NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767966168|ref|XP_011518521|]
View 

matrix metalloproteinase-26 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 28-183 2.57e-77

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: 228.27  E-value: 2.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168   28 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 107
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168  108 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 183
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 ...
 28-183 2.57e-77

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: 228.27  E-value: 2.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168   28 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 107
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168  108 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 183
Cdd:pfam00413  81 GPGLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 28-183 3.05e-76

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: 3.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  28 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNG-DADIKVSFWQWAHEDGWPFDGPGGILGHAFL 106
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168 107 PnSGNPGVVHFDKNEHWSASD--TGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPrTFQLSADDIQRIQHLYG 183
Cdd:cd04278   81 P-GGIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 25-183 7.43e-24

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: 91.26  E-value: 7.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168    25 GRCKWNKHTLTYRIINYPHDmkpSAVKDSIYNAVSIWSNVTPLIFQQVqNGDADIKVSFWQWAHedgwpfdgpGGILGHA 104
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168   105 FLPNsgnpGVVHFDkNEHWSASDTgynlflVATHEIGHSLGLQHSGNQSS---IMYPTYWYHDPRTFQLSADDIQRIQHL 181
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 767966168   182 YG 183
Cdd:smart00235 137 YG 138
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 48-182 6.63e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  48 SAVKDsiynAVSIWSNVTPLifQQVQNGD-ADIKVSFWQWAHEDGwPFDGPGGILGHA-FLPNSGNPGVVH-FdkNEHWS 124
Cdd:COG5549  104 AAVLQ----AIAEWNAYLPL--EVVENPEnADIIIVRSNPPLTAS-PNPETGARSAETtYEFYDTGNILSHrF--TILLS 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168 125 ASDTGYNLFLVATHEIGHSLGLQ-HSGNQSSIMYPTYWYHDPrtfQLSADDIQRIQHLY 182
Cdd:COG5549  175 PNQTGKYLLATARHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
Zn_serralysin NF035945
serralysin family metalloprotease;
33-183 8.00e-07

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 48.05  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  33 TLTYRIINYPHDMKPSAVKD-SIYNAVSI---------WSNVTPLIFQQVQ-NGDADIKVSFWQwahEDGWPFdgpggil 101
Cdd:NF035945  54 NLTYSFLTSAPSSNPNGDTGfSAFNAEQKaqaklslqsWSDVANITFTEVSaGQKANITFGNYS---DSGQAY------- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 102 ghAFLPNSGNPG-------------VVHFDKNEHwsasdtGYNLFlvaTHEIGHSLGLQHSGN-QSSIMYPTY----WYH 163
Cdd:NF035945 124 --AYLPGTSDVSgqswynynsdyirNLTPDLGNY------GRQTL---THEIGHTLGLSHPGDyNAGEGNPTYkdatYAE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767966168 164 DPRTFQL------------------SA---DDIQRIQHLYG 183
Cdd:NF035945 193 DTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
136-157 6.38e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 6.38e-04
                         10        20
                 ....*....|....*....|..
gi 767966168 136 ATHEIGHSLGLQHSGNQSSIMY 157
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 136-187 1.46e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767966168 136 ATHEIGHSLGLQHSGNQSSIMYptywyhdprtFQLSADDIQRIQHLYGEKCS 187
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 ...
 28-183 2.57e-77

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: 228.27  E-value: 2.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168   28 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLP 107
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168  108 NSGNPGVVHFDKNEHW---SASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 183
Cdd:pfam00413  81 GPGLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 28-183 3.05e-76

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: 3.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  28 KWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNG-DADIKVSFWQWAHEDGWPFDGPGGILGHAFL 106
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168 107 PnSGNPGVVHFDKNEHWSASD--TGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPrTFQLSADDIQRIQHLYG 183
Cdd:cd04278   81 P-GGIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 25-183 7.43e-24

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: 91.26  E-value: 7.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168    25 GRCKWNKHTLTYRIINYPHDmkpSAVKDSIYNAVSIWSNVTPLIFQQVqNGDADIKVSFWQWAHedgwpfdgpGGILGHA 104
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168   105 FLPNsgnpGVVHFDkNEHWSASDTgynlflVATHEIGHSLGLQHSGNQSS---IMYPTYWYHDPRTFQLSADDIQRIQHL 181
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 767966168   182 YG 183
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 42-183 5.01e-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: 74.03  E-value: 5.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  42 PHDMKPSAVKDSIYNAVSIWSNVTPL--IFQQVQNGDADIKVSFwqwahEDGWPFDGPGGILGHAFLPNSGNPGVV---H 116
Cdd:cd04279   14 PPDSRAQSWLQAVKQAAAEWENVGPLkfVYNPEEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlfnR 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767966168 117 FDKNEHWSASDTGYNLFLVATHEIGHSLGLQH-SGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYG 183
Cdd:cd04279   89 TDINLGPGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 33-182 2.78e-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: 69.86  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  33 TLTYRIINYPHDMKPSAVKDSIYNAVS----IWSNVTPLIFQ--QVQNGDADIKVSFWQWAHEdgwpfdgpGGILGHAFL 106
Cdd:cd00203    2 VIPYVVVADDRDVEEENLSAQIQSLILiamqIWRDYLNIRFVlvGVEIDKADIAILVTRQDFD--------GGTGGWAYL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 107 PNSGNP--GVVHFDKNEHWsasdtGYNLFLVATHEIGHSLGLQHSGN--------------------QSSIMYPTYW-YH 163
Cdd:cd00203   74 GRVCDSlrGVGVLQDNQSG-----TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTKGsFS 148

                        170
                 ....*....|....*....
gi 767966168 164 DPRTFQLSADDIQRIQHLY 182
Cdd:cd00203  149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 33-182 3.72e-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: 61.36  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  33 TLTYRIINYPhdmkPSAVKDSIYNAVSIWSNVTPLIFQQVQNGD-ADIKVSFWQWAHEDgwpfDGPGGILGHAFLPNSGN 111
Cdd:cd04268    3 PITYYIDDSV----PDKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 112 pgvVHFDKN--EHWSASDTGYNLFLVATHEIGHSLGLQHS----------------GNQSSIMYPTYWYHDPRTFQ---- 169
Cdd:cd04268   75 ---ILLARVylYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSIQLGDgqky 151

                        170
                 ....*....|....
gi 767966168 170 -LSADDIQRIQHLY 182
Cdd:cd04268  152 tIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 51-183 9.60e-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: 60.89  E-value: 9.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  51 KDSIYNAVSIWSNVTPLIFQQV-QNGDADIKVsfwqwahedGWPFDGPGGILGHAFLPNSG----NPGVVHFDKNEHWSA 125
Cdd:cd04277   36 QAAARDALEAWEDVADIDFVEVsDNSGADIRF---------GNSSDPDGNTAGYAYYPGSGsgtaYGGDIWFNSSYDTNS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 126 SDTG-YNlFLVATHEIGHSLGLQHSGN----------------QSSIMypTYW----------YHDPRTFQLsaDDIQRI 178
Cdd:cd04277  107 DSPGsYG-YQTIIHEIGHALGLEHPGDynggdpvpptyaldsrEYTVM--SYNsgygngasagGGYPQTPML--LDIAAL 181


                 ....*
gi 767966168 179 QHLYG 183
Cdd:cd04277  182 QYLYG 186
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 51-159 6.42e-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: 50.50  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  51 KDSIYNAVSIWSNVTPLIFQ-QVQNGDADIKV----------SFWQWAHEDGWPFD----------GPGGILGHAFLPNS 109
Cdd:cd04267   35 ANSIYRSTNLRLGIRISLEGlQILKGEQFAPPidsdasntlnSFSFWRAEGPIRHDnavlltaqdfIEGDILGLAYVGSM 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966168 110 GNP----GVVhfdknehwsaSDTGYNLF--LVATHEIGHSLGLQHSG----------NQSSIMYPT 159
Cdd:cd04267  115 CNPyssvGVV----------EDTGFTLLtaLTMAHELGHNLGAEHDGgdelafecdgGGNYIMAPV 170
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 48-182 6.63e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  48 SAVKDsiynAVSIWSNVTPLifQQVQNGD-ADIKVSFWQWAHEDGwPFDGPGGILGHA-FLPNSGNPGVVH-FdkNEHWS 124
Cdd:COG5549  104 AAVLQ----AIAEWNAYLPL--EVVENPEnADIIIVRSNPPLTAS-PNPETGARSAETtYEFYDTGNILSHrF--TILLS 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168 125 ASDTGYNLFLVATHEIGHSLGLQ-HSGNQSSIMYPTYWYHDPrtfQLSADDIQRIQHLY 182
Cdd:COG5549  175 PNQTGKYLLATARHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
Zn_serralysin NF035945
serralysin family metalloprotease;
33-183 8.00e-07

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 48.05  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  33 TLTYRIINYPHDMKPSAVKD-SIYNAVSI---------WSNVTPLIFQQVQ-NGDADIKVSFWQwahEDGWPFdgpggil 101
Cdd:NF035945  54 NLTYSFLTSAPSSNPNGDTGfSAFNAEQKaqaklslqsWSDVANITFTEVSaGQKANITFGNYS---DSGQAY------- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 102 ghAFLPNSGNPG-------------VVHFDKNEHwsasdtGYNLFlvaTHEIGHSLGLQHSGN-QSSIMYPTY----WYH 163
Cdd:NF035945 124 --AYLPGTSDVSgqswynynsdyirNLTPDLGNY------GRQTL---THEIGHTLGLSHPGDyNAGEGNPTYkdatYAE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767966168 164 DPRTFQL------------------SA---DDIQRIQHLYG 183
Cdd:NF035945 193 DTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 95-148 3.38e-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: 40.02  E-value: 3.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767966168  95 DGPGGILGHAFLPNSGNPGVVHFDK-NEHWSA----SDTGYNLFLVATHEIGHSLGLQH 148
Cdd:cd04275   95 FLGGGLLGYATFPDSLVSLAFITDGvVINPSSlpggSAAPYNLGDTATHEVGHWLGLYH 153
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
136-157 6.38e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 6.38e-04
                         10        20
                 ....*....|....*....|..
gi 767966168 136 ATHEIGHSLGLQHSGNQSSIMY 157
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 122-159 6.90e-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: 38.76  E-value: 6.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966168 122 HWSAS---DTGYNLFLVATHEIGHSLGLQHSGNQSS---------IMYPT 159
Cdd:cd04273  127 SRSCSineDTGLSSAFTIAHELGHVLGMPHDGDGNScgpegkdghIMSPT 176
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 97-149 7.54e-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: 39.03  E-value: 7.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966168   97 PGGILGHAFLPNSGNP-GVVHF---------DKNEHwsasdtgynlflVATHEIGHSLGLQHS 149
Cdd:pfam12388 100 PSGTGGSAGFPSGGLPyGTIQIgtglqsystDVNEH------------VITHELGHSIGFRHS 150
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 135-165 1.11e-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: 38.77  E-value: 1.11e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 767966168  135 VATHEIGHSLGLQHsgNQ-SSIMYPTYWYHDP 165
Cdd:pfam16313  16 VSAHEVGHTLGLRH--NFaASSAYPVDSLRDK 45
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 136-187 1.46e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767966168 136 ATHEIGHSLGLQHSGNQSSIMYptywyhdprtFQLSADDIQRIQHLYGEKCS 187
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN----------FSNSVRDVDIKEPNFCGSCQ 170
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
89-159 3.28e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.86  E-value: 3.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966168  89 EDGWPFdgpggILGHAFLPnsGNPGVVHFDK-NEHWSASDTGYNLFL-----VATHEIGHSLGLQHSGNQSSIMYPT 159
Cdd:COG1913   81 APGLNF-----VFGLAYLG--GRVAVVSTARlRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHFS 150
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 127-186 3.79e-03

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 36.95  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168 127 DTG--YNLFLVATHEIGHSLGLQHSG------------------NQSSIMypTYWYHDPRTFQLSA---DDIQRIQHLYG 183
Cdd:cd04272  138 DTPgsYYGVYTMTHELAHLLGAPHDGspppswvkghpgsldcpwDDGYIM--SYVVNGERQYRFSQcsqRQIRNVFRRLG 215


                 ...
gi 767966168 184 EKC 186
Cdd:cd04272  216 ASC 218
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 135-159 4.95e-03

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: 36.12  E-value: 4.95e-03
                         10        20
                 ....*....|....*....|....*
gi 767966168 135 VATHEIGHSLGLQHSGNQSSIMYPT 159
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFS 150
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 78-165 5.02e-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: 36.53  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  78 DIKVSFWQWAHED--GWPFdGP-------GGIL-GHAFLPNSgnpgvvhFDKNEH-WSASDTGYNLFLVATHEIGHSLGL 146
Cdd:cd04276   59 DIRYNVIRWIHSPngGWAY-GPsvvdprtGEILkADVILYSG-------FLRQDQlWYEDLLAASLRYLLAHEVGHTLGL 130

                         90       100
                 ....*....|....*....|
gi 767966168 147 QHsgN-QSSIMYPTYWYHDP 165
Cdd:cd04276  131 RH--NfKASSDGSNEELEDP 148
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 95-186 6.14e-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: 36.05  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966168  95 DGPGGILGHAFL------PNSGnpGVVHFDKNehwsasdtgyNLFLVA---THEIGHSLGLQHSGN----QSS--IMYPt 159
Cdd:cd04269   97 DFDGNTVGLAYVggmcspKYSG--GVVQDHSR----------NLLLFAvtmAHELGHNLGMEHDDGgctcGRStcIMAP- 163

                         90       100
                 ....*....|....*....|....*...
gi 767966168 160 YWYHDPRTF-QLSADDIQRIQHLYGEKC 186
Cdd:cd04269  164 SPSSLTDAFsNCSYEDYQKFLSRGGGQC 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH