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Conserved domains on  [gi|73808266|ref|NP_068573|]
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matrix metalloproteinase-26 isoform 1 preproprotein [Homo sapiens]

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 11995183)

M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 98-253 2.27e-76

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: 228.66  E-value: 2.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266    98 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 177
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266   178 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 253
Cdd:pfam00413  81 GPGLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 98-253 2.27e-76

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: 228.66  E-value: 2.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266    98 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 177
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266   178 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 253
Cdd:pfam00413  81 GPGLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 98-253 3.74e-75

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: 225.55  E-value: 3.74e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  98 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNG-DADIKVSFWQWAHEDGWPFDGPGGILGHAFL 176
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266 177 PnSGNPGVVHFDKNEHWSASD--TGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPrTFQLSADDIQRIQHLYG 253
Cdd:cd04278  81 P-GGIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 95-253 1.10e-23

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: 92.80  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266     95 GRCKWNKHTLTYRIINYPHDmkpSAVKDSIYNAVSIWSNVTPLIFQQVqNGDADIKVSFWQWAHedgwpfdgpGGILGHA 174
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266    175 FLPNsgnpGVVHFDkNEHWSASDTgynlflVATHEIGHSLGLQHSGNQSS---IMYPTYWYHDPRTFQLSADDIQRIQHL 251
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 73808266    252 YG 253
Cdd:smart00235 137 YG 138
Zn_serralysin NF035945
serralysin family metalloprotease;
103-253 4.66e-07

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 50.36  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  103 TLTYRIINYPHDMKPSAVKD-SIYNAVSI---------WSNVTPLIFQQVQ-NGDADIKVSFWQwahEDGWPFdgpggil 171
Cdd:NF035945  54 NLTYSFLTSAPSSNPNGDTGfSAFNAEQKaqaklslqsWSDVANITFTEVSaGQKANITFGNYS---DSGQAY------- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  172 ghAFLPNSGNPG-------------VVHFDKNEHwsasdtGYNLFlvaTHEIGHSLGLQHSGN-QSSIMYPTY----WYH 233
Cdd:NF035945 124 --AYLPGTSDVSgqswynynsdyirNLTPDLGNY------GRQTL---THEIGHTLGLSHPGDyNAGEGNPTYkdatYAE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 73808266  234 DPRTFQL------------------SA---DDIQRIQHLYG 253
Cdd:NF035945 193 DTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 118-252 9.78e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.53  E-value: 9.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 118 SAVKDsiynAVSIWSNVTPLifQQVQNGD-ADIKVSFWQWAHEDGwPFDGPGGILGHA-FLPNSGNPGVVH-FdkNEHWS 194
Cdd:COG5549 104 AAVLQ----AIAEWNAYLPL--EVVENPEnADIIIVRSNPPLTAS-PNPETGARSAETtYEFYDTGNILSHrF--TILLS 174

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266 195 ASDTGYNLFLVATHEIGHSLGLQ-HSGNQSSIMYPTYWYHDPrtfQLSADDIQRIQHLY 252
Cdd:COG5549 175 PNQTGKYLLATARHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
206-227 1.13e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.13e-03
                         10        20
                 ....*....|....*....|..
gi 73808266  206 ATHEIGHSLGLQHSGNQSSIMY 227
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 206-257 2.59e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 2.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 73808266  206 ATHEIGHSLGLQHSGNQSSIMYptywyhdprtFQLSADDIQRIQHLYGEKCS 257
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN----------FSNSVRDVDIKEPNFCGSCQ 170
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 98-253 2.27e-76

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: 228.66  E-value: 2.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266    98 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 177
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266   178 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 253
Cdd:pfam00413  81 GPGLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 98-253 3.74e-75

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: 225.55  E-value: 3.74e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  98 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNG-DADIKVSFWQWAHEDGWPFDGPGGILGHAFL 176
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266 177 PnSGNPGVVHFDKNEHWSASD--TGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPrTFQLSADDIQRIQHLYG 253
Cdd:cd04278  81 P-GGIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 95-253 1.10e-23

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: 92.80  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266     95 GRCKWNKHTLTYRIINYPHDmkpSAVKDSIYNAVSIWSNVTPLIFQQVqNGDADIKVSFWQWAHedgwpfdgpGGILGHA 174
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266    175 FLPNsgnpGVVHFDkNEHWSASDTgynlflVATHEIGHSLGLQHSGNQSS---IMYPTYWYHDPRTFQLSADDIQRIQHL 251
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 73808266    252 YG 253
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 112-253 9.76e-17

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: 75.19  E-value: 9.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 112 PHDMKPSAVKDSIYNAVSIWSNVTPL--IFQQVQNGDADIKVSFwqwahEDGWPFDGPGGILGHAFLPNSGNPGVV---H 186
Cdd:cd04279  14 PPDSRAQSWLQAVKQAAAEWENVGPLkfVYNPEEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlfnR 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73808266 187 FDKNEHWSASDTGYNLFLVATHEIGHSLGLQH-SGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 253
Cdd:cd04279  89 TDINLGPGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 103-252 2.17e-15

