NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|116874798|emb|CAA77093|]
View 

MtN9 [Medicago truncatula]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 super family cl37987
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 128-273 8.87e-47

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


The actual alignment was detected with superfamily member pfam00413:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 155.08  E-value: 8.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  128 KWFPKgtkELTYGFLPESKI--SIDKVNVFRNAFTRWSQTTRvLKFSEAtSYDDADIKIGFYNISYNSKEVID----VVV 201
Cdd:pfam00413   1 KWRKK---NLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTP-LTFTEV-STGEADIMIGFGRGDHGDGYPFDgpggVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  202 SDFFINLRS-----------FTIRLEASKVWDLETVAMHQIGHLLGLDHSSDVESIMYPTIVPLHQKKVQITVSDNQAIQ 270
Cdd:pfam00413  76 HAFFPGPGLggdihfdddetWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQ 155


                  ...
gi 116874798  271 QLY 273
Cdd:pfam00413 156 QLY 158
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-101 1.24e-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: 53.29  E-value: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116874798   48 IKQHLYHFKYLQGlylvGFDDYLDNKTISAIKAYQQFFNLQVTGHLDTETLQQI 101
Cdd:pfam01471   8 LQRYLNRLGYYPG----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 128-273 8.87e-47

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: 155.08  E-value: 8.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  128 KWFPKgtkELTYGFLPESKI--SIDKVNVFRNAFTRWSQTTRvLKFSEAtSYDDADIKIGFYNISYNSKEVID----VVV 201
Cdd:pfam00413   1 KWRKK---NLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTP-LTFTEV-STGEADIMIGFGRGDHGDGYPFDgpggVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  202 SDFFINLRS-----------FTIRLEASKVWDLETVAMHQIGHLLGLDHSSDVESIMYPTIVPLHQKKVQITVSDNQAIQ 270
Cdd:pfam00413  76 HAFFPGPGLggdihfdddetWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQ 155


                  ...
gi 116874798  271 QLY 273
Cdd:pfam00413 156 QLY 158
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 128-273 3.90e-31

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: 114.61  E-value: 3.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 128 KWfpkGTKELTYGFLPE-SKISIDKV-NVFRNAFTRWSQTTrVLKFSEATSYDDADIKIGFYNISYNSKEVID----VVV 201
Cdd:cd04278    1 KW---SKTNLTYRILNYpPDLPRDDVrRAIARAFRVWSDVT-PLTFREVTSGQEADIRISFARGNHGDGYPFDgpggTLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 202 SDFFINLRSFTIRLEASKVW---------DLETVAMHQIGHLLGLDHSSDVESIMYPTIVPLHqKKVQITVSDNQAIQQL 272
Cdd:cd04278   77 HAFFPGGIGGDIHFDDDEQWtlgsdsggtDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQAL 155


                 .
gi 116874798 273 Y 273
Cdd:cd04278  156 Y 156
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 128-275 4.77e-10

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: 56.98  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798   128 KWfPKGTkeLTYgFLPESKISIDKVNVFRNAFTRWSQTTrVLKFSEATSydDADIKIGFYNI-SYNSKEVIDVVVSDFFI 206
Cdd:smart00235   4 KW-PKGT--VPY-VIDSSSLSPEEREAIAKALAEWSDVT-CIRFVERTG--TADIYISFGSGdSGCTLSHAGRPGGDQHL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116874798   207 NLRSFTIRLeaskvwdleTVAMHQIGHLLGLDHS---SDVESIMYPTIVPLHQKKVQITVSDNQAIQQLYTK 275
Cdd:smart00235  77 SLGNGCINT---------GVAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-101 1.24e-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: 53.29  E-value: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116874798   48 IKQHLYHFKYLQGlylvGFDDYLDNKTISAIKAYQQFFNLQVTGHLDTETLQQI 101
Cdd:pfam01471   8 LQRYLNRLGYYPG----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 56-101 3.70e-05

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 41.05  E-value: 3.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116874798  56 KYLQ------GLYLVGFDDYLDNKTISAIKAYQQFFNLQVTGHLDTETLQQI 101
Cdd:COG3409   16 RELQqrlnalGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
223-250 3.18e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 3.18e-03
                         10        20
                 ....*....|....*....|....*...
gi 116874798 223 LETVAMHQIGHLLGLDHSSDVESIMYPT 250
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 128-273 8.87e-47

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: 155.08  E-value: 8.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  128 KWFPKgtkELTYGFLPESKI--SIDKVNVFRNAFTRWSQTTRvLKFSEAtSYDDADIKIGFYNISYNSKEVID----VVV 201
Cdd:pfam00413   1 KWRKK---NLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTP-LTFTEV-STGEADIMIGFGRGDHGDGYPFDgpggVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798  202 SDFFINLRS-----------FTIRLEASKVWDLETVAMHQIGHLLGLDHSSDVESIMYPTIVPLHQKKVQITVSDNQAIQ 270
Cdd:pfam00413  76 HAFFPGPGLggdihfdddetWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQ 155


                  ...
gi 116874798  271 QLY 273
Cdd:pfam00413 156 QLY 158
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 128-273 3.90e-31

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: 114.61  E-value: 3.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 128 KWfpkGTKELTYGFLPE-SKISIDKV-NVFRNAFTRWSQTTrVLKFSEATSYDDADIKIGFYNISYNSKEVID----VVV 201
Cdd:cd04278    1 KW---SKTNLTYRILNYpPDLPRDDVrRAIARAFRVWSDVT-PLTFREVTSGQEADIRISFARGNHGDGYPFDgpggTLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 202 SDFFINLRSFTIRLEASKVW---------DLETVAMHQIGHLLGLDHSSDVESIMYPTIVPLHqKKVQITVSDNQAIQQL 272
Cdd:cd04278   77 HAFFPGGIGGDIHFDDDEQWtlgsdsggtDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQAL 155


                 .
gi 116874798 273 Y 273
Cdd:cd04278  156 Y 156
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 128-275 4.77e-10

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: 56.98  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798   128 KWfPKGTkeLTYgFLPESKISIDKVNVFRNAFTRWSQTTrVLKFSEATSydDADIKIGFYNI-SYNSKEVIDVVVSDFFI 206
Cdd:smart00235   4 KW-PKGT--VPY-VIDSSSLSPEEREAIAKALAEWSDVT-CIRFVERTG--TADIYISFGSGdSGCTLSHAGRPGGDQHL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116874798   207 NLRSFTIRLeaskvwdleTVAMHQIGHLLGLDHS---SDVESIMYPTIVPLHQKKVQITVSDNQAIQQLYTK 275
Cdd:smart00235  77 SLGNGCINT---------GVAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-101 1.24e-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: 53.29  E-value: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116874798   48 IKQHLYHFKYLQGlylvGFDDYLDNKTISAIKAYQQFFNLQVTGHLDTETLQQI 101
Cdd:pfam01471   8 LQRYLNRLGYYPG----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 156-273 1.28e-09

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: 55.93  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 156 RNAFTRWSQTTRVLKFSEATSYDDADIKIGFYNI--SYNSKEVIDVVV---SDFFINLRS--FTIRLE---ASKVWDLET 225
Cdd:cd04279   27 KQAAAEWENVGPLKFVYNPEEDNDADIVIFFDRPppVGGAGGGLARAGfplISDGNRKLFnrTDINLGpgqPRGAENLQA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 116874798 226 VAMHQIGHLLGLDHSSD-VESIMYPTIVPLHQKKVQITVSDNQAIQQLY 273
Cdd:cd04279  107 IALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLY 155
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 128-239 1.13e-08

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: 54.31  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 128 KWFPKGTKELTYGFLPESKISIDKVnvfRNAFTRWSQTTRvLKFSEATsYDDADIKIGFY----NISYNSKEVIDVVVSD 203
Cdd:cd04327    1 KLWRNGTVLRIAFLGGPDAFLKDKV---RAAAREWLPYAN-LKFKFVT-DADADIRISFTpgdgYWSYVGTDALLIGADA 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 116874798 204 FFINLRSFTIRLEASkvwDLETVAMHQIGHLLGLDH 239
Cdd:cd04327   76 PTMNLGWFTDDTPDP---EFSRVVLHEFGHALGFIH 108
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 134-273 5.70e-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: 48.65  E-value: 5.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 134 TKELTYGFlpESKISIDKVNVFRNAFTRWSQTTRVlKFSEATSYDDADIKIGFYN-ISYNS------KEVID----VVVS 202
Cdd:cd04268    1 KKPITYYI--DDSVPDKLRAAILDAIEAWNKAFAI-GFKNANDVDPADIRYSVIRwIPYNDgtwsygPSQVDpltgEILL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 203 DFFINLRSFTIRLEASKVwdleTVAMHQIGHLLGLDHSS----------------DVESIMYPT--IVPLHQKKVQ---I 261
Cdd:cd04268   78 ARVYLYSSFVEYSGARLR----NTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYApsNFSIQLGDGQkytI 153

                        170
                 ....*....|..
gi 116874798 262 TVSDNQAIQQLY 273
Cdd:cd04268  154 GPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 130-242 1.26e-05

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: 45.10  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 130 FPKGTKELTYGFLPESKISI------DKVNVFRNAFTRWSQTTRvLKFSEATSYDDADIKIGFYNIS---------YNSK 194
Cdd:cd04277    8 FSNTGGPYSYGYGREEDTTNtaalsaAQQAAARDALEAWEDVAD-IDFVEVSDNSGADIRFGNSSDPdgntagyayYPGS 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116874798 195 EVIDVVVSDFFINLRSFTIRLEASKVWdlETVAMHQIGHLLGLDHSSD 242
Cdd:cd04277   87 GSGTAYGGDIWFNSSYDTNSDSPGSYG--YQTIIHEIGHALGLEHPGD 132
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 56-101 3.70e-05

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 41.05  E-value: 3.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116874798  56 KYLQ------GLYLVGFDDYLDNKTISAIKAYQQFFNLQVTGHLDTETLQQI 101
Cdd:COG3409   16 RELQqrlnalGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
223-250 3.18e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 3.18e-03
                         10        20
                 ....*....|....*....|....*...
gi 116874798 223 LETVAMHQIGHLLGLDHSSDVESIMYPT 250
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 226-250 7.56e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 36.51  E-value: 7.56e-03
                         10        20
                 ....*....|....*....|....*
gi 116874798 226 VAMHQIGHLLGLDHSSDVESIMYPT 250
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFS 150
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 144-273 7.63e-03

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: 36.73  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116874798 144 ESKISIDKVNVFRNAFTRWSQTTRVlKFSEAT-SYDDADIKIGFYNISYNSKEVIDVVVSDFfINLRSFTIRLEASKVWD 222
Cdd:cd00203   16 EENLSAQIQSLILIAMQIWRDYLNI-RFVLVGvEIDKADIAILVTRQDFDGGTGGWAYLGRV-CDSLRGVGVLQDNQSGT 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116874798 223 LET--VAMHQIGHLLGLDHSSDVE--------------------SIMYPTIVP-LHQKKVQITVSDNQAIQQLY 273
Cdd:cd00203   94 KEGaqTIAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKGSfSDGQRKDFSQCDIDQINKLY 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH