMGHSSDPNAVMY 233
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-259 7.31e-97

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: 280.66  E-value: 7.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219    103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAP 182
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505219    183 GTGLGGDAHFDEDERWTDGS--SLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-259 1.57e-85

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: 252.12  E-value: 1.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWG-TADIMIGFARGAHGDSYPFDGPGNTLAHAFA 181
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505219  182 PGtGLGGDAHFDEDERWTDGS-SLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPqNFKLSQDDIKGIQKLYG 259
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 100-260 8.31e-35

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: 122.07  E-value: 8.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219     100 NSPKWTSKVVTYRIvsYTRDLPHiTVDRLVSKALNMWGKEIPLHFRKVVwGTADIMIGFARGAHGdsyPFdgpgntLAHA 179
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219     180 FAPGtglgGDAHFDeDERWTDGSslGInflyaATHELGHSLGMGHSSDPNA---VMYPTYGNGDPQNFKLSQDDIKGIQK 256
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINT--GV-----AAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 4505219     257 LYGK 260
Cdd:smart00235 136 DYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-258 1.25e-28

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: 106.84  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  107 KVVTYRIVSYTR----DLPHITVDRLVSKALNMWGKEIPLHFRKVVWG--TADIMIGFARGAHgdsypfdgPGNTLAHAF 180
Cdd:cd00203   1 KVIPYVVVADDRdveeENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQDF--------DGGTGGWAY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  181 APGT--GLGGDAHFDEDERWTDgsslgiNFLYAATHELGHSLGMGHSSDPNA--------------------VMYPTYGN 238
Cdd:cd00203  73 LGRVcdSLRGVGVLQDNQSGTK------EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGS 146

                       170       180
                ....*....|....*....|.
gi 4505219  239 G-DPQNFKLSQDDIKGIQKLY 258
Cdd:cd00203 147 FsDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 107-258 1.03e-17

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: 77.92  E-value: 1.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  107 KVVTYRIVsytrDLPHITVDRLVSKALNMWGKEIPLHFRKVVWG-TADIMIGFARgahgdsypfDGPGNTLAHAFAPGT- 184
Cdd:cd04268   2 KPITYYID----DSVPDKLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIR---------WIPYNDGTWSYGPSQv 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  185 -GLGGDAHFDEDERWTDGSSL-GINFLYAATHELGHSLGMGHSS----------------DPNAVMYPTYGN-----GDP 241
Cdd:cd04268  69 dPLTGEILLARVYLYSSFVEYsGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNfsiqlGDG 148

                       170
                ....*....|....*..
gi 4505219  242 QNFKLSQDDIKGIQKLY 258
Cdd:cd04268 149 QKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 129-259 1.38e-12

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: 64.01  E-value: 1.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  129 VSKALNMWGKEIPLHFRKVVWGT--ADIMIgfargAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERW--TDGSSL 204
Cdd:cd04279  26 VKQAAAEWENVGPLKFVYNPEEDndADIVI-----FFDRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINlgPGQPRG 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505219  205 GINFLYAATHELGHSLGMGHSSD-PNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYG 259
Cdd:cd04279 101 AENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 127-259 9.52e-12

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: 62.05  E-value: 9.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  127 RLVSKALNMWGKEIPLHFRKVVWGT-ADIMIGFargahgdsypFDGP-GNTLAHAFAPGTG----LGGDAHFDEDERwTD 200
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGsgtaYGGDIWFNSSYD-TN 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  201 GSSLGINFLYAATHELGHSLGMGHSSDPNA----------------VM--------YPTYGNGDPQNFklSQDDIKGIQK 256
Cdd:cd04277 106 SDSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgygnGASAGGGYPQTP--MLLDIAALQY 183


                ...
gi 4505219  257 LYG 259
Cdd:cd04277 184 LYG 186
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 1.69e-09

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: 52.52  E-value: 1.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505219     31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPvdGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 129-258 2.51e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 53.15  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  129 VSKALNMWGKEIPLhfrKVVWGT--ADIMIGFAR---GAHGD----------SYPFDGPGNTLAHAFAPGTGlggdahfd 193
Cdd:COG5549 106 VLQAIAEWNAYLPL---EVVENPenADIIIVRSNpplTASPNpetgarsaetTYEFYDTGNILSHRFTILLS-------- 174

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505219  194 ederwtdgSSLGINFLYAAT-HELGHSLG-MGHSSDPNAVMYPTYGNGDPQnfkLSQDDIKGIQKLY 258
Cdd:COG5549 175 --------PNQTGKYLLATArHELGHALGiWGHSPSPTDAMYFSQVRNPPP---ISPRDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
212-233 1.08e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 41.84  E-value: 1.08e-04
                         10        20
                 ....*....|....*....|..
gi 4505219   212 ATHELGHSLGMGHSSDPNAVMY 233
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 212-235 1.80e-04

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: 41.13  E-value: 1.80e-04
                        10        20
                ....*....|....*....|....
gi 4505219  212 ATHELGHSLGMGHSSDPNAVMYPT 235
Cdd:cd11375 127 AVHELGHLFGLDHCPYYACVMNFS 150
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
212-235 3.23e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 3.23e-04
                        10        20
                ....*....|....*....|....
gi 4505219  212 ATHELGHSLGMGHSSDPNAVMYPT 235
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMHFS 150
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 212-233 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|..
gi 4505219   212 ATHELGHSLGMGHSSDPNAVMY 233
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 212-259 2.27e-03

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: 38.17  E-value: 2.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4505219  212 ATHELGHSLGMGHS----------SDPNAVMYPTYGNGDPQNFklSQDDIKGIQKLYG 259
Cdd:cd04267 137 MAHELGHNLGAEHDggdelafecdGGGNYIMAPVDSGLNSYRF--SQCSIGSIREFLD 192
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 129-224 4.14e-03

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: 37.36  E-value: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505219  129 VSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPfdGPGNTLAHAFAPGTGLGGDAHFDEDERWTDgsslginf 208
Cdd:cd04327  25 VRAAAREWLPYANLKFKFVTDADADIRISFTPGDGYWSYV--GTDALLIGADAPTMNLGWFTDDTPDPEFSR-------- 94

                        90
                ....*....|....*.
gi 4505219  209 lyAATHELGHSLGMGH 224
Cdd:cd04327  95 --VVLHEFGHALGFIH 108
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 200-240 8.88e-03

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: 36.45  E-value: 8.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4505219  200 DGSSLGinflYAATHELGHSLGMGHSSDPNA---------VMYPTYGNGD 240
Cdd:cd04273 136 TGLSSA----FTIAHELGHVLGMPHDGDGNScgpegkdghIMSPTLGANT 181
 
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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