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Conserved domains on  [gi|60207645|gb|AAX14806|]
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collagenase [Notophthalmus viridescens]

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 ...
108-262 2.63e-95

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: 284.51  E-value: 2.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645   108 WKHTEITYRILNYTPDMAKADVDAAIQRALNVWADVTPLTFTRLYEGTADIQISFAAGDHRDNSPFDGPDGLLAHAFEPG 187
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60207645   188 RGIGGDAHFDEDERWTKGSER---YNLFLMAAHEFGHSLGLSHSNDPGALMYPTYSSTDPDEFRLPQDDINGIQSLYG 262
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
276-466 5.46e-85

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: 259.17  E-value: 5.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 276 PSICDTKViFDAVATLRGEMLFLKERFFWRRHAQYPEAELHFIKSFWPSLPSDIEAAYENPEQDEVLIFKGSKYWALNGY 355
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 356 DIVQGYPKNIHTLGFPTTVKKIDAAVYNEETGKTFFFVGNQYWSYDESTRTMDQGFPKETINDFPGIGQKVHAVFQSN-G 434
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 60207645 435 FLYFFSGKYQFEFSMKSKRVM--RVLRNNS-WLGC 466
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRvgYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
27-86 3.89e-09

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: 52.52  E-value: 3.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    27 EESDIQRAEAYLKRFYGLDTