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Conserved domains on  [gi|30348960|ref|NP_536701|]
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matrix metalloproteinase-28 isoform 1 precursor [Mus musculus]

Protein Classification

PG_binding_1 and ZnMc_MMP domain-containing protein( domain architecture ID 10477998)

protein containing domains PG_binding_1, ZnMc_MMP, and HX

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 4.61e-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: 4.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30348960 209 FLP--RRGEAHFDGDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278  79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX super family cl02471
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-500 3.93e-28

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.


The actual alignment was detected with superfamily member cd00094:

Pssm-ID: 413329 [Multi-domain]  Cd Length: 194  Bit Score: 110.86  E-value: 3.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 321 PKYCHS-SFDAITV---------GSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGTK 390
Cdd:cd00094   1 PDACDPlSFDAVTTlrgelyffkGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 391 SVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDGS 466
Cdd:cd00094  81 LEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDGY 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 30348960 467 IIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 500
Cdd:cd00094 161 YYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 7.81e-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: 43.27  E-value: 7.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    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 4.61e-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: 4.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30348960 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 7.24e-67

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: 212.48  E-value: 7.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960   129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLAnaFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYP--FDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960   209 FLP---RRGEAHFDGDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 30348960   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. ...
 321-500 3.93e-28

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: 110.86  E-value: 3.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 321 PKYCHS-SFDAITV---------GSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGTK 390
Cdd:cd00094   1 PDACDPlSFDAVTTlrgelyffkGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 391 SVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDGS 466
Cdd:cd00094  81 LEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDGY 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 30348960 467 IIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 500
Cdd:cd00094 161 YYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 126-285 9.55e-24

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: 9.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    126 PGNKWYKQHLSYRLVNWPErlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglanafdgpGGAL 205
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    206 AHAFLPRrGEAHFDgDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKKLGRDAL-LSWDDVLAVQS 281
Cdd:smart00235  65 SHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPY 135


                   ....
gi 30348960    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 7.81e-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: 43.27  E-value: 7.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    31 ELRQEAEAFLEKYGYLSEqgskaPASAQF----RNAIREFQWISQLPLSGVLDQATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFgpstEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.12e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 47.66  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960  158 AFQLWSNVSALEFWEAPATGPADIrlTFfqGDHNDGLAnafdgpggalAHAFLPRRGEAhfDGDERWSLSRRRGRNLFVV 237
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF--GNYSDSGQ----------AYAYLPGTSDV--SGQSWYNYNSDYIRNLTPD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960  238 --------LAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KKLGRD--------ALLswDDVLAV 279
Cdd:NF035945 152 lgnygrqtLTHEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DDIAAI 228


                 ....*
gi 30348960  280 QSLYG 284
Cdd:NF035945 229 QKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
193-260 3.35e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 44.56  E-value: 3.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30348960 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. ...
 366-395 6.69e-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: 37.55  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 30348960   366 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGF 395
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGY 32
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-398 1.43e-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: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 30348960    366 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGFAQL 398
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 3.03e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 3.03e-03
                         10
                 ....*....|....*....
gi 30348960  240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 193-258 5.27e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30348960  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 4.61e-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: 4.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlaNAFDGPGGALAHA 208
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30348960 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 7.24e-67

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: 212.48  E-value: 7.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960   129 KWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLAnaFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYP--FDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960   209 FLP---RRGEAHFDGDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 30348960   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. ...
 321-500 3.93e-28

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: 110.86  E-value: 3.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 321 PKYCHS-SFDAITV---------GSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGTK 390
Cdd:cd00094   1 PDACDPlSFDAVTTlrgelyffkGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 391 SVWGFAQLCRAGGLPRHP---DAALFFPPLRRLVLFKGSRYYVL-AQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDGS 466
Cdd:cd00094  81 LEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYdEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDGY 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 30348960 467 IIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGC 500
Cdd:cd00094 161 YYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 126-285 9.55e-24

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: 9.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    126 PGNKWYKQHLSYRLVNWPErlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglanafdgpGGAL 205
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    206 AHAFLPRrGEAHFDgDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKKLGRDAL-LSWDDVLAVQS 281
Cdd:smart00235  65 SHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPY 135


                   ....
gi 30348960    282 LYGK 285
Cdd:smart00235 136 DYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 154-284 4.17e-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: 4.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 154 AVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFDGPGGAlahaFLPRRGEAHFDGDERWSLSRRRGRN 233
Cdd:cd04277  38 AARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYYPGSGS----GTAYGGDIWFNSSYDTNSDSPGSYG 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30348960 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 3.17e-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: 64.83  E-value: 3.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 149 PAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFdGPGGALahaflPRRGEAHFD----GDERW 224
Cdd:cd04268  14 DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSY-GPSQVD-----PLTGEILLArvylYSSFV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 225 SLSRRRGRNlfvVLAHEIGHTLGLTHSPApRALMAPYYkklgrDALLSWDDVLAVQSlygkPLGRSVATQLPGKVFTDFE 304
Cdd:cd04268  88 EYSGARLRN---TAEHELGHALGLRHNFA-ASDRDDNV-----DLLAEKGDTSSVMD----YAPSNFSIQLGDGQKYTIG 154


                ...
gi 30348960 305 AWD 307
Cdd:cd04268 155 PYD 157
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 150-283 2.64e-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: 2.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 150 AVRGAVRAAFQLWSNVSALEFWEAPAT-GPADIRLTFFQGDHNdglanafdgpGGALAHAFLPR-----RGEAHFDGDER 223
Cdd:cd00203  22 QIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRQDFD----------GGTGGWAYLGRvcdslRGVGVLQDNQS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 224 WslsrrrGRNLFVVLAHEIGHTLGLTHSP--------------------APRALMAPYY--KKLGRDALLSWDDVLAVQS 281
Cdd:cd00203  92 G------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKgsFSDGQRKDFSQCDIDQINK 165


                ..
gi 30348960 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 2.99e-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: 2.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 141 NWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGP-ADIRLtFFQGDHNDGLAnafdgpGGALAHAFlpRRGEAHFD 219
Cdd:cd04279  12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVI-FFDRPPPVGGA------GGGLARAG--FPLISDGN 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30348960 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 7.81e-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: 43.27  E-value: 7.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960    31 ELRQEAEAFLEKYGYLSEqgskaPASAQF----RNAIREFQWISQLPLSGVLDQATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFgpstEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.12e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 47.66  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960  158 AFQLWSNVSALEFWEAPATGPADIrlTFfqGDHNDGLAnafdgpggalAHAFLPRRGEAhfDGDERWSLSRRRGRNLFVV 237
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF--GNYSDSGQ----------AYAYLPGTSDV--SGQSWYNYNSDYIRNLTPD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960  238 --------LAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KKLGRD--------ALLswDDVLAV 279
Cdd:NF035945 152 lgnygrqtLTHEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DDIAAI 228


                 ....*
gi 30348960  280 QSLYG 284
Cdd:NF035945 229 QKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
193-260 3.35e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 44.56  E-value: 3.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30348960 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 1.68e-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: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 147 PEPaVRGAVRAAFQLW---------SNVSALEFWEAPATgPADIRLTFFQGDHNDGLANAFdgpGGALAHaflPRRGEAh 217
Cdd:cd04276  19 PEK-YRDAIREGVLYWnkafekagfKNAIIVKVLPDDAD-PGDIRYNVIRWIHSPNGGWAY---GPSVVD---PRTGEI- 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30348960 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 6.23e-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: 6.23e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 30348960 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. ...
 366-395 6.69e-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: 37.55  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 30348960   366 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGF 395
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGY 32
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-398 1.43e-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: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 30348960    366 AAVSLEDGDFYFFKGNRCWRFQGTKSVWGFAQL 398
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
188-253 1.75e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 39.71  E-value: 1.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30348960   188 GDHNDGLANAF---DGPGGALAHAFLPRRGEAHFDGDERWSLSR--RRGRNLFVVLAHEIGHTLGLTHSPA 253
Cdd:pfam13688  86 GTQNDDLAYLFlmtNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNvvVSTATEWQVFAHEIGHNFGAVHDCD 156
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 3.03e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 3.03e-03
                         10
                 ....*....|....*....
gi 30348960  240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 169-260 4.21e-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: 4.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 169 EFWEAPATGPADirltffqgDHNDGLANAFD-GPGGALAHAFLPRRGEAHFDGderwSLSRRRGRNLFV--VLAHEIGHT 245
Cdd:cd04267  77 SFSFWRAEGPIR--------HDNAVLLTAQDfIEGDILGLAYVGSMCNPYSSV----GVVEDTGFTLLTalTMAHELGHN 144

                        90       100
                ....*....|....*....|....*
gi 30348960 246 LGLTHSPAPRA----------LMAP 260
Cdd:cd04267 145 LGAEHDGGDELafecdgggnyIMAP 169
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 193-258 5.27e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30348960  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 5.48e-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: 5.48e-03
                          10
                  ....*....|....
gi 30348960   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 5.95e-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: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30348960 147 PEPAVRGAVRAAFQLWSNVSALEFWEApATGPADIRLTFfqgdhndglaNAFDGPGGALA-HAFLPRRGEA--HFDGDER 223
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFV-TDADADIRISF----------TPGDGYWSYVGtDALLIGADAPtmNLGWFTD 85

                        90       100       110
                ....*....|....*....|....*....|...
gi 30348960 224 WSLSRRRGRnlfVVLaHEIGHTLGLTH---SPA 253
Cdd:cd04327  86 DTPDPEFSR---VVL-HEFGHALGFIHehqSPA 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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