NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|213424542|pdb|3F19|A]
View 

Chain A, Macrophage metalloelastase

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 11995183)

M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

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 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 4-158 1.29e-94

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: 270.64  E-value: 1.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A          4 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPG 83
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A         84 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 4-158 1.29e-94

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: 270.64  E-value: 1.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A          4 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPG 83
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A         84 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 4-158 1.48e-80

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: 234.79  E-value: 1.48e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A        4 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDDHAFDGKGGILAHAFGP 82
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A       83 GsGIGGDAHFDEDEFWTTHS--GGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDiNTFRLSADDIRGIQSLYG 158
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 4-158 8.50e-36

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: 120.92  E-value: 8.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A           4 WRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGddhafdgkgGILAHAFGPG 83
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---------CTLSHAGRPG 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A          84 sgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:smart00235  72 ----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 28-144 2.48e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.22  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       28 AIRKAFQVWSNVTPLKFSKiNTGMADILVVFAR---GAHGDDHA----------FDGKGGILAHAF----GPgsgiggda 90
Cdd:COG5549 105 AVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRFtillSP-------- 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3F19_A       91 hfdedefwttHSGGTNLFLTAVHEIGHSLGL-GHSSDPKAVMFP----TYKYV---DINTFR 144
Cdd:COG5549 176 ----------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFsqvrNPPPIsprDINTLK 227
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
111-132 2.87e-06

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.92  E-value: 2.87e-06
                         10        20
                 ....*....|....*....|..
3F19_A       111 AVHEIGHSLGLGHSSDPKAVMF 132
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 111-140 8.12e-05

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 8.12e-05
                         10        20        30
                 ....*....|....*....|....*....|..
3F19_A       111 AVHEIGHSLGLGHSSDPKAVMF--PTYKYVDI 140
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMNfsNSVRDVDI 160
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 4-158 1.29e-94

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: 270.64  E-value: 1.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A          4 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPG 83
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A         84 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 4-158 1.48e-80

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: 234.79  E-value: 1.48e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A        4 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDDHAFDGKGGILAHAFGP 82
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A       83 GsGIGGDAHFDEDEFWTTHS--GGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDiNTFRLSADDIRGIQSLYG 158
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 4-158 8.50e-36

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: 120.92  E-value: 8.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A           4 WRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGddhafdgkgGILAHAFGPG 83
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---------CTLSHAGRPG 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3F19_A          84 sgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:smart00235  72 ----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 28-158 3.77e-19

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: 78.65  E-value: 3.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       28 AIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGDdhafdGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH---S 102
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGNRKLFNRTDINLGPgqpR 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
3F19_A      103 GGTNLFLTAVHEIGHSLGLGHSSD-PKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 158
Cdd:cd04279 100 GAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 28-158 5.19e-15

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: 68.60  E-value: 5.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       28 AIRKAFQVWSNVTPLKFSKI-NTGMADILVVFARGAHGDDHAFdgkggilAHAFGPGSGI--GGDAHFDEDEFWTTHSGG 104
Cdd:cd04277  38 AARDALEAWEDVADIDFVEVsDNSGADIRFGNSSDPDGNTAGY-------AYYPGSGSGTayGGDIWFNSSYDTNSDSPG 110

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3F19_A      105 TNLFLTAVHEIGHSLGLGHSSDPKA----------------VM----FPTYKYVDINTF--RLSADDIRGIQSLYG 158
Cdd:cd04277 111 SYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsGYGNGASAGGGYpqTPMLLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 8-157 3.16e-12

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: 61.00  E-value: 3.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A        8 YITYRI----NNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGddhafdgkGGILAHAFG 81
Cdd:cd00203   2 VIPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDFD--------GGTGGWAYL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       82 PGS--GIGGDAHFDEDEFWTThsggtNLFLTAVHEIGHSLGLGHSSDPKA--------------------VMFPTY-KYV 138
Cdd:cd00203  74 GRVcdSLRGVGVLQDNQSGTK-----EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFS 148

                       170
                ....*....|....*....
3F19_A      139 DINTFRLSADDIRGIQSLY 157
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 9-157 4.12e-12

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: 60.59  E-value: 4.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A        9 ITYRINNYTPDMNREdvdyAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDDHAfdgkGGILAHAFGPGSGig 87
Cdd:cd04268   4 ITYYIDDSVPDKLRA----AILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYNDGT----WSYGPSQVDPLTG-- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       88 gDAHFDEDEFWTTHSGGTNLFL--TAVHEIGHSLGLGHSSDPKA----------------VMFPTYKYVDINTF-----R 144
Cdd:cd04268  74 -EILLARVYLYSSFVEYSGARLrnTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMDYAPSNFSIQLGdgqkyT 152

                       170
                ....*....|...
3F19_A      145 LSADDIRGIQSLY 157
Cdd:cd04268 153 IGPYDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 28-144 2.48e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.22  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A       28 AIRKAFQVWSNVTPLKFSKiNTGMADILVVFAR---GAHGDDHA----------FDGKGGILAHAF----GPgsgiggda 90
Cdd:COG5549 105 AVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRFtillSP-------- 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3F19_A       91 hfdedefwttHSGGTNLFLTAVHEIGHSLGL-GHSSDPKAVMFP----TYKYV---DINTFR 144
Cdd:COG5549 176 ----------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFsqvrNPPPIsprDINTLK 227
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
111-134 1.67e-06

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 1.67e-06
                        10        20
                ....*....|....*....|....
3F19_A      111 AVHEIGHSLGLGHSSDPKAVMFPT 134
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
111-132 2.87e-06

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.92  E-value: 2.87e-06
                         10        20
                 ....*....|....*....|..
3F19_A       111 AVHEIGHSLGLGHSSDPKAVMF 132
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 110-134 1.03e-05

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: 43.05  E-value: 1.03e-05
                        10        20
                ....*....|....*....|....*
3F19_A      110 TAVHEIGHSLGLGHSSDPKAVMFPT 134
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVMNFS 150
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 111-140 8.12e-05

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 8.12e-05
                         10        20        30
                 ....*....|....*....|....*....|..
3F19_A       111 AVHEIGHSLGLGHSSDPKAVMF--PTYKYVDI 140
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMNfsNSVRDVDI 160
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
60-123 4.66e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 35.86  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3F19_A         60 RGAHGDDHAF-----DGKGGILAHAFGP-GSGIGGDAHFDeDEFWTTHSGGTNLFLTAVHEIGHSLGLGH 123
Cdd:pfam13688  85 RGTQNDDLAYlflmtNCSGGGLAWLGQLcNSGSAGSVSTR-VSGNNVVVSTATEWQVFAHEIGHNFGAVH 153
 
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