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Conserved domains on  [gi|15225398|ref|NP_182030|]
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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 ...
 133-296 3.34e-73

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: 223.65  E-value: 3.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   133 RWTRDVplkLTYAFSqeNLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETeDYVIADIKIGFFNGDHGDGEPFDGVLGVL 212
Cdd:pfam00413   1 KWRKKN---LTYRIL--NYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   213 AHTFSP---ENGRLHLDKAETWAVDfdeEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKP-RSKKVNLNMDDV 288
Cdd:pfam00413  75 AHAFFPgpgLGGDIHFDDDETWTVG---SDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPlDSKKFRLSQDDI 151


                  ....*...
gi 15225398   289 VGVQSLYG 296
Cdd:pfam00413 152 KGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-101 1.86e-08

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: 50.21  E-value: 1.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225398    45 SPDVSipEIKRHLQQYGYLPQNKESD-DVSFEQALVRYQKNLGLPITGKPDSDTLSQI 101
Cdd:pfam01471   2 GEDVK--ELQRYLNRLGYYPGPVDGYfGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 133-296 3.34e-73

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: 223.65  E-value: 3.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   133 RWTRDVplkLTYAFSqeNLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETeDYVIADIKIGFFNGDHGDGEPFDGVLGVL 212
Cdd:pfam00413   1 KWRKKN---LTYRIL--NYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   213 AHTFSP---ENGRLHLDKAETWAVDfdeEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKP-RSKKVNLNMDDV 288
Cdd:pfam00413  75 AHAFFPgpgLGGDIHFDDDETWTVG---SDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPlDSKKFRLSQDDI 151


                  ....*...
gi 15225398   289 VGVQSLYG 296
Cdd:pfam00413 152 KGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 133-296 7.28e-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: 204.75  E-value: 7.28e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 133 RWTRdvpLKLTYAFSqeNLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDGEPFDGVLGVL 212
Cdd:cd04278   1 KWSK---TNLTYRIL--NYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 213 AHTFSP--ENGRLHLDKAETWAVDFDEEkssvAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKPRSKKVNLNMDDVVG 290
Cdd:cd04278  76 AHAFFPggIGGDIHFDDDEQWTLGSDSG----GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRG 151


                ....*.
gi 15225398 291 VQSLYG 296
Cdd:cd04278 152 IQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-296 2.57e-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: 101.66  E-value: 2.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398    130 GRPRWTRDVplkLTYAFSQENLTPYlaptdIRRVFRRAFGKWASVIPVSFieTEDYVIADIKIGFFNGDHGdgePFdgvl 209
Cdd:smart00235   1 GSKKWPKGT---VPYVIDSSSLSPE-----EREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDSG---CT---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398    210 gvLAHTFSPeNGRLHLDkAETWAVDFDeekssvavdlesVAVHEIGHVLGLGHSSVK---DAAMYPTLKP-RSKKVNLNM 285
Cdd:smart00235  64 --LSHAGRP-GGDQHLS-LGNGCINTG------------VAAHELGHALGLYHEQSRsdrDNYMYINYTNiDTRNFDLSE 127

                          170
                   ....*....|.
gi 15225398    286 DDVVGVQSLYG 296
Cdd:smart00235 128 DDSLGIPYDYG 138
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-101 1.86e-08

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: 50.21  E-value: 1.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225398    45 SPDVSipEIKRHLQQYGYLPQNKESD-DVSFEQALVRYQKNLGLPITGKPDSDTLSQI 101
Cdd:pfam01471   2 GEDVK--ELQRYLNRLGYYPGPVDGYfGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 166-272 2.83e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 41.59  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 166 RAFGKWASVIPvsFIETEDYVIADIKIgfFNGDHGDGEPFDGVLG-VLAHT-FSPE-NGRLHLDKAETWAVDFDEEKSsv 242
Cdd:COG5549 108 QAIAEWNAYLP--LEVVENPENADIII--VRSNPPLTASPNPETGaRSAETtYEFYdTGNILSHRFTILLSPNQTGKY-- 181

                        90       100       110
                ....*....|....*....|....*....|.
gi 15225398 243 avdLESVAVHEIGHVLGL-GHSSVKDAAMYP 272
Cdd:COG5549 182 ---LLATARHELGHALGIwGHSPSPTDAMYF 209
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
250-271 1.43e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.43e-03
                         10        20
                 ....*....|....*....|..
gi 15225398  250 AVHEIGHVLGLGHSSVKDAAMY 271
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 234-265 1.54e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 39.61  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15225398  234 DFDEEKSSVAVDLESVAVHEIGHVLGLGhSSV 265
Cdd:NF038122 123 DPSDGISAGTYDFVGVAAHEIGHALGFV-SGV 153
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 46-102 6.83e-03

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 34.88  E-value: 6.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225398  46 PDVSipEIKRHLQQYGYLPqnKESDDVsF----EQALVRYQKNLGLPITGKPDSDTLSQIL 102
Cdd:COG3409  13 EDVR--ELQQRLNALGYYP--GPVDGI-FgpatEAAVRAFQRANGLPVDGIVGPATWAALR 68
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 133-296 3.34e-73

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: 223.65  E-value: 3.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   133 RWTRDVplkLTYAFSqeNLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETeDYVIADIKIGFFNGDHGDGEPFDGVLGVL 212
Cdd:pfam00413   1 KWRKKN---LTYRIL--NYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398   213 AHTFSP---ENGRLHLDKAETWAVDfdeEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKP-RSKKVNLNMDDV 288
Cdd:pfam00413  75 AHAFFPgpgLGGDIHFDDDETWTVG---SDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPlDSKKFRLSQDDI 151


                  ....*...
gi 15225398   289 VGVQSLYG 296
Cdd:pfam00413 152 KGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 133-296 7.28e-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: 204.75  E-value: 7.28e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 133 RWTRdvpLKLTYAFSqeNLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDGEPFDGVLGVL 212
Cdd:cd04278   1 KWSK---TNLTYRIL--NYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 213 AHTFSP--ENGRLHLDKAETWAVDFDEEkssvAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKPRSKKVNLNMDDVVG 290
Cdd:cd04278  76 AHAFFPggIGGDIHFDDDEQWTLGSDSG----GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRG 151


                ....*.
gi 15225398 291 VQSLYG 296
Cdd:cd04278 152 IQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-296 2.57e-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: 101.66  E-value: 2.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398    130 GRPRWTRDVplkLTYAFSQENLTPYlaptdIRRVFRRAFGKWASVIPVSFieTEDYVIADIKIGFFNGDHGdgePFdgvl 209
Cdd:smart00235   1 GSKKWPKGT---VPYVIDSSSLSPE-----EREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDSG---CT---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398    210 gvLAHTFSPeNGRLHLDkAETWAVDFDeekssvavdlesVAVHEIGHVLGLGHSSVK---DAAMYPTLKP-RSKKVNLNM 285
Cdd:smart00235  64 --LSHAGRP-GGDQHLS-LGNGCINTG------------VAAHELGHALGLYHEQSRsdrDNYMYINYTNiDTRNFDLSE 127

                          170
                   ....*....|.
gi 15225398    286 DDVVGVQSLYG 296
Cdd:smart00235 128 DDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 165-296 1.35e-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: 64.79  E-value: 1.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 165 RRAFGKWASVIPVSFIETEDYVI-ADIKIgffngDHGDGEPFDGVLGVLAHTFSPENGRLHLDKAETWAVDFDEEKSSVA 243
Cdd:cd04279  27 KQAAAEWENVGPLKFVYNPEEDNdADIVI-----FFDRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINLGPGQPRGA 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225398 244 VDLESVAVHEIGHVLGLGHSSV-KDAAMYPTLKPR-SKKVNLNMDDVVGVQSLYG 296
Cdd:cd04279 102 ENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGpDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 139-263 1.63e-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: 59.35  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 139 PLKLTYAFS------------QENLTPYLAPTD-IRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGdgepf 205
Cdd:cd04277   1 DTTLTYSFSntggpysygygrEEDTTNTAALSAaQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDG----- 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225398 206 dgvlGVLAHTFSPENGrlhLDKAETWAVDFDEEKSSVAVDLES----VAVHEIGHVLGLGHS 263
Cdd:cd04277  76 ----NTAGYAYYPGSG---SGTAYGGDIWFNSSYDTNSDSPGSygyqTIIHEIGHALGLEHP 130
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-101 1.86e-08

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: 50.21  E-value: 1.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225398    45 SPDVSipEIKRHLQQYGYLPQNKESD-DVSFEQALVRYQKNLGLPITGKPDSDTLSQI 101
Cdd:pfam01471   2 GEDVK--ELQRYLNRLGYYPGPVDGYfGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 156-264 1.35e-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: 50.57  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 156 APTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDgepfDGVLGVLAHTFSPENGRLHLDKAETWAVDF 235
Cdd:cd04268  12 VPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGEILLARVYLYSSFV 87

                        90       100
                ....*....|....*....|....*....
gi 15225398 236 DEEKSSVAvdleSVAVHEIGHVLGLGHSS 264
Cdd:cd04268  88 EYSGARLR----NTAEHELGHALGLRHNF 112
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 138-273 1.05e-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: 45.21  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 138 VPLKLTYAFSQENLTPYLAPTDIRRVFRRAFGKWASVIPVSF-IETEDYVIADIKIGFFNGDHGDGepfDGVLGVLAHTF 216
Cdd:cd00203   1 KVIPYVVVADDRDVEEENLSAQIQSLILIAMQIWRDYLNIRFvLVGVEIDKADIAILVTRQDFDGG---TGGWAYLGRVC 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225398 217 SPENGRLHLDKAETWAVDFDeekssvavdleSVAVHEIGHVLGLGHSSV-KDAAMYPT 273
Cdd:cd00203  78 DSLRGVGVLQDNQSGTKEGA-----------QTIAHELGHALGFYHDHDrKDRDDYPT 124
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 166-272 2.83e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 41.59  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225398 166 RAFGKWASVIPvsFIETEDYVIADIKIgfFNGDHGDGEPFDGVLG-VLAHT-FSPE-NGRLHLDKAETWAVDFDEEKSsv 242
Cdd:COG5549 108 QAIAEWNAYLP--LEVVENPENADIII--VRSNPPLTASPNPETGaRSAETtYEFYdTGNILSHRFTILLSPNQTGKY-- 181

                        90       100       110
                ....*....|....*....|....*....|.
gi 15225398 243 avdLESVAVHEIGHVLGL-GHSSVKDAAMYP 272
Cdd:COG5549 182 ---LLATARHELGHALGIwGHSPSPTDAMYF 209
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
249-273 6.70e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 6.70e-04
                        10        20
                ....*....|....*....|....*
gi 15225398 249 VAVHEIGHVLGLGHSSVKDAAMYPT 273
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
250-271 1.43e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.43e-03
                         10        20
                 ....*....|....*....|..
gi 15225398  250 AVHEIGHVLGLGHSSVKDAAMY 271
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 234-265 1.54e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 39.61  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15225398  234 DFDEEKSSVAVDLESVAVHEIGHVLGLGhSSV 265
Cdd:NF038122 123 DPSDGISAGTYDFVGVAAHEIGHALGFV-SGV 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 249-273 2.79e-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: 38.05  E-value: 2.79e-03
                        10        20
                ....*....|....*....|....*
gi 15225398 249 VAVHEIGHVLGLGHSSVKDAAMYPT 273
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVMNFS 150
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 246-280 2.90e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 39.16  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 15225398   246 LESVAVHEIGHVLGLGH---SSvkdaAMYPTLKPRSKK 280
Cdd:pfam16313  13 LRFVSAHEVGHTLGLRHnfaAS----SAYPVDSLRDKS 46
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 46-102 6.83e-03

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 34.88  E-value: 6.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225398  46 PDVSipEIKRHLQQYGYLPqnKESDDVsF----EQALVRYQKNLGLPITGKPDSDTLSQIL 102
Cdd:COG3409  13 EDVR--ELQQRLNALGYYP--GPVDGI-FgpatEAAVRAFQRANGLPVDGIVGPATWAALR 68
 
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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