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Conserved domains on  [gi|157818219|ref|NP_001099638|]
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matrix metalloproteinase-15 precursor [Rattus norvegicus]

Protein Classification

M10A family metallopeptidase( domain architecture ID 12021161)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix; also contains a possible peptidoglycan binding domain at the N-terminus and a DUF3377 domain at the C-terminal end

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 ...
 135-300 3.55e-88

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: 271.80  E-value: 3.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  135 WSNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVPYDdirlrrraEADIMVLFASGFHGDSSPFDGVGGF 214
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  215 LAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 157818219  295 IQQLYG 300
Cdd:pfam00413 154 IQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-555 5.30e-74

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 236.05  E-value: 5.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 363 PNICDG-NFDTVAVLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGNISAAYER-QDGHFVFFKGNRYWLFREA 440
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 441 NLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPIS-VWQGIPNSPKGAFLSNDa 519
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157818219 520 AYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGC 555
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 632-657 6.06e-12

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


:

Pssm-ID: 463374  Cd Length: 72  Bit Score: 61.18  E-value: 6.06e-12
                          10        20
                  ....*....|....*....|....*.
gi 157818219  632 FALVQMQRKGAPRMLLYCKRSLQEWV 657
Cdd:pfam11857  47 YAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-102 1.34e-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: 54.06  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818219   42 EDAEVYAAENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWM 102
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 135-300 3.55e-88

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: 271.80  E-value: 3.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  135 WSNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVPYDdirlrrraEADIMVLFASGFHGDSSPFDGVGGF 214
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  215 LAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 157818219  295 IQQLYG 300
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 135-300 6.08e-78

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: 245.19  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 135 WSNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVPYDDirlrrraEADIMVLFASGFHGDSSPFDGVGGF 214
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ-------EADIRISFARGNHGDGYPFDGPGGT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 215 LAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTdNFQLPEDDLRG 294
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151


                 ....*.
gi 157818219 295 IQQLYG 300
Cdd:cd04278  152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-555 5.30e-74

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 236.05  E-value: 5.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 363 PNICDG-NFDTVAVLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGNISAAYER-QDGHFVFFKGNRYWLFREA 440
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 441 NLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPIS-VWQGIPNSPKGAFLSNDa 519
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157818219 520 AYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGC 555
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 133-301 9.87e-34

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: 125.54  E-value: 9.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219   133 KTWSNYHLTFSIqnYTEKLGWYNsMEAVRRAFQVWEQVTPLVFQEVPyddirlrrrAEADIMVLFASGFHGdsspfdgvg 212
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT---------GTADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219   213 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgislflVAVHELGHALGLEHSSNPSA---IMAPFYQWMDTDNFQLPE 289
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 157818219   290 DDLRGIQQLYGS 301
Cdd:smart00235 128 DDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 632-657 6.06e-12

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 61.18  E-value: 6.06e-12
                          10        20
                  ....*....|....*....|....*.
gi 157818219  632 FALVQMQRKGAPRMLLYCKRSLQEWV 657
Cdd:pfam11857  47 YAIVQFQRKGTPRRLLYCKRSLQDWV 72
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 415-458 2.73e-10

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.71  E-value: 2.73e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 157818219   415 ISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIP 458
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 462-508 3.59e-10

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 55.27  E-value: 3.59e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 157818219  462 IDTAIWWEPtGHTFFFQADRYWRFNEETQhgDPGYPKPISVWQGIPN 508
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-102 1.34e-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: 54.06  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818219   42 EDAEVYAAENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWM 102
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
253-273 6.67e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.76  E-value: 6.67e-05
                         10        20
                 ....*....|....*....|.
gi 157818219 253 AVHELGHALGLEHSSNPSAIM 273
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
252-275 4.85e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.48  E-value: 4.85e-04
                         10        20
                 ....*....|....*....|....
gi 157818219 252 VAVHELGHALGLEHSSNPSAIMAP 275
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 253-273 1.88e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.88e-03
                         10        20
                 ....*....|....*....|.
gi 157818219 253 AVHELGHALGLEHSSNPSAIM 273
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 135-300 3.55e-88

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: 271.80  E-value: 3.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  135 WSNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVPYDdirlrrraEADIMVLFASGFHGDSSPFDGVGGF 214
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219  215 LAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 157818219  295 IQQLYG 300
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 135-300 6.08e-78

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: 245.19  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 135 WSNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVPYDDirlrrraEADIMVLFASGFHGDSSPFDGVGGF 214
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ-------EADIRISFARGNHGDGYPFDGPGGT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 215 LAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTdNFQLPEDDLRG 294
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151


                 ....*.
gi 157818219 295 IQQLYG 300
Cdd:cd04278  152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-555 5.30e-74

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 236.05  E-value: 5.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 363 PNICDG-NFDTVAVLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGNISAAYER-QDGHFVFFKGNRYWLFREA 440
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 441 NLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPIS-VWQGIPNSPKGAFLSNDa 519
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157818219 520 AYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGC 555
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 133-301 9.87e-34

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: 125.54  E-value: 9.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219   133 KTWSNYHLTFSIqnYTEKLGWYNsMEAVRRAFQVWEQVTPLVFQEVPyddirlrrrAEADIMVLFASGFHGdsspfdgvg 212
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT---------GTADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219   213 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgislflVAVHELGHALGLEHSSNPSA---IMAPFYQWMDTDNFQLPE 289
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 157818219   290 DDLRGIQQLYGS 301
Cdd:smart00235 128 DDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 153-300 7.74e-17

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: 78.27  E-value: 7.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 153 WYNSM-EAVRRAFQVWEQVTPLVFQEVPyddirlRRRAEADIMVLFasgfhGDSSPFDGVGGFLAHAYFPGPGLGGDT-- 229
Cdd:cd04279   18 RAQSWlQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlf 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157818219 230 -HFDADEPWTFSSTDLhgiSLFLVAVHELGHALGLEHSS-NPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYG 300
Cdd:cd04279   87 nRTDINLGPGQPRGAE---NLQAIALHELGHALGLWHHSdRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 128-300 8.85e-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: 79.00  E-value: 8.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 128 YTLTGKTWSNYHLTFSIQNYTEKLGWYNSM-EAVRRAFQVWEQVTPLVFQEVPYDDirlrrraEADIMvlfasgFHGDSS 206
Cdd:cd04277    6 YSFSNTGGPYSYGYGREEDTTNTAALSAAQqAAARDALEAWEDVADIDFVEVSDNS-------GADIR------FGNSSD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 207 PFDGVGGFlahAYFPGPG----LGGDTHFDADEPWTFSSTDLHGislFLVAVHELGHALGLEHS-----SNPSAIMAPFY 277
Cdd:cd04277   73 PDGNTAGY---AYYPGSGsgtaYGGDIWFNSSYDTNSDSPGSYG---YQTIIHEIGHALGLEHPgdyngGDPVPPTYALD 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157818219 278 QWMDT-------------------DNFQLpeDDLRGIQQLYG 300
Cdd:cd04277  147 SREYTvmsynsgygngasagggypQTPML--LDIAALQYLYG 186
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 632-657 6.06e-12

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 61.18  E-value: 6.06e-12
                          10        20
                  ....*....|....*....|....*.
gi 157818219  632 FALVQMQRKGAPRMLLYCKRSLQEWV 657
Cdd:pfam11857  47 YAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 158-299 2.23e-10

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: 59.84  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 158 EAVRRAFQVWEQVTPLVFQEVPYDDIRlrrraeADIMVLFASGFHGdsspfdgvGGFLAHAYFPG--PGLGGDTHFDADE 235
Cdd:cd00203   25 SLILIAMQIWRDYLNIRFVLVGVEIDK------ADIAILVTRQDFD--------GGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 236 PWTFSstdlhgisLFLVAVHELGHALGLEHSSNPSA--------------------IMAPFY-QWMDTDNFQLPEDDLRG 294
Cdd:cd00203   91 SGTKE--------GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162


                 ....*
gi 157818219 295 IQQLY 299
Cdd:cd00203  163 INKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 415-458 2.73e-10

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.71  E-value: 2.73e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 157818219   415 ISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIP 458
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 462-508 3.59e-10

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 55.27  E-value: 3.59e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 157818219  462 IDTAIWWEPtGHTFFFQADRYWRFNEETQhgDPGYPKPISVWQGIPN 508
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-102 1.34e-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: 54.06  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818219   42 EDAEVYAAENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWM 102
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 415-453 1.44e-09

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 53.72  E-value: 1.44e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 157818219  415 ISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSY 453
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 462-507 1.93e-08

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 50.70  E-value: 1.93e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 157818219   462 IDTAIWWEPtGHTFFFQADRYWRFNEETQhgDPGYPKPIS-VWQGIP 507
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 370-412 1.83e-07

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 47.95  E-value: 1.83e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157818219  370 FDTVAVLR-GEMFVFKGRWFWRVRHNRVLDNYPMPIGHFwRGLP 412
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 158-299 1.06e-06

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: 49.03  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 158 EAVRRAFQVWEQVTPLVFQEVpyddirlRRRAEADIMVlfasGFHGDSSPFDGVGGFLAHAYFPGPGlggdTHFDADEPW 237
Cdd:cd04268   18 AAILDAIEAWNKAFAIGFKNA-------NDVDPADIRY----SVIRWIPYNDGTWSYGPSQVDPLTG----EILLARVYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 238 TFSSTDLHGISLFLVAVHELGHALGLEHSSNPSA----------------IM--APFYQWMDTDNFQLP---EDDLRGIQ 296
Cdd:cd04268   83 YSSFVEYSGARLRNTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMdyAPSNFSIQLGDGQKYtigPYDIAAIK 162


                 ...
gi 157818219 297 QLY 299
Cdd:cd04268  163 KLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-413 2.19e-06

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 44.93  E-value: 2.19e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 157818219   377 RGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPG 413
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 518-554 3.34e-06

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 44.16  E-value: 3.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 157818219   518 DAAY------TYFYKGTKYWKFNNErlRMEPGHPKSILRDFMG 554
Cdd:smart00120   2 DAAFelrdgkTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 518-555 8.75e-06

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 42.94  E-value: 8.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 157818219  518 DAAY------TYFYKGTKYWKFNNErlRMEPGHPKSILRD-FMGC 555
Cdd:pfam00045   2 DAAFedrdgkTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
253-273 6.67e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.76  E-value: 6.67e-05
                         10        20
                 ....*....|....*....|.
gi 157818219 253 AVHELGHALGLEHSSNPSAIM 273
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
252-275 4.85e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.48  E-value: 4.85e-04
                         10        20
                 ....*....|....*....|....
gi 157818219 252 VAVHELGHALGLEHSSNPSAIMAP 275
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHF 149
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 158-275 6.91e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 41.59  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 158 EAVRRAFQVWEQVTPLvfQEVpyddirlRRRAEADIMVLFAS---GFHGDSSPfdgvGGFLAHAyfpgpglggDTHFDAD 234
Cdd:COG5549  104 AAVLQAIAEWNAYLPL--EVV-------ENPENADIIIVRSNpplTASPNPET----GARSAET---------TYEFYDT 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157818219 235 EPW---TFS---STDLHGISLFLVAVHELGHALGLE-HSSNPSAIMAP 275
Cdd:COG5549  162 GNIlshRFTillSPNQTGKYLLATARHELGHALGIWgHSPSPTDAMYF 209
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 248-275 7.81e-04

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: 40.74  E-value: 7.81e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 157818219 248 SLFL-----VAVHELGHALGLEHSSNPSAIMAP 275
Cdd:cd11375  117 GLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 253-273 1.88e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.88e-03
                         10        20
                 ....*....|....*....|.
gi 157818219 253 AVHELGHALGLEHSSNPSAIM 273
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 158-265 5.25e-03

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: 38.52  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818219 158 EAVRRAFQVWEQVTPLVFQEVpyddirlrRRAEADIMVLFASGfHGDSSpFDGVGGFLAHAYFPGPGLGGDTHFDADEpw 237
Cdd:cd04327   23 DKVRAAAREWLPYANLKFKFV--------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDP-- 90

                         90       100
                 ....*....|....*....|....*...
gi 157818219 238 TFSSTdlhgislflvAVHELGHALGLEH 265
Cdd:cd04327   91 EFSRV----------VLHEFGHALGFIH 108
 
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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