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Conserved domains on  [gi|15223067|ref|NP_177174|]
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matrix metalloproteinase [Arabidopsis thaliana]

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 ...
 163-324 2.21e-70

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: 217.48  E-value: 2.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   163 RWprNRRDLTYAFDPKNPL--TEEVKSVFSRAFGRWSDVTALNFTLSeSFSTSDITIGFYTGDHGDGEPFDGVLGTLAHA 240
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   241 FSP---PSGKFHLDADENWVVSGDLDSflsvtaAVDLESVAVHEIGHLLGLGHSSVEESIMYPTI-TTGKRKVDLTNDDV 316
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPPH------GINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDI 151


                  ....*...
gi 15223067   317 EGIQYLYG 324
Cdd:pfam00413 152 KGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 62-115 3.08e-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: 3.08e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15223067    62 IKKYFQRFGYIPetfsGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHI 115
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 163-324 2.21e-70

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: 217.48  E-value: 2.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   163 RWprNRRDLTYAFDPKNPL--TEEVKSVFSRAFGRWSDVTALNFTLSeSFSTSDITIGFYTGDHGDGEPFDGVLGTLAHA 240
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   241 FSP---PSGKFHLDADENWVVSGDLDSflsvtaAVDLESVAVHEIGHLLGLGHSSVEESIMYPTI-TTGKRKVDLTNDDV 316
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPPH------GINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDI 151


                  ....*...
gi 15223067   317 EGIQYLYG 324
Cdd:pfam00413 152 KGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 163-324 6.03e-64

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: 200.89  E-value: 6.03e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 163 RWprNRRDLTYAFD--PKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHA 240
Cdd:cd04278   1 KW--SKTNLTYRILnyPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 241 FSP--PSGKFHLDADENWVVSGDLDsflsvtaAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEG 318
Cdd:cd04278  79 FFPggIGGDIHFDDDEQWTLGSDSG-------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRG 151


                ....*.
gi 15223067 319 IQYLYG 324
Cdd:cd04278 152 IQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 160-325 1.12e-28

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: 108.59  E-value: 1.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067    160 GEPRWPRNRrdLTYAFDpKNPLTEEVKSVFSRAFGRWSDVTALNFTlsESFSTSDITIGFYTGDHGdgePFdgvlgtLAH 239
Cdd:smart00235   1 GSKKWPKGT--VPYVID-SSSLSPEEREAIAKALAEWSDVTCIRFV--ERTGTADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067    240 AFsPPSGKFHLDaDENWVVSGDldsflsvtaavdlesVAVHEIGHLLGLGHSSVE---ESIMYPTIT-TGKRKVDLTNDD 315
Cdd:smart00235  67 AG-RPGGDQHLS-LGNGCINTG---------------VAAHELGHALGLYHEQSRsdrDNYMYINYTnIDTRNFDLSEDD 129

                          170
                   ....*....|
gi 15223067    316 VEGIQYLYGA 325
Cdd:smart00235 130 SLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 62-115 3.08e-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: 3.08e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15223067    62 IKKYFQRFGYIPetfsGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHI 115
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 276-300 2.34e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.06  E-value: 2.34e-05
                        10        20
                ....*....|....*....|....*.
gi 15223067 276 SVAVHEIGHLLGL-GHSSVEESIMYP 300
Cdd:COG5549 184 ATARHELGHALGIwGHSPSPTDAMYF 209
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
278-299 3.59e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 40.68  E-value: 3.59e-04
                         10        20
                 ....*....|....*....|..
gi 15223067  278 AVHEIGHLLGLGHSSVEESIMY 299
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 163-324 2.21e-70

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: 217.48  E-value: 2.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   163 RWprNRRDLTYAFDPKNPL--TEEVKSVFSRAFGRWSDVTALNFTLSeSFSTSDITIGFYTGDHGDGEPFDGVLGTLAHA 240
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067   241 FSP---PSGKFHLDADENWVVSGDLDSflsvtaAVDLESVAVHEIGHLLGLGHSSVEESIMYPTI-TTGKRKVDLTNDDV 316
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPPH------GINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDI 151


                  ....*...
gi 15223067   317 EGIQYLYG 324
Cdd:pfam00413 152 KGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 163-324 6.03e-64

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: 200.89  E-value: 6.03e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 163 RWprNRRDLTYAFD--PKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHA 240
Cdd:cd04278   1 KW--SKTNLTYRILnyPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 241 FSP--PSGKFHLDADENWVVSGDLDsflsvtaAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEG 318
Cdd:cd04278  79 FFPggIGGDIHFDDDEQWTLGSDSG-------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRG 151


                ....*.
gi 15223067 319 IQYLYG 324
Cdd:cd04278 152 IQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 160-325 1.12e-28

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: 108.59  E-value: 1.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067    160 GEPRWPRNRrdLTYAFDpKNPLTEEVKSVFSRAFGRWSDVTALNFTlsESFSTSDITIGFYTGDHGdgePFdgvlgtLAH 239
Cdd:smart00235   1 GSKKWPKGT--VPYVID-SSSLSPEEREAIAKALAEWSDVTCIRFV--ERTGTADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067    240 AFsPPSGKFHLDaDENWVVSGDldsflsvtaavdlesVAVHEIGHLLGLGHSSVE---ESIMYPTIT-TGKRKVDLTNDD 315
Cdd:smart00235  67 AG-RPGGDQHLS-LGNGCINTG---------------VAAHELGHALGLYHEQSRsdrDNYMYINYTnIDTRNFDLSEDD 129

                          170
                   ....*....|
gi 15223067    316 VEGIQYLYGA 325
Cdd:smart00235 130 SLGIPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 179-324 2.19e-13

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: 67.83  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 179 NPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGdgepfdgvlGTLAHAFSPPSGkfhldadENWVV 258
Cdd:cd04277  29 AALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDG---------NTAGYAYYPGSG-------SGTAY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 259 SGdlDSFLSVTAAVDLES-------VAVHEIGHLLGLGHS----------------SVEESIM-------YPTITTGKRK 308
Cdd:cd04277  93 GG--DIWFNSSYDTNSDSpgsygyqTIIHEIGHALGLEHPgdynggdpvpptyaldSREYTVMsynsgygNGASAGGGYP 170

                       170
                ....*....|....*.
gi 15223067 309 VDLTNDDVEGIQYLYG 324
Cdd:cd04277 171 QTPMLLDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 191-324 2.12e-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: 64.40  E-value: 2.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 191 RAFGRWSDVTALNFTLSESFST-SDITIgfytgDHGDGEPFDGVLGTLAHAFSPPSGKFhlDADENWVVSGDLDSFLSVT 269
Cdd:cd04279  28 QAAAEWENVGPLKFVYNPEEDNdADIVI-----FFDRPPPVGGAGGGLARAGFPLISDG--NRKLFNRTDINLGPGQPRG 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15223067 270 AAvDLESVAVHEIGHLLGLGHSSV-EESIMYPT-ITTGKRKVDLTNDDVEGIQYLYG 324
Cdd:cd04279 101 AE-NLQAIALHELGHALGLWHHSDrPEDAMYPSqGQGPDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 62-115 3.08e-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: 3.08e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15223067    62 IKKYFQRFGYIPetfsGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHI 115
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 171-323 1.83e-08

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: 53.27  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 171 LTYAFDPKNPltEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDgepfDGVLGTLAHAFSPPSGKFHL 250
Cdd:cd04268   4 ITYYIDDSVP--DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGEILL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 251 dadeNWVVSGDLDSFLSVTAavdLESVAVHEIGHLLGLGHSS----------------VEESIMYPT------ITTGKRK 308
Cdd:cd04268  78 ----ARVYLYSSFVEYSGAR---LRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYApsnfsiQLGDGQK 150

                       170
                ....*....|....*
gi 15223067 309 VDLTNDDVEGIQYLY 323
Cdd:cd04268 151 YTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 179-323 8.26e-08

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: 51.37  E-value: 8.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 179 NPLTEEVKSVFSRAFGRWSDVTALNFTLS-ESFSTSDITIGFYTGDHGdgepfdgvLGTLAHAFSPPSgkfhLDADENWV 257
Cdd:cd00203  17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVgVEIDKADIAILVTRQDFD--------GGTGGWAYLGRV----CDSLRGVG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 258 VSGDLDSFLSVTAAVdlesvAVHEIGHLLGLGHSSVEE--------------------SIMYPTITTGK--RKVDLTNDD 315
Cdd:cd00203  85 VLQDNQSGTKEGAQT-----IAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKGSFSdgQRKDFSQCD 159


                ....*...
gi 15223067 316 VEGIQYLY 323
Cdd:cd00203 160 IDQINKLY 167
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 276-300 2.34e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.06  E-value: 2.34e-05
                        10        20
                ....*....|....*....|....*.
gi 15223067 276 SVAVHEIGHLLGL-GHSSVEESIMYP 300
Cdd:COG5549 184 ATARHELGHALGIwGHSPSPTDAMYF 209
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 165-290 1.05e-04

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: 42.75  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223067 165 PRNRRDLTYAF--DPKNPLTEEVKSvfsrAFGRWSDVTALNFTLSESFStSDITIGFYTGDhgdgepfdG---VLGTLAH 239
Cdd:cd04327   3 WRNGTVLRIAFlgGPDAFLKDKVRA----AAREWLPYANLKFKFVTDAD-ADIRISFTPGD--------GywsYVGTDAL 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15223067 240 AFsppsgkfhlDADENwvvSGDLDSFLSVTAAVDLESVAVHEIGHLLGLGH 290
Cdd:cd04327  70 LI---------GADAP---TMNLGWFTDDTPDPEFSRVVLHEFGHALGFIH 108
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
278-299 3.59e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 40.68  E-value: 3.59e-04
                         10        20
                 ....*....|....*....|..
gi 15223067  278 AVHEIGHLLGLGHSSVEESIMY 299
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
277-301 7.25e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 7.25e-04
                        10        20
                ....*....|....*....|....*
gi 15223067 277 VAVHEIGHLLGLGHSSVEESIMYPT 301
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 277-301 1.63e-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: 38.82  E-value: 1.63e-03
                        10        20
                ....*....|....*....|....*
gi 15223067 277 VAVHEIGHLLGLGHSSVEESIMYPT 301
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVMNFS 150
 
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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