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: 71.78  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 103 TLTYRIINYPHDMKPSAVKDSIYNAVS----IWSNVTPLIFQ--QVQNGDADIKVSFWQWAHEdgwpfdgpGGILGHAFL 176
Cdd:cd00203   2 VIPYVVVADDRDVEEENLSAQIQSLILiamqIWRDYLNIRFVlvGVEIDKADIAILVTRQDFD--------GGTGGWAYL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 177 PNSGNP--GVVHFDKNEHWsasdtGYNLFLVATHEIGHSLGLQHSGN--------------------QSSIMYPTYW-YH 233
Cdd:cd00203  74 GRVCDSlrGVGVLQDNQSG-----TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTKGsFS 148

                       170
                ....*....|....*....
gi 73808266 234 DPRTFQLSADDIQRIQHLY 252
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 103-252 2.55e-12

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: 63.28  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 103 TLTYRIINYPhdmkPSAVKDSIYNAVSIWSNVTPLIFQQVQNGD-ADIKVSFWQWAHEDgwpfDGPGGILGHAFLPNSGN 181
Cdd:cd04268   3 PITYYIDDSV----PDKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 182 pgvVHFDKN--EHWSASDTGYNLFLVATHEIGHSLGLQHS----------------GNQSSIMYPTYWYHDPRTFQ---- 239
Cdd:cd04268  75 ---ILLARVylYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSIQLGDgqky 151

                       170
                ....*....|....
gi 73808266 240 -LSADDIQRIQHLY 252
Cdd:cd04268 152 tIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 121-253 3.72e-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: 63.20  E-value: 3.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 121 KDSIYNAVSIWSNVTPLIFQQV-QNGDADIKVsfwqwahedGWPFDGPGGILGHAFLPNSG----NPGVVHFDKNEHWSA 195
Cdd:cd04277  36 QAAARDALEAWEDVADIDFVEVsDNSGADIRF---------GNSSDPDGNTAGYAYYPGSGsgtaYGGDIWFNSSYDTNS 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 196 SDTG-YNlFLVATHEIGHSLGLQHSGN----------------QSSIMypTYW----------YHDPRTFQLsaDDIQRI 248
Cdd:cd04277 107 DSPGsYG-YQTIIHEIGHALGLEHPGDynggdpvpptyaldsrEYTVM--SYNsgygngasagGGYPQTPML--LDIAAL 181


                ....*
gi 73808266 249 QHLYG 253
Cdd:cd04277 182 QYLYG 186
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 121-229 5.67e-08

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: 51.65  E-value: 5.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 121 KDSIYNAVSIWSNVTPLIFQ-QVQNGDADIKV----------SFWQWAHEDGWPFD----------GPGGILGHAFLPNS 179
Cdd:cd04267  35 ANSIYRSTNLRLGIRISLEGlQILKGEQFAPPidsdasntlnSFSFWRAEGPIRHDnavlltaqdfIEGDILGLAYVGSM 114

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73808266 180 GNP----GVVhfdknehwsaSDTGYNLF--LVATHEIGHSLGLQHSG----------NQSSIMYPT 229
Cdd:cd04267 115 CNPyssvGVV----------EDTGFTLLtaLTMAHELGHNLGAEHDGgdelafecdgGGNYIMAPV 170
Zn_serralysin NF035945
serralysin family metalloprotease;
103-253 4.66e-07

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 50.36  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  103 TLTYRIINYPHDMKPSAVKD-SIYNAVSI---------WSNVTPLIFQQVQ-NGDADIKVSFWQwahEDGWPFdgpggil 171
Cdd:NF035945  54 NLTYSFLTSAPSSNPNGDTGfSAFNAEQKaqaklslqsWSDVANITFTEVSaGQKANITFGNYS---DSGQAY------- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266  172 ghAFLPNSGNPG-------------VVHFDKNEHwsasdtGYNLFlvaTHEIGHSLGLQHSGN-QSSIMYPTY----WYH 233
Cdd:NF035945 124 --AYLPGTSDVSgqswynynsdyirNLTPDLGNY------GRQTL---THEIGHTLGLSHPGDyNAGEGNPTYkdatYAE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 73808266  234 DPRTFQL------------------SA---DDIQRIQHLYG 253
Cdd:NF035945 193 DTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 118-252 9.78e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.53  E-value: 9.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 118 SAVKDsiynAVSIWSNVTPLifQQVQNGD-ADIKVSFWQWAHEDGwPFDGPGGILGHA-FLPNSGNPGVVH-FdkNEHWS 194
Cdd:COG5549 104 AAVLQ----AIAEWNAYLPL--EVVENPEnADIIIVRSNPPLTAS-PNPETGARSAETtYEFYDTGNILSHrF--TILLS 174

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266 195 ASDTGYNLFLVATHEIGHSLGLQ-HSGNQSSIMYPTYWYHDPrtfQLSADDIQRIQHLY 252
Cdd:COG5549 175 PNQTGKYLLATARHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 165-218 3.90e-04

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: 40.79  E-value: 3.90e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 73808266 165 DGPGGILGHAFLPNSGNPGVVHFDK-NEHWSA----SDTGYNLFLVATHEIGHSLGLQH 218
Cdd:cd04275  95 FLGGGLLGYATFPDSLVSLAFITDGvVINPSSlpggSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 167-219 6.12e-04

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 39.80  E-value: 6.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73808266   167 PGGILGHAFLPNSGNP-GVVHF---------DKNEHwsasdtgynlflVATHEIGHSLGLQHS 219
Cdd:pfam12388 100 PSGTGGSAGFPSGGLPyGTIQIgtglqsystDVNEH------------VITHELGHSIGFRHS 150
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 192-229 8.24e-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: 8.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 73808266 192 HWSAS---DTGYNLFLVATHEIGHSLGLQHSGNQSS---------IMYPT 229
Cdd:cd04273 127 SRSCSineDTGLSSAFTIAHELGHVLGMPHDGDGNScgpegkdghIMSPT 176
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
206-227 1.13e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.13e-03
                         10        20
                 ....*....|....*....|..
gi 73808266  206 ATHEIGHSLGLQHSGNQSSIMY 227
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 205-235 1.86e-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: 39.16  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 73808266   205 VATHEIGHSLGLQHsgNQ-SSIMYPTYWYHDP 235
Cdd:pfam16313  16 VSAHEVGHTLGLRH--NFaASSAYPVDSLRDK 45
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 206-257 2.59e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 2.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 73808266  206 ATHEIGHSLGLQHSGNQSSIMYptywyhdprtFQLSADDIQRIQHLYGEKCS 257
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN----------FSNSVRDVDIKEPNFCGSCQ 170
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 197-256 4.97e-03

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 37.33  E-value: 4.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 197 DTG--YNLFLVATHEIGHSLGLQHSG------------------NQSSIMypTYWYHDPRTFQLSA---DDIQRIQHLYG 253
Cdd:cd04272 138 DTPgsYYGVYTMTHELAHLLGAPHDGspppswvkghpgsldcpwDDGYIM--SYVVNGERQYRFSQcsqRQIRNVFRRLG 215


                ...
gi 73808266 254 EKC 256
Cdd:cd04272 216 ASC 218
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
159-229 5.69e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.86  E-value: 5.69e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73808266 159 EDGWPFdgpggILGHAFLPnsGNPGVVHFDK-NEHWSASDTGYNLFL-----VATHEIGHSLGLQHSGNQSSIMYPT 229
Cdd:COG1913  81 APGLNF-----VFGLAYLG--GRVAVVSTARlRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHFS 150
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 148-235 6.61e-03

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: 36.92  E-value: 6.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 148 DIKVSFWQWAHED--GWPFdGP-------GGIL-GHAFLPNSgnpgvvhFDKNEH-WSASDTGYNLFLVATHEIGHSLGL 216
Cdd:cd04276  59 DIRYNVIRWIHSPngGWAY-GPsvvdprtGEILkADVILYSG-------FLRQDQlWYEDLLAASLRYLLAHEVGHTLGL 130

                        90       100
                ....*....|....*....|
gi 73808266 217 QHsgN-QSSIMYPTYWYHDP 235
Cdd:cd04276 131 RH--NfKASSDGSNEELEDP 148
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 165-256 6.67e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 36.82  E-value: 6.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266 165 DGPGGILGHAFL------PNSGnpGVVHFDKNehwsasdtgyNLFLVA---THEIGHSLGLQHSGN----QSS--IMYPt 229
Cdd:cd04269  97 DFDGNTVGLAYVggmcspKYSG--GVVQDHSR----------NLLLFAvtmAHELGHNLGMEHDDGgctcGRStcIMAP- 163

                        90       100
                ....*....|....*....|....*...
gi 73808266 230 YWYHDPRTF-QLSADDIQRIQHLYGEKC 256
Cdd:cd04269 164 SPSSLTDAFsNCSYEDYQKFLSRGGGQC 191
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
144-230 8.87e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 36.24  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808266   144 NGDADIKVSFWqWAHEDgwpFDGPG-GILGHafLPNSGNPGVVHFDKNEHWSASDTGYnLFLVATHEIGHSLGLQHSGNQ 222
Cdd:pfam13688  85 RGTQNDDLAYL-FLMTN---CSGGGlAWLGQ--LCNSGSAGSVSTRVSGNNVVVSTAT-EWQVFAHEIGHNFGAVHDCDS 157

                          90       100
                  ....*....|....*....|....*.
gi 73808266   223 SS------------------IMYPTY 230
Cdd:pfam13688 158 STssqccppsnstcpaggryIMNPSS 183
 
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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