NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767970183|ref|XP_011541138|]
View 

neutrophil collagenase isoform X3 [Homo sapiens]

Protein Classification

PG_binding_1 and Peptidase_M10 domain-containing protein (domain architecture ID 12021168)

protein containing domains PG_binding_1, Peptidase_M10, and HX

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
116-271 8.10e-93

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


:

Pssm-ID: 334067  Cd Length: 159  Bit Score: 274.49  E-value: 8.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183  116 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183  196 GQGIGGDAHFDAEETWTNTSAN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSSApngINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDPKKFRLSQDDIKGIQQLYG 159
HX super family cl02471
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
285-355 1.79e-27

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: 351767 [Multi-domain]  Cd Length: 194  Bit Score: 107.01  E-value: 1.79e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970183 285 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKD 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
45-95 5.84e-07

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: 334552 [Multi-domain]  Cd Length: 57  Bit Score: 45.96  E-value: 5.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767970183   45 YLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 95
Cdd:pfam01471  11 YLNRLGYYSGPI---DGVFGPST-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 ...
116-271 8.10e-93

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 334067  Cd Length: 159  Bit Score: 274.49  E-value: 8.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183  116 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183  196 GQGIGGDAHFDAEETWTNTSAN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSSApngINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDPKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
116-271 4.03e-82

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: 247.12  E-value: 4.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 116 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRI-SQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQ 194
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183 195 PGqGIGGDAHFDAEETWT--NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDIDGIQAIYG 271
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
113-271 1.02e-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: 121.69  E-value: 1.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183   113 GNPKWERTNLTYRIrnYTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGeADINIAFYQRDHGdnsPFdgpngiLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183   193 FQPGqgigGDAHFDaEETWTNTSAnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDIDGIQAI 269
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 767970183   270 YG 271
Cdd:smart00235 137 YG 138
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
285-355 1.79e-27

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: 107.01  E-value: 1.79e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970183 285 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKD 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
294-335 6.62e-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: 333794  Cd Length: 44  Bit Score: 48.34  E-value: 6.62e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767970183  294 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFWPSLP 335
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQkVEPGYPKLISDFWPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
294-335 2.27e-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: 46.85  E-value: 2.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767970183   294 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFWPSLP 335
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
45-95 5.84e-07

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: 334552 [Multi-domain]  Cd Length: 57  Bit Score: 45.96  E-value: 5.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767970183   45 YLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 95
Cdd:pfam01471  11 YLNRLGYYSGPI---DGVFGPST-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 ...
116-271 8.10e-93

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 334067  Cd Length: 159  Bit Score: 274.49  E-value: 8.10e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183  116 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183  196 GQGIGGDAHFDAEETWTNTSAN---YNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSSApngINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDPKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
116-271 4.03e-82

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: 247.12  E-value: 4.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 116 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRI-SQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQ 194
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183 195 PGqGIGGDAHFDAEETWT--NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDIDGIQAIYG 271
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
113-271 1.02e-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: 121.69  E-value: 1.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183   113 GNPKWERTNLTYRIrnYTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGeADINIAFYQRDHGdnsPFdgpngiLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183   193 FQPGqgigGDAHFDaEETWTNTSAnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDIDGIQAI 269
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 767970183   270 YG 271
Cdd:smart00235 137 YG 138
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
285-355 1.79e-27

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: 107.01  E-value: 1.79e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970183 285 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKD 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
141-271 3.25e-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  Cd Length: 156  Bit Score: 77.88  E-value: 3.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 141 AIKDAFELWSVASPLIFTRISQGEADINIAFYQRDhgdNSPFDGPNGILAHAFQPGQGIGGDA---HFDAEETWTNTSAN 217
Cdd:cd04279   25 AVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDR---PPPVGGAGGGLARAGFPLISDGNRKlfnRTDINLGPGQPRGA 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767970183 218 YNLFLVAAHEFGHSLGLAHSSD-PGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 271
Cdd:cd04279  102 ENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
129-271 6.13e-16

