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Conserved domains on  [gi|17555226|ref|NP_498599|]
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Peptidase metallopeptidase domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-205 7.80e-69

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: 210.14  E-value: 7.80e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  48 RWKKHTLTWQLQTQNLlDPDVFIVRNTMHRAFNEWSTVSSVDFREIPPDlvtkQPPDIYIAFEKGEHSDGFPFDGQDGVV 127
Cdd:cd04278   1 KWSKTNLTYRILNYPP-DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG----QEADIRISFARGNHGDGYPFDGPGGTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226 128 AHAFYP--RDGRLHFDAEEQWSLNS-VEGVNLFQTAVHEIGHLLGLEHSMDVRAAMFAAKRPYDPAFTLGDDDVRAIRSL 204
Cdd:cd04278  76 AHAFFPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQAL 155


                .
gi 17555226 205 F 205
Cdd:cd04278 156 Y 156
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-205 7.80e-69

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: 210.14  E-value: 7.80e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  48 RWKKHTLTWQLQTQNLlDPDVFIVRNTMHRAFNEWSTVSSVDFREIPPDlvtkQPPDIYIAFEKGEHSDGFPFDGQDGVV 127
Cdd:cd04278   1 KWSKTNLTYRILNYPP-DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG----QEADIRISFARGNHGDGYPFDGPGGTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226 128 AHAFYP--RDGRLHFDAEEQWSLNS-VEGVNLFQTAVHEIGHLLGLEHSMDVRAAMFAAKRPYDPAFTLGDDDVRAIRSL 204
Cdd:cd04278  76 AHAFFPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQAL 155


                .
gi 17555226 205 F 205
Cdd:cd04278 156 Y 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 48-204 5.43e-54

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: 172.42  E-value: 5.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226    48 RWKKHTLTWQLQTQ-NLLDPDVfiVRNTMHRAFNEWSTVSSVDFREippdlVTKQPPDIYIAFEKGEHSDGFPFDGQDGV 126
Cdd:pfam00413   1 KWRKKNLTYRILNYtPDLPRAE--VRRAIRRAFKVWSEVTPLTFTE-----VSTGEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226   127 VAHAFYP---RDGRLHFDAEEQWSLNSV--EGVNLFQTAVHEIGHLLGLEHSMDVRAAMFAAKRPYDPA-FTLGDDDVRA 200
Cdd:pfam00413  74 LAHAFFPgpgLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKG 153


                  ....
gi 17555226   201 IRSL 204
Cdd:pfam00413 154 IQQL 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 45-205 1.89e-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: 95.50  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226     45 RAKRWKKHTLTWQLQTqNLLDPDVfivRNTMHRAFNEWSTVSSVDFREIPPDlvtkqpPDIYIAFEKGEHsdgFPFdgqd 124
Cdd:smart00235   1 GSKKWPKGTVPYVIDS-SSLSPEE---REAIAKALAEWSDVTCIRFVERTGT------ADIYISFGSGDS---GCT---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226    125 gvVAHAFYPrDGRLHFDaEEQWSLNsvegvnlFQTAVHEIGHLLGLEHSMDVRA---AMFAAKRPYDP-AFTLGDDDVRA 200
Cdd:smart00235  64 --LSHAGRP-GGDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTrNFDLSEDDSLG 132


                   ....*
gi 17555226    201 IRSLF 205
Cdd:smart00235 133 IPYDY 137
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
160-181 1.03e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.14  E-value: 1.03e-03
                         10        20
                 ....*....|....*....|..
gi 17555226  160 AVHEIGHLLGLEHSMDVRAAMF 181
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
160-181 3.76e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 3.76e-03
                        10        20
                ....*....|....*....|..
gi 17555226 160 AVHEIGHLLGLEHSMDVRAAMF 181
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMH 148
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 160-180 6.58e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.54  E-value: 6.58e-03
                         10        20
                 ....*....|....*....|.
gi 17555226  160 AVHEIGHLLGLEHSMDVRAAM 180
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-205 7.80e-69

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: 210.14  E-value: 7.80e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  48 RWKKHTLTWQLQTQNLlDPDVFIVRNTMHRAFNEWSTVSSVDFREIPPDlvtkQPPDIYIAFEKGEHSDGFPFDGQDGVV 127
Cdd:cd04278   1 KWSKTNLTYRILNYPP-DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG----QEADIRISFARGNHGDGYPFDGPGGTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226 128 AHAFYP--RDGRLHFDAEEQWSLNS-VEGVNLFQTAVHEIGHLLGLEHSMDVRAAMFAAKRPYDPAFTLGDDDVRAIRSL 204
Cdd:cd04278  76 AHAFFPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQAL 155


                .
gi 17555226 205 F 205
Cdd:cd04278 156 Y 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 48-204 5.43e-54

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: 172.42  E-value: 5.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226    48 RWKKHTLTWQLQTQ-NLLDPDVfiVRNTMHRAFNEWSTVSSVDFREippdlVTKQPPDIYIAFEKGEHSDGFPFDGQDGV 126
Cdd:pfam00413   1 KWRKKNLTYRILNYtPDLPRAE--VRRAIRRAFKVWSEVTPLTFTE-----VSTGEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226   127 VAHAFYP---RDGRLHFDAEEQWSLNSV--EGVNLFQTAVHEIGHLLGLEHSMDVRAAMFAAKRPYDPA-FTLGDDDVRA 200
Cdd:pfam00413  74 LAHAFFPgpgLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKG 153


                  ....
gi 17555226   201 IRSL 204
Cdd:pfam00413 154 IQQL 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 45-205 1.89e-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: 95.50  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226     45 RAKRWKKHTLTWQLQTqNLLDPDVfivRNTMHRAFNEWSTVSSVDFREIPPDlvtkqpPDIYIAFEKGEHsdgFPFdgqd 124
Cdd:smart00235   1 GSKKWPKGTVPYVIDS-SSLSPEE---REAIAKALAEWSDVTCIRFVERTGT------ADIYISFGSGDS---GCT---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226    125 gvVAHAFYPrDGRLHFDaEEQWSLNsvegvnlFQTAVHEIGHLLGLEHSMDVRA---AMFAAKRPYDP-AFTLGDDDVRA 200
Cdd:smart00235  64 --LSHAGRP-GGDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTrNFDLSEDDSLG 132


                   ....*
gi 17555226    201 IRSLF 205
Cdd:smart00235 133 IPYDY 137
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 53-206 1.16e-10

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: 58.62  E-value: 1.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  53 TLTWQLQTQNLLDPDVF-IVRNTMHRAFNEWSTVSSVDFREIPPDlvtKQPPDIYIAFEkgehsDGFPFDGQDGVVAHAF 131
Cdd:cd04279   3 PIRVYIDPTPAPPDSRAqSWLQAVKQAAAEWENVGPLKFVYNPEE---DNDADIVIFFD-----RPPPVGGAGGGLARAG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226 132 YPRDGRLHFDAEEQWSLNSV-----EGVNLFQTAVHEIGHLLGLEHS----MDVRAAMFAAKRPYDPafTLGDDDVRAIR 202
Cdd:cd04279  75 FPLISDGNRKLFNRTDINLGpgqprGAENLQAIALHELGHALGLWHHsdrpEDAMYPSQGQGPDGNP--TLSARDVATLK 152


                ....
gi 17555226 203 SLFP 206
Cdd:cd04279 153 RLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 78-175 5.02e-10

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: 57.43  E-value: 5.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  78 AFNEWSTVSSVDFREIPPDLVTkqppDIYIAFEKGEHSDGFpfdgqdgvvAHAFYP-------RDGRLHFDAeeQWSLNS 150
Cdd:cd04277  42 ALEAWEDVADIDFVEVSDNSGA----DIRFGNSSDPDGNTA---------GYAYYPgsgsgtaYGGDIWFNS--SYDTNS 106

                        90       100
                ....*....|....*....|....*.
gi 17555226 151 VEGVNL-FQTAVHEIGHLLGLEHSMD 175
Cdd:cd04277 107 DSPGSYgYQTIIHEIGHALGLEHPGD 132
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 71-204 3.34e-07

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: 49.03  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  71 VRNTMHRAFNEWSTVSSVDFREIppdlVTKQPPDIYIafekGEHSDGFPFDGQDGVVAHAFYPRDGRLHFDAEEQWSLN- 149
Cdd:cd04268  16 LRAAILDAIEAWNKAFAIGFKNA----NDVDPADIRY----SVIRWIPYNDGTWSYGPSQVDPLTGEILLARVYLYSSFv 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555226 150 SVEGVNLFQTAVHEIGHLLGLEHS----------------------MDVRAAMFAAKRPYDPAFTLGDDDVRAIRSL 204
Cdd:cd04268  88 EYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekgdtssvMDYAPSNFSIQLGDGQKYTIGPYDIAAIKKL 164
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 71-175 6.47e-05

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: 42.51  E-value: 6.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226  71 VRNTMHRAFNEWSTVSSVDFREIPPDLvtkQPPDIYIAFEKGEHSDGFpfdgqdgvVAHAFYPRDGrlhfDAEEQWSL-- 148
Cdd:cd00203  23 IQSLILIAMQIWRDYLNIRFVLVGVEI---DKADIAILVTRQDFDGGT--------GGWAYLGRVC----DSLRGVGVlq 87

                        90       100
                ....*....|....*....|....*...
gi 17555226 149 -NSVEGVNLFQTAVHEIGHLLGLEHSMD 175
Cdd:cd00203  88 dNQSGTKEGAQTIAHELGHALGFYHDHD 115
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 104-199 3.51e-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: 40.36  E-value: 3.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555226 104 DIYiafekgEHSDGFPF---DGQDGVVAHAFYprdgRLHFDAEEQWSLNSVEGVNLFQTAVHEIGHLLGLEHSMDVRAAM 180
Cdd:cd11375  78 DLY------EPGLNFVFglaDGGSGVAVVSTA----RLRPEFYGLPPDEGLFLERLLKEAVHELGHLFGLDHCPYYACVM 147

                        90       100
                ....*....|....*....|
gi 17555226 181 -FAAkrpydpafTLGDDDVR 199
Cdd:cd11375 148 nFSN--------SLEETDRK 159
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
160-181 1.03e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.14  E-value: 1.03e-03
                         10        20
                 ....*....|....*....|..
gi 17555226  160 AVHEIGHLLGLEHSMDVRAAMF 181
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
160-181 3.76e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 3.76e-03
                        10        20
                ....*....|....*....|..
gi 17555226 160 AVHEIGHLLGLEHSMDVRAAMF 181
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMH 148
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 160-180 6.58e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.54  E-value: 6.58e-03
                         10        20
                 ....*....|....*....|.
gi 17555226  160 AVHEIGHLLGLEHSMDVRAAM 180
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
 
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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