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Conserved domains on  [gi|998429207|ref|NP_001307229|]
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matrix metalloproteinase-28 isoform 3 precursor [Mus musculus]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 129-284 7.94e-74

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: 230.94  E-value: 7.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998429207 209 FLP--RRGEAHFDGDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-510 4.10e-33

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: 124.73  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 321 PKYCHS-SFDAITVDGQwRLYVFKGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGT 399
Cdd:cd00094    1 PDACDPlSFDAVTTLRG-ELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 400 KSVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDG 475
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 998429207 476 SIIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 510
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 9.14e-06

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: 42.89  E-value: 9.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   31 ELRQEAEAFLEKYGYLSEqgskaPASAQF----RNAIREFQWISQLPLSGVLDQATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFgpstEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 129-284 7.94e-74

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: 230.94  E-value: 7.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998429207 209 FLP--RRGEAHFDGDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-284 1.20e-66

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: 212.09  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207  129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLAnaFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYP--FDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207  209 FLP---RRGEAHFDGDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 998429207  283 YG 284
Cdd:pfam00413 158 YG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-510 4.10e-33

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: 124.73  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 321 PKYCHS-SFDAITVDGQwRLYVFKGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGT 399
Cdd:cd00094    1 PDACDPlSFDAVTTLRG-ELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 400 KSVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDG 475
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 998429207 476 SIIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 510
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 126-285 1.20e-23

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: 96.65  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   126 PGNKWYKQHLSYRLVNWPErlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglanafdgpGGAL 205
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   206 AHAFLPRrGEAHFDgDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKKLGRDAL-LSWDDVLAVQS 281
Cdd:smart00235  65 SHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPY 135


                   ....
gi 998429207   282 LYGK 285
Cdd:smart00235 136 DYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 9.14e-06

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: 42.89  E-value: 9.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   31 ELRQEAEAFLEKYGYLSEqgskaPASAQF----RNAIREFQWISQLPLSGVLDQATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFgpstEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.26e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 47.66  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqGDHNDGLAnafdgpggalAHAFLPRRGEAhfDGDERWSLSRRRGRNLFVV 237
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF--GNYSDSGQ----------AYAYLPGTSDV--SGQSWYNYNSDYIRNLTPD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 238 --------LAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KKLGRD--------ALLswDDVLAV 279
Cdd:NF035945 152 lgnygrqtLTHEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DDIAAI 228


                 ....*
gi 998429207 280 QSLYG 284
Cdd:NF035945 229 QKLYG 233
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-371 1.74e-05

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: 41.84  E-value: 1.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 998429207   328 FDAITVDGQWRLYVFKGSYFWEVTV-DGNVSEPRPLQKRWPGLPP 371
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPkRVDPGYPKLISSFFPGLPC 45
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
193-260 3.43e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 44.56  E-value: 3.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998429207 193 GLANafdgPGGALAHAFLPRRGEAHFDGDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913   89 GLAY----LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-405 7.75e-04

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: 37.16  E-value: 7.75e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 998429207  376 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGF 405
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGY 32
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 3.10e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 3.10e-03
                         10
                 ....*....|....*....
gi 998429207 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 193-258 5.40e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 5.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998429207 193 GLANafdgPGGALAHAFLPR-RGEahfdgderwSLSRRRGRNLF-------VVlaHEIGHTLGLTHSPAPRALM 258
Cdd:PRK13267  91 GLAY----PNLRGAVISTYRlRPE---------FYGNKPDSELFeervrkeVT--HELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 129-284 7.94e-74

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: 230.94  E-value: 7.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998429207 209 FLP--RRGEAHFDGDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-284 1.20e-66

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: 212.09  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207  129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLAnaFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYP--FDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207  209 FLP---RRGEAHFDGDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 998429207  283 YG 284
Cdd:pfam00413 158 YG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-510 4.10e-33

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: 124.73  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 321 PKYCHS-SFDAITVDGQwRLYVFKGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGT 399
Cdd:cd00094    1 PDACDPlSFDAVTTLRG-ELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 400 KSVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDG 475
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 998429207 476 SIIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 510
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 126-285 1.20e-23