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  Cd Length: 186  Bit Score: 75.14  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 129 YTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGE-ADINIAFYQRDHGDNspfdgpngiLAHAFQPG----QGIGGDA 203
Cdd:cd04277   27 NTAALSAAQQA-AARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNT---------AGYAYYPGsgsgTAYGGDI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 204 HFDAEETWTNTSA-NYNlFLVAAHEFGHSLGLAHSSDPGAL-MYPNYAFRETSNYSL-----------------PQ---- 260
Cdd:cd04277   97 WFNSSYDTNSDSPgSYG-YQTIIHEIGHALGLEHPGDYNGGdPVPPTYALDSREYTVmsynsgygngasagggyPQtpml 175
                        170
                 ....*....|.
gi 767970183 261 DDIDGIQAIYG 271
Cdd:cd04277  176 LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
127-270 5.06e-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: 60.61  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 127 RNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGE--ADINIAFYQRDHgdnspfdgPNGILAHAFQPG--QGIGGD 202
Cdd:cd00203   12 RDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 203 AHFDaeetwTNTSANYNLFLVAAHEFGHSLGLAHSSD--------------------PGALMYP-NYAFRETSNYSLPQD 261
Cdd:cd00203   84 GVLQ-----DNQSGTKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYtKGSFSDGQRKDFSQC 158

                 ....*....
gi 767970183 262 DIDGIQAIY 270
Cdd:cd00203  159 DIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
122-270 1.13e-09

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: 56.74  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 122 LTYRIRNYTPQlseaEVERAIKDAFELWSVASPLIFT-RISQGEADINIAFYQrdhgDNSPFDGPNGILAHAFQPGQGIG 200
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKnANDVDPADIRYSVIR----WIPYNDGTWSYGPSQVDPLTGEI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 201 GDAHFDAEETWTNTSANYnLFLVAAHEFGHSLGLAHSS----------------DPGALMYP-----NYAFRETSNYSLP 259
Cdd:cd04268   76 LLARVYLYSSFVEYSGAR-LRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYapsnfSIQLGDGQKYTIG 154
                        170
                 ....*....|.
gi 767970183 260 QDDIDGIQAIY 270
Cdd:cd04268  155 PYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
294-335 6.62e-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: 333794  Cd Length: 44  Bit Score: 48.34  E-value: 6.62e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767970183  294 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFWPSLP 335
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQkVEPGYPKLISDFWPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
294-335 2.27e-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: 46.85  E-value: 2.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767970183   294 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFWPSLP 335
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
45-95 5.84e-07

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: 334552 [Multi-domain]  Cd Length: 57  Bit Score: 45.96  E-value: 5.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767970183   45 YLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 95
Cdd:pfam01471  11 YLNRLGYYSGPI---DGVFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
134-236 4.70e-05

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: 43.52  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183 134 SEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYqRDHGDNSpFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN 213
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFT-PGDGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDPEFSR 94
                         90       100
                 ....*....|....*....|...
gi 767970183 214 TsanynlflvAAHEFGHSLGLAH 236
Cdd:cd04327   95 V---------VLHEFGHALGFIH 108
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
118-239 5.16e-04

Metallo-peptidase family M12;


Pssm-ID: 338898  Cd Length: 188  Bit Score: 40.44  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970183  118 ERT-NLTYRIRN---------YTPQLSEAEVERAIKDAFELWSvasplifTRISQGEADINIAFyqrdhgdnSPFDGPNG 187
Cdd:pfam13688  40 ERNfNISLGLVNltitdytdpYTSPPTSSGNASDRLNRFQSFS-------AWRGTQNDDLAHLF--------LDTNCSGG 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767970183  188 ILAHAFQP-GQGIGGDAHFDAeetwTNTSANYNLFLVAAHEFGHSLGLAHSSD 239
Cdd:pfam13688 105 GLAWLGQLcNSGSAGSVSTSV----NVVVGTATEWQVFAHEIGHNFGAVHDCD 153
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
163-236 9.64e-04

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 40.02  E-value: 9.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767970183 163 GEADINIAFYQrdhgdnspfDGPNGILAHAFQPGQGIGGDAHFD-----AEETWTNTSANYNLFLVAAHEFGHSLGLAH 236
Cdd:cd04275   84 GYKYLNIYVAN---------FLGGGLLGYATFPDSLVSLAFITDgvvinPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
216-262 4.33e-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: 37.66  E-value: 4.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767970183 216 ANYNLFL-----VAAHEFGHSLGLAHSSDPGALMYPnyafretSNySLPQDD 262
Cdd:cd11375  114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF-------SN-SLEETD 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH