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Conserved domains on  [gi|30688744|ref|NP_173824|]
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Matrixin family protein [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 ...
 167-329 2.24e-71

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: 220.18  E-value: 2.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   167 RWprNRRDLTYAFDPRNAL--TEEVKSVFSRAFTRWEEVTPLTFTRVeRFSTSDISIGFYSGEHGDGEPFDGPMRTLAHA 244
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   245 FSP---PTGHFHLDGEENWIVSGEggdgfisVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGR-RKVDLTTDD 320
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSD-------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDsKKFRLSQDD 150


                  ....*....
gi 30688744   321 VEGVQYLYG 329
Cdd:pfam00413 151 IKGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 64-116 2.01e-10

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: 55.98  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30688744    64 LKQYFQHFGYitetnLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLK 116
Cdd:pfam01471   8 LQRYLNRLGY-----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLA 55
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 167-329 2.24e-71

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: 220.18  E-value: 2.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   167 RWprNRRDLTYAFDPRNAL--TEEVKSVFSRAFTRWEEVTPLTFTRVeRFSTSDISIGFYSGEHGDGEPFDGPMRTLAHA 244
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   245 FSP---PTGHFHLDGEENWIVSGEggdgfisVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGR-RKVDLTTDD 320
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSD-------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDsKKFRLSQDD 150


                  ....*....
gi 30688744   321 VEGVQYLYG 329
Cdd:pfam00413 151 IKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 167-329 4.98e-66

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: 206.67  E-value: 4.98e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 167 RWprNRRDLTYAFD--PRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHA 244
Cdd:cd04278   1 KW--SKTNLTYRILnyPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 245 FSPPT--GHFHLDGEENWIVSgeggdgfiSVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVE 322
Cdd:cd04278  79 FFPGGigGDIHFDDDEQWTLG--------SDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIR 150


                ....*..
gi 30688744 323 GVQYLYG 329
Cdd:cd04278 151 GIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 164-330 3.01e-26

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: 102.43  E-value: 3.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744    164 GEPRWPRNRrdLTYAFDPRNaLTEEVKSVFSRAFTRWEEVTPLTFtrVERFSTSDISIGFYSGEHGdgePFdgpmrtLAH 243
Cdd:smart00235   1 GSKKWPKGT--VPYVIDSSS-LSPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744    244 AFsPPTGHFHLDgEENWivsgeggdgfisvseaVDLESVAVHEIGHLLGLGHSSVEGS---IMYPTIR-TGRRKVDLTTD 319
Cdd:smart00235  67 AG-RPGGDQHLS-LGNG----------------CINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTnIDTRNFDLSED 128

                          170
                   ....*....|.
gi 30688744    320 DVEGVQYLYGA 330
Cdd:smart00235 129 DSLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 64-116 2.01e-10

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: 55.98  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30688744    64 LKQYFQHFGYitetnLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLK 116
Cdd:pfam01471   8 LQRYLNRLGY-----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLA 55
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 281-305 5.61e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 43.91  E-value: 5.61e-05
                        10        20
                ....*....|....*....|....*.
gi 30688744 281 SVAVHEIGHLLGL-GHSSVEGSIMYP 305
Cdd:COG5549 184 ATARHELGHALGIwGHSPSPTDAMYF 209
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
283-308 1.10e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|....*...
gi 30688744  283 AVHEIGHLLGLGHSSVEGSIMY--PTIR 308
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMHfsNSLD 153
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 167-329 2.24e-71

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: 220.18  E-value: 2.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   167 RWprNRRDLTYAFDPRNAL--TEEVKSVFSRAFTRWEEVTPLTFTRVeRFSTSDISIGFYSGEHGDGEPFDGPMRTLAHA 244
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744   245 FSP---PTGHFHLDGEENWIVSGEggdgfisVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGR-RKVDLTTDD 320
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSD-------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDsKKFRLSQDD 150


                  ....*....
gi 30688744   321 VEGVQYLYG 329
Cdd:pfam00413 151 IKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 167-329 4.98e-66

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: 206.67  E-value: 4.98e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 167 RWprNRRDLTYAFD--PRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHA 244
Cdd:cd04278   1 KW--SKTNLTYRILnyPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 245 FSPPT--GHFHLDGEENWIVSgeggdgfiSVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVE 322
Cdd:cd04278  79 FFPGGigGDIHFDDDEQWTLG--------SDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIR 150


                ....*..
gi 30688744 323 GVQYLYG 329
Cdd:cd04278 151 GIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 164-330 3.01e-26

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: 102.43  E-value: 3.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744    164 GEPRWPRNRrdLTYAFDPRNaLTEEVKSVFSRAFTRWEEVTPLTFtrVERFSTSDISIGFYSGEHGdgePFdgpmrtLAH 243
Cdd:smart00235   1 GSKKWPKGT--VPYVIDSSS-LSPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744    244 AFsPPTGHFHLDgEENWivsgeggdgfisvseaVDLESVAVHEIGHLLGLGHSSVEGS---IMYPTIR-TGRRKVDLTTD 319
Cdd:smart00235  67 AG-RPGGDQHLS-LGNG----------------CINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTnIDTRNFDLSED 128

                          170
                   ....*....|.
gi 30688744    320 DVEGVQYLYGA 330
Cdd:smart00235 129 DSLGIPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 158-329 5.01e-17

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: 78.23  E-value: 5.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 158 HYSFFPGEPRWPRNRRDLTYAFDPrNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDgepfdgp 237
Cdd:cd04277   5 TYSFSNTGGPYSYGYGREEDTTNT-AALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGN------- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 238 mrTLAHAFSPPTGHFHLDGEENWIVSGEGGDGFISVSEAvdlESVAVHEIGHLLGLGHS----------------SVEGS 301
Cdd:cd04277  77 --TAGYAYYPGSGSGTAYGGDIWFNSSYDTNSDSPGSYG---YQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYT 151

                       170       180       190
                ....*....|....*....|....*....|....*
gi 30688744 302 IM-------YPTIRTGRRKVDLTTDDVEGVQYLYG 329
Cdd:cd04277 152 VMsynsgygNGASAGGGYPQTPMLLDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 195-329 7.18e-13

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: 65.94  E-value: 7.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 195 RAFTRWEEVTPLTFTRVERFST-SDISIGFYSGEHGDGEPFdgpmrTLAHAFSPPTGHFHLDGEENWIVSGeggdGFISV 273
Cdd:cd04279  28 QAAAEWENVGPLKFVYNPEEDNdADIVIFFDRPPPVGGAGG-----GLARAGFPLISDGNRKLFNRTDINL----GPGQP 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30688744 274 SEAVDLESVAVHEIGHLLGLGHSSVEGS-IMYPT-IRTGRRKVDLTTDDVEGVQYLYG 329
Cdd:cd04279  99 RGAENLQAIALHELGHALGLWHHSDRPEdAMYPSqGQGPDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 64-116 2.01e-10

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: 55.98  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30688744    64 LKQYFQHFGYitetnLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLK 116
Cdd:pfam01471   8 LQRYLNRLGY-----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLA 55
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 175-328 4.68e-09

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: 55.20  E-value: 4.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 175 LTYAFDprNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDgepfDGPMRTLAHAFSPPTGHFHL 254
Cdd:cd04268   4 ITYYID--DSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGEILL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 255 dgeeNWIVSGeggDGFISVSEAVdLESVAVHEIGHLLGLGHSS----------------VEGSIMYPT------IRTGRR 312
Cdd:cd04268  78 ----ARVYLY---SSFVEYSGAR-LRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYApsnfsiQLGDGQ 149

                       170
                ....*....|....*.
gi 30688744 313 KVDLTTDDVEGVQYLY 328
Cdd:cd04268 150 KYTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 183-328 4.25e-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: 52.52  E-value: 4.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 183 NALTEEVKSVFSRAFTRWEEVTPLTFTRV-ERFSTSDISIGFYSGEHGDGepfdgpmrTLAHAFSPPtghfhldgeenwI 261
Cdd:cd00203  17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVgVEIDKADIAILVTRQDFDGG--------TGGWAYLGR------------V 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688744 262 VSGEGGDGFISVSEAVDLESVAV--HEIGHLLGLGHSSVE--------------------GSIMYPTI--RTGRRKVDLT 317
Cdd:cd00203  77 CDSLRGVGVLQDNQSGTKEGAQTiaHELGHALGFYHDHDRkdrddyptiddtlnaedddyYSVMSYTKgsFSDGQRKDFS 156

                       170
                ....*....|.
gi 30688744 318 TDDVEGVQYLY 328
Cdd:cd00203 157 QCDIDQINKLY 167
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 281-305 5.61e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 43.91  E-value: 5.61e-05
                        10        20
                ....*....|....*....|....*.
gi 30688744 281 SVAVHEIGHLLGL-GHSSVEGSIMYP 305
Cdd:COG5549 184 ATARHELGHALGIwGHSPSPTDAMYF 209
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
282-306 1.07e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 1.07e-03
                        10        20
                ....*....|....*....|....*
gi 30688744 282 VAVHEIGHLLGLGHSSVEGSIMYPT 306
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
283-308 1.10e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|....*...
gi 30688744  283 AVHEIGHLLGLGHSSVEGSIMY--PTIR 308
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMHfsNSLD 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 282-306 1.53e-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: 39.20  E-value: 1.53e-03
                        10        20
                ....*....|....*....|....*
gi 30688744 282 VAVHEIGHLLGLGHSSVEGSIMYPT 306
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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