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Conserved domains on  [gi|4505213|ref|NP_002420|]
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matrix metalloproteinase-19 isoform 1 preproprotein [Homo sapiens]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-256 2.49e-73

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: 229.01  E-value: 2.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPGRVLAHAD 181
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPGGTLAHAF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505213  182 IP--ELGSVHFDEDEFWTEGT-YRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRPHFKLHPDDVAGIQALYG 256
Cdd:cd04278  80 FPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-472 6.21e-67

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: 214.10  E-value: 6.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  286 PDPCSS-ELDAMMLGpRGKTYAFKGDYVWTVSD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHFFKGDKVWRYINF 363
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  364 KMSPGFPKKLN-----RVEPNLDAALYWPLNQKVFLFKGSGYWQWDELARTDFSSYPKPIKGLFTGVPNQPSAAMSWQDG 438
Cdd:cd00094  80 NLEPGYPKPISdlgfpPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505213  439 RVYFFKGKVYWRLNQQLR-VEKGYPRNISHNWMHC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKeVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 9.75e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.89  E-value: 9.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4505213     31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-256 2.49e-73

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: 229.01  E-value: 2.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPGRVLAHAD 181
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPGGTLAHAF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505213  182 IP--ELGSVHFDEDEFWTEGT-YRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRPHFKLHPDDVAGIQALYG 256
Cdd:cd04278  80 FPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-256 2.91e-68

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: 215.94  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213    103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFhGRQSSYCSNTFDGPGRVLAHADI 182
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGF-GRGDHGDGYPFDGPGGVLAHAFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213    183 PEL---GSVHFDEDEFWTEGT--YRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRP-HFKLHPDDVAGIQALYG 256
Cdd:pfam00413  80 PGPglgGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-472 6.21e-67

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: 214.10  E-value: 6.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  286 PDPCSS-ELDAMMLGpRGKTYAFKGDYVWTVSD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHFFKGDKVWRYINF 363
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  364 KMSPGFPKKLN-----RVEPNLDAALYWPLNQKVFLFKGSGYWQWDELARTDFSSYPKPIKGLFTGVPNQPSAAMSWQDG 438
Cdd:cd00094  80 NLEPGYPKPISdlgfpPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505213  439 RVYFFKGKVYWRLNQQLR-VEKGYPRNISHNWMHC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKeVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 103-257 3.14e-30

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: 114.76  E-value: 3.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213     103 RWRKKHLTFRILnlPSTLPPHtARAALRQAFQDWSNVAPLTFQEVQAGAaDIRLSFhGRQSSYCSntfdgpgrvLAHADI 182
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSPE-EREAIAKALAEWSDVTCIRFVERTGTA-DIYISF-GSGDSGCT---------LSHAGR 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505213     183 PElGSVHFDeDEFWTEGTYrgvnlriIAAHEVGHALGLGHSRYSQA---LMAPVYEGYRPH-FKLHPDDVAGIQALYGK 257
Cdd:smart00235  70 PG-GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRnFDLSEDDSLGIPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 431-469 4.99e-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: 54.94  E-value: 4.99e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4505213     431 AAMSWQDGRVYFFKGKVYWRLNQQlRVEKGYPRNISHNW 469
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPK-RVDPGYPKLISSFF 40
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 431-472 4.50e-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: 4.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 4505213    431 AAMSWQDGRVYFFKGKVYWRLNQQlRVEKGYPRNISH-NWMHC 472
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQ-RVEPGYPKLISDfPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 9.75e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.89  E-value: 9.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4505213     31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-256 2.49e-73

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: 229.01  E-value: 2.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPGRVLAHAD 181
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPGGTLAHAF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505213  182 IP--ELGSVHFDEDEFWTEGT-YRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRPHFKLHPDDVAGIQALYG 256
Cdd:cd04278  80 FPggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-256 2.91e-68

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: 215.94  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213    103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFhGRQSSYCSNTFDGPGRVLAHADI 182
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGF-GRGDHGDGYPFDGPGGVLAHAFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213    183 PEL---GSVHFDEDEFWTEGT--YRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRP-HFKLHPDDVAGIQALYG 256
Cdd:pfam00413  80 PGPglgGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-472 6.21e-67

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: 214.10  E-value: 6.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  286 PDPCSS-ELDAMMLGpRGKTYAFKGDYVWTVSD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHFFKGDKVWRYINF 363
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  364 KMSPGFPKKLN-----RVEPNLDAALYWPLNQKVFLFKGSGYWQWDELARTDFSSYPKPIKGLFTGVPNQPSAAMSWQDG 438
Cdd:cd00094  80 NLEPGYPKPISdlgfpPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505213  439 RVYFFKGKVYWRLNQQLR-VEKGYPRNISHNWMHC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKeVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 103-257 3.14e-30

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: 114.76  E-value: 3.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213     103 RWRKKHLTFRILnlPSTLPPHtARAALRQAFQDWSNVAPLTFQEVQAGAaDIRLSFhGRQSSYCSntfdgpgrvLAHADI 182
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSPE-EREAIAKALAEWSDVTCIRFVERTGTA-DIYISF-GSGDSGCT---------LSHAGR 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505213     183 PElGSVHFDeDEFWTEGTYrgvnlriIAAHEVGHALGLGHSRYSQA---LMAPVYEGYRPH-FKLHPDDVAGIQALYGK 257
Cdd:smart00235  70 PG-GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRnFDLSEDDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 121-256 6.92e-15

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: 72.10  E-value: 6.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  121 PPHTARAALRQAFQDWSNVAPLTFQEVQAG--AADIRLSF-----HGRQSSYCSNTFDGPGRVLAHADIPELgsvhfdeD 193
Cdd:cd04279  18 RAQSWLQAVKQAAAEWENVGPLKFVYNPEEdnDADIVIFFdrpppVGGAGGGLARAGFPLISDGNRKLFNRT-------D 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505213  194 EFWTEGTYRGV-NLRIIAAHEVGHALGL-GHSRYSQALMAPVYeGYRPHFK--LHPDDVAGIQALYG 256
Cdd:cd04279  91 INLGPGQPRGAeNLQAIALHELGHALGLwHHSDRPEDAMYPSQ-GQGPDGNptLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 121-255 3.52e-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: 61.77  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  121 PPHTARAALRQAFQDWSNVAPLTFQEVQAG--AADIRLSFhgrqssyCSNTFDGPGRVLAH-ADI--PELGSVHFDEDEF 195
Cdd:cd00203  19 LSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILV-------TRQDFDGGTGGWAYlGRVcdSLRGVGVLQDNQS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  196 WTEgtyrgvNLRIIAAHEVGHALGLGH-----SRYSQA---------------LMAPVYEGYRPHFKLHP--DDVAGIQA 253
Cdd:cd00203  92 GTK------EGAQTIAHELGHALGFYHdhdrkDRDDYPtiddtlnaedddyysVMSYTKGSFSDGQRKDFsqCDIDQINK 165


                ..
gi 4505213  254 LY 255
Cdd:cd00203 166 LY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 106-255 4.63e-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: 61.36  E-value: 4.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  106 KKHLTFRIlnlpSTLPPHTARAALRQAFQDWSNVAPLTFQEV-QAGAADIRLSFHGRQSSYcsntfDGPGRVLAHADIPE 184
Cdd:cd04268   1 KKPITYYI----DDSVPDKLRAAILDAIEAWNKAFAIGFKNAnDVDPADIRYSVIRWIPYN-----DGTWSYGPSQVDPL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  185 LGSVHFDEDEFWTEGT-YRGVNLRIIAAHEVGHALGLGHSR----------------------YSQALMAPVYEGYRPHF 241
Cdd:cd04268  72 TGEILLARVYLYSSFVeYSGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgdtssvmDYAPSNFSIQLGDGQKY 151

                       170
                ....*....|....
gi 4505213  242 KLHPDDVAGIQALY 255
Cdd:cd04268 152 TIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 117-256 9.22e-11

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: 60.89  E-value: 9.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  117 PSTLPPHTARAAlRQAFQDWSNVAPLTFQEVQAG-AADIRLSFhgrqssycSNTFDGPGRVLAH-----ADIPELGSVHF 190
Cdd:cd04277  28 TAALSAAQQAAA-RDALEAWEDVADIDFVEVSDNsGADIRFGN--------SSDPDGNTAGYAYypgsgSGTAYGGDIWF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  191 DEDEFW---TEGTYRgvnlRIIAAHEVGHALGLGHS-------------------------------------RYSQALM 230
Cdd:cd04277  99 NSSYDTnsdSPGSYG----YQTIIHEIGHALGLEHPgdynggdpvpptyaldsreytvmsynsgygngasaggGYPQTPM 174

                       170       180
                ....*....|....*....|....*.
gi 4505213  231 ApvyegyrphfklhpDDVAGIQALYG 256
Cdd:cd04277 175 L--------------LDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 431-469 4.99e-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: 54.94  E-value: 4.99e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4505213     431 AAMSWQDGRVYFFKGKVYWRLNQQlRVEKGYPRNISHNW 469
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPK-RVDPGYPKLISSFF 40
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 337-380 2.71e-09

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: 52.63  E-value: 2.71e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505213     337 LDAAVYSPRTQwIHFFKGDKVWRYINFKMSPGFPKKLNRVEPNL 380
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDPKRVDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 431-472 4.50e-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: 4.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 4505213    431 AAMSWQDGRVYFFKGKVYWRLNQQlRVEKGYPRNISH-NWMHC 472
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQ-RVEPGYPKLISDfPGLPC 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 121-222 8.78e-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: 46.60  E-value: 8.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505213  121 PPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSF--HGRQSSYCsntfdGPGRVLAHADIPelgSVHFDedefWTE 198
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFtpGDGYWSYV-----GTDALLIGADAP---TMNLG----WFT 84

                        90       100
                ....*....|....*....|....
gi 4505213  199 GTYRGVNLRIIAAHEVGHALGLGH 222
Cdd:cd04327  85 DDTPDPEFSRVVLHEFGHALGFIH 108
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 9.75e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.89  E-value: 9.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4505213     31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-335 1.25e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 42.23  E-value: 1.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 4505213     293 LDAMMLGPRGKTYAFKGDYVWTVSDS--GPGPLFRVSALWEGLPG 335
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKrvDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 337-371 1.34e-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: 39.47  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 4505213    337 LDAAVYSPRTQwIHFFKGDKVWRYINFKMSPGFPK 371
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDPQRVEPGYPK 34
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 380-426 1.58e-04

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: 39.15  E-value: 1.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505213     380 LDAALYWPlNQKVFLFKGSGYWQWDElaRTDFSSYPKPIKGLFTGVP 426
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 206-222 8.47e-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: 38.39  E-value: 8.47e-03
                          10
                  ....*....|....*..
gi 4505213    206 LRIIAAHEVGHALGLGH 222
Cdd:pfam16313  13 LRFVSAHEVGHTLGLRH 29
 
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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