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: 96.65  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   126 PGNKWYKQHLSYRLVNWPErlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglanafdgpGGAL 205
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   206 AHAFLPRrGEAHFDgDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKKLGRDAL-LSWDDVLAVQS 281
Cdd:smart00235  65 SHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPY 135


                   ....
gi 998429207   282 LYGK 285
Cdd:smart00235 136 DYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 154-284 4.90e-14

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: 70.52  E-value: 4.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 154 AVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFDGPGGAlahaFLPRRGEAHFDGDERWSLSRRRGRN 233
Cdd:cd04277   38 AARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYYPGSGS----GTAYGGDIWFNSSYDTNSDSPGSYG 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998429207 234 LFVVLaHEIGHTLGLTHS-------PAPRA---------LMA----PYYKKLGRDALLSW---DDVLAVQSLYG 284
Cdd:cd04277  114 YQTII-HEIGHALGLEHPgdynggdPVPPTyaldsreytVMSynsgYGNGASAGGGYPQTpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 149-307 3.68e-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: 64.44  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 149 PAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFdGPGGALahaflPRRGEAHFD----GDERW 224
Cdd:cd04268   14 DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSY-GPSQVD-----PLTGEILLArvylYSSFV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 225 SLSRRRGRNlfvVLAHEIGHTLGLTHSPApRALMAPYYkklgrDALLSWDDVLAVQSlygkPLGRSVATQLPGKVFTDFE 304
Cdd:cd04268   88 EYSGARLRN---TAEHELGHALGLRHNFA-ASDRDDNV-----DLLAEKGDTSSVMD----YAPSNFSIQLGDGQKYTIG 154


                 ...
gi 998429207 305 AWD 307
Cdd:cd04268  155 PYD 157
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 150-283 2.71e-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: 59.07  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 150 AVRGAVRAAFQLWSNVSALEFWEAPAT-GPADIRLTFFQGDHNdglanafdgpGGALAHAFLPR-----RGEAHFDGDER 223
Cdd:cd00203   22 QIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRQDFD----------GGTGGWAYLGRvcdslRGVGVLQDNQS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 224 WslsrrrGRNLFVVLAHEIGHTLGLTHSP--------------------APRALMAPYY--KKLGRDALLSWDDVLAVQS 281
Cdd:cd00203   92 G------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKgsFSDGQRKDFSQCDIDQINK 165


                 ..
gi 998429207 282 LY 283
Cdd:cd00203  166 LY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 141-284 3.56e-08

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: 52.84  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 141 NWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGP-ADIRLtFFQGDHNDGLAnafdgpGGALAHAFlpRRGEAHFD 219
Cdd:cd04279   12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVI-FFDRPPPVGGA------GGGLARAG--FPLISDGN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998429207 220 GDERWSL-------SRRRGRNLFVVLAHEIGHTLGLTH-SPAPRALMAPYYKKLG-RDALLSWDDVLAVQSLYG 284
Cdd:cd04279   83 RKLFNRTdinlgpgQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPdGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 9.14e-06

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: 42.89  E-value: 9.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207   31 ELRQEAEAFLEKYGYLSEqgskaPASAQF----RNAIREFQWISQLPLSGVLDQATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFgpstEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.26e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 47.66  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqGDHNDGLAnafdgpggalAHAFLPRRGEAhfDGDERWSLSRRRGRNLFVV 237
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF--GNYSDSGQ----------AYAYLPGTSDV--SGQSWYNYNSDYIRNLTPD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 238 --------LAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KKLGRD--------ALLswDDVLAV 279
Cdd:NF035945 152 lgnygrqtLTHEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DDIAAI 228


                 ....*
gi 998429207 280 QSLYG 284
Cdd:NF035945 229 QKLYG 233
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-371 1.74e-05

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: 41.84  E-value: 1.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 998429207   328 FDAITVDGQWRLYVFKGSYFWEVTV-DGNVSEPRPLQKRWPGLPP 371
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPkRVDPGYPKLISSFFPGLPC 45
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
193-260 3.43e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 44.56  E-value: 3.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998429207 193 GLANafdgPGGALAHAFLPRRGEAHFDGDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913   89 GLAY----LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 147-250 1.86e-04

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 42.70  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 147 PEPaVRGAVRAAFQLW---------SNVSALEFWEAPATgPADIRLTFFQGDHNDGLANAFdgpGGALAHaflPRRGEAh 217
Cdd:cd04276   19 PEK-YRDAIREGVLYWnkafekagfKNAIIVKVLPDDAD-PGDIRYNVIRWIHSPNGGWAY---GPSVVD---PRTGEI- 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 998429207 218 FDGD-------------ERWSLSRRRGRNLfvvLAHEIGHTLGLTH 250
Cdd:cd04276   90 LKADvilysgflrqdqlWYEDLLAASLRYL---LAHEVGHTLGLRH 132
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 218-260 6.56e-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: 6.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 998429207 218 FDGDERW-SLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:cd11375  109 FYGLPPDeGLFLER---LLKEAVHELGHLFGLDHCPYYACVMNF 149
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-405 7.75e-04

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: 37.16  E-value: 7.75e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 998429207  376 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGF 405
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGY 32
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-408 1.66e-03

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: 36.45  E-value: 1.66e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 998429207   376 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGFAQL 408
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
188-253 1.79e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 39.71  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998429207  188 GDHNDGLANAF---DGPGGALAHAFLPRRGEAHFDGDERWSLSR--RRGRNLFVVLAHEIGHTLGLTHSPA 253
Cdd:pfam13688  86 GTQNDDLAYLFlmtNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNvvVSTATEWQVFAHEIGHNFGAVHDCD 156
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 3.10e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 3.10e-03
                         10
                 ....*....|....*....
gi 998429207 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-371 3.24e-03

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: 35.62  E-value: 3.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 998429207  328 FDAITVDGQWRLYVFKGSYFWEvtVDGNVSE---PRPLqKRWPGLPP 371
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWR--FDPQRVEpgyPKLI-SDFPGLPC 44
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 169-260 4.31e-03

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 38.56  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 169 EFWEAPATGPADirltffqgDHNDGLANAFD-GPGGALAHAFLPRRGEAHFDGderwSLSRRRGRNLFV--VLAHEIGHT 245
Cdd:cd04267   77 SFSFWRAEGPIR--------HDNAVLLTAQDfIEGDILGLAYVGSMCNPYSSV----GVVEDTGFTLLTalTMAHELGHN 144

                         90       100
                 ....*....|....*....|....*
gi 998429207 246 LGLTHSPAPRA----------LMAP 260
Cdd:cd04267  145 LGAEHDGGDELafecdgggnyIMAP 169
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 193-258 5.40e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 5.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998429207 193 GLANafdgPGGALAHAFLPR-RGEahfdgderwSLSRRRGRNLF-------VVlaHEIGHTLGLTHSPAPRALM 258
Cdd:PRK13267  91 GLAY----PNLRGAVISTYRlRPE---------FYGNKPDSELFeervrkeVT--HELGHTLGLEHCDNPRCVM 149
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 237-250 5.83e-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: 38.77  E-value: 5.83e-03
                          10
                  ....*....|....
gi 998429207  237 VLAHEIGHTLGLTH 250
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 147-253 6.50e-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: 38.13  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998429207 147 PEPAVRGAVRAAFQLWSNVSALEFWEApATGPADIRLTFFQGDHN------DGLANAFDGPGGALAhaflprrgeahfdg 220
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFV-TDADADIRISFTPGDGYwsyvgtDALLIGADAPTMNLG-------------- 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998429207 221 derWSLSRRRGRNLFVVLAHEIGHTLGLTH---SPA 253
Cdd:cd04327   82 ---WFTDDTPDPEFSRVVLHEFGHALGFIHehqSPA 114
 
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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