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Conserved domains on  [gi|966988098|ref|XP_014971042|]
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neutrophil collagenase isoform X2 [Macaca mulatta]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

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 ...
 107-262 2.72e-91

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: 274.11  E-value: 2.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098  107 KWERTNLTYSILNYTPQLSETDVEGAIKKAFEVWSKASPLTFTRISQGQADINIAFFQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098  187 GQGIGGDAHFDAEETWTKTSTN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDINGIQAIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 4.22e-76

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: 236.44  E-value: 4.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 276 PKSCDPrLTFDAITTLRGEILFFKDEYFWRRHPHLQSVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWAVSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 356 DIQQGYPRDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGTFPGIENKVDAVFQ-QEH 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966988098 433 FFLFFSGPRYYAFDLIAE--RVTRVARANK-WLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-86 3.49e-10

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: 55.60  E-value: 3.49e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098   28 ENTKIVQDYLEKFYQLPSNQyqsTRKNGTSMiVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-262 2.72e-91

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: 274.11  E-value: 2.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098  107 KWERTNLTYSILNYTPQLSETDVEGAIKKAFEVWSKASPLTFTRISQGQADINIAFFQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098  187 GQGIGGDAHFDAEETWTKTSTN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDINGIQAIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 8.12e-80

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 244.42  E-value: 8.12e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 107 KWERTNLTYSILNYTPQLSETDVEGAIKKAFEVWSKASPLTFTRI-SQGQADINIAFFQRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098 186 PGqGIGGDAHFDAEETWTKTS--TNYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDINGIQAIYG 262
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 4.22e-76

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: 236.44  E-value: 4.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 276 PKSCDPrLTFDAITTLRGEILFFKDEYFWRRHPHLQSVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWAVSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 356 DIQQGYPRDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGTFPGIENKVDAVFQ-QEH 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966988098 433 FFLFFSGPRYYAFDLIAE--RVTRVARANK-WLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-263 2.13e-33

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: 122.84  E-value: 2.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098   104 GNPKWERTNLTYSIlnYTPQLSETDVEgAIKKAFEVWSKASPLTFTRISQGqADINIAFFQRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098   184 FQPGqgigGDAHFDaEETWTKTSTnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDINGIQAI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 966988098   261 YGP 263
Cdd:smart00235 137 YGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-86 3.49e-10

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: 55.60  E-value: 3.49e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098   28 ENTKIVQDYLEKFYQLPSNQyqsTRKNGTSMiVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-420 4.77e-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: 54.56  E-value: 4.77e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 966988098   377 IDAAVFYR-SKTYFFVNDQFWRYDNQRqfMEPGYPKSISGTFPGI 420
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 2.86e-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: 52.57  E-value: 2.86e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 966988098  377 IDAAVFYRS-KTYFFVNDQFWRYDNQRqfMEPGYPKSISgTFPGIEN 422
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-271 3.60e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.14  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 132 AIKKAFEVWSKAspLTFTRISQG-QADINIafFQRDHGDNSPFDGPNGI-LAHA-FQPGQGIGGDAHfdaeeTWT-KTST 207
Cdd:COG5549  105 AVLQAIAEWNAY--LPLEVVENPeNADIII--VRSNPPLTASPNPETGArSAETtYEFYDTGNILSH-----RFTiLLSP 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098 208 NY-NLFLVAA--HEFGHSLGL-AHSSDPGALMYpnyaFRETSN-YSLPQDDINGIQAIYGpssnpiQPT 271
Cdd:COG5549  176 NQtGKYLLATarHELGHALGIwGHSPSPTDAMY----FSQVRNpPPISPRDINTLKRIYQ------QPT 234
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-262 2.72e-91

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: 274.11  E-value: 2.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098  107 KWERTNLTYSILNYTPQLSETDVEGAIKKAFEVWSKASPLTFTRISQGQADINIAFFQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098  187 GQGIGGDAHFDAEETWTKTSTN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDINGIQAIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 8.12e-80

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 244.42  E-value: 8.12e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 107 KWERTNLTYSILNYTPQLSETDVEGAIKKAFEVWSKASPLTFTRI-SQGQADINIAFFQRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098 186 PGqGIGGDAHFDAEETWTKTS--TNYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDINGIQAIYG 262
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 4.22e-76

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: 236.44  E-value: 4.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 276 PKSCDPrLTFDAITTLRGEILFFKDEYFWRRHPHLQSVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWAVSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 356 DIQQGYPRDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGTFPGIENKVDAVFQ-QEH 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966988098 433 FFLFFSGPRYYAFDLIAE--RVTRVARANK-WLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-263 2.13e-33

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: 122.84  E-value: 2.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098   104 GNPKWERTNLTYSIlnYTPQLSETDVEgAIKKAFEVWSKASPLTFTRISQGqADINIAFFQRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098   184 FQPGqgigGDAHFDaEETWTKTSTnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDINGIQAI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 966988098   261 YGP 263
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 132-262 1.08e-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: 79.81  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 132 AIKKAFEVWSKASPLTFTRISQGQADINIAFFQRDhgdNSPFDGPNGILAHAFQPGQGIGGDA---HFDAEETWTKTSTN 208
Cdd:cd04279   25 AVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDR---PPPVGGAGGGLARAGFPLISDGNRKlfnRTDINLGPGQPRGA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966988098 209 YNLFLVAAHEFGHSLGLAHSSD-PGALMYPNYAFRETSNYSLPQDDINGIQAIYG 262
Cdd:cd04279  102 ENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 111-262 3.72e-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: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 111 TNLTYSILN--------YTPQLSETDVEG-------AIKKAFEVWSKASPLTFTRISQGQ-ADINIAFFQRDHGDNspfd 174
Cdd:cd04277    2 TTLTYSFSNtggpysygYGREEDTTNTAAlsaaqqaAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNT---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 175 gpngiLAHAFQPG----QGIGGDAHFDAEETWTKTST-NYNlFLVAAHEFGHSLGLAHSSDPGAL-MYPNYAFRETSNYS 248
Cdd:cd04277   78 -----AGYAYYPGsgsgTAYGGDIWFNSSYDTNSDSPgSYG-YQTIIHEIGHALGLEHPGDYNGGdPVPPTYALDSREYT 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966988098 249 L-----------------PQ----DDINGIQAIYG 262
Cdd:cd04277  152 VmsynsgygngasagggyPQtpmlLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 128-261 1.59e-11

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: 62.54  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 128 DVEGAIKKAFEVWSKASPLTFT--RISQGQADINIAFFQRDHgdnspfdgPNGILAHAFQPG--QGIGGDAHFDaeetwT 203
Cdd:cd00203   22 QIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGVGVLQ-----D 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098 204 KTSTNYNLFLVAAHEFGHSLGLAHSSD--------------------PGALMYP-NYAFRETSNYSLPQDDINGIQAIY 261
Cdd:cd00203   89 NQSGTKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYtKGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 113-261 6.86e-11

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 60.59  E-value: 6.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 113 LTYSILNYTPQlsetDVEGAIKKAFEVWSKASPLTFT-RISQGQADINIAFFQrdhgDNSPFDGPNGILAHAFQPGQGIG 191
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKnANDVDPADIRYSVIR----WIPYNDGTWSYGPSQVDPLTGEI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 192 GDAHFDAEETWTKTSTNYnLFLVAAHEFGHSLGLAHSS----------------DPGALMYP-----NYAFRETSNYSLP 250
Cdd:cd04268   76 LLARVYLYSSFVEYSGAR-LRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYapsnfSIQLGDGQKYTIG 154

                        170
                 ....*....|.
gi 966988098 251 QDDINGIQAIY 261
Cdd:cd04268  155 PYDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-86 3.49e-10

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: 55.60  E-value: 3.49e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098   28 ENTKIVQDYLEKFYQLPSNQyqsTRKNGTSMiVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-420 4.77e-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: 54.56  E-value: 4.77e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 966988098   377 IDAAVFYR-SKTYFFVNDQFWRYDNQRqfMEPGYPKSISGTFPGI 420
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 2.86e-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: 52.57  E-value: 2.86e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 966988098  377 IDAAVFYRS-KTYFFVNDQFWRYDNQRqfMEPGYPKSISgTFPGIEN 422
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-372 4.61e-08

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: 49.10  E-value: 4.61e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 966988098  329 IQAAYEDfDRDLIFLFKGNQYWAVSGYDIQQGYPRDISNY-GFPS 372
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-372 5.78e-07

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: 46.08  E-value: 5.78e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 966988098   329 IQAAYEDfDRDLIFLFKGNQYWAVSGYDIQQGYPRDISNY--GFPS 372
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 125-227 2.23e-06

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: 48.15  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 125 SETDVEGAIKKAFEVWSKASPLTFTRISQGQADINIAfFQRDHGDNSpFDGPNGILAHAFQPGQGIGGDAHFDAEETWTK 204
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRIS-FTPGDGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDPEFSR 94

                         90       100
                 ....*....|....*....|...
gi 966988098 205 TstnynlflvAAHEFGHSLGLAH 227
Cdd:cd04327   95 V---------VLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-271 3.60e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.14  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098 132 AIKKAFEVWSKAspLTFTRISQG-QADINIafFQRDHGDNSPFDGPNGI-LAHA-FQPGQGIGGDAHfdaeeTWT-KTST 207
Cdd:COG5549  105 AVLQAIAEWNAY--LPLEVVENPeNADIII--VRSNPPLTASPNPETGArSAETtYEFYDTGNILSH-----RFTiLLSP 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966988098 208 NY-NLFLVAA--HEFGHSLGL-AHSSDPGALMYpnyaFRETSN-YSLPQDDINGIQAIYGpssnpiQPT 271
Cdd:COG5549  176 NQtGKYLLATarHELGHALGIwGHSPSPTDAMY----FSQVRNpPPISPRDINTLKRIYQ------QPT 234
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 6.52e-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: 43.00  E-value: 6.52e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 966988098   285 FDAITTLR-GEILFFKDEYFWRRHPH-LQSVEMNFISLFWPSLP 326
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
151-267 1.05e-04

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 43.18  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098  151 ISQGQADINIAFfqrdhgdnSPFDGPNGILAHAFQP-GQGIGGDAHFDAEETWTKTSTnYNLFLVAAHEFGHSLGLAHss 229
Cdd:pfam13688  85 RGTQNDDLAYLF--------LMTNCSGGGLAWLGQLcNSGSAGSVSTRVSGNNVVVST-ATEWQVFAHEIGHNFGAVH-- 153

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 966988098  230 DPGALMYPNYAFreTSNYSLPqddiNGIQAIYGPSSNP 267
Cdd:pfam13688 154 DCDSSTSSQCCP--PSNSTCP----AGGRYIMNPSSSP 185
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
208-237 2.05e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.17  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 966988098 208 NYNLFL-----VAAHEFGHSLGLAHSSDPGALMYP 237
Cdd:COG1913  115 DEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 2.71e-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: 2.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 966988098  285 FDAITTLR-GEILFFKDEYFWRRHP-HLQSVEMNFISLFwPSLP 326
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPqRVEPGYPKLISDF-PGLP 43
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 136-228 7.55e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 36.58  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988098  136 AFEVWSKASPLTFTRISQGQADINIAFFQRDHGDNSpfdgpnGI--LAHAFQPGQGIGGdahfdaeeTWTKTSTNYNLFL 213
Cdd:pfam13582  42 ALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG------GIayVGGVCNSGSKFGV--------NSGSGPVGDTGAD 107

                          90
                  ....*....|....*
gi 966988098  214 VAAHEFGHSLGLAHS 228
Cdd:pfam13582 108 TFAHEIGHNFGLNHT 122
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 208-253 8.98e-03

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 37.28  E-value: 8.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 966988098 208 NYNLFL-----VAAHEFGHSLGLAHSSDPGALMYPnyafretSNySLPQDD 253
Cdd:cd11375  115 DEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF-------SN-SLEETD 157
 
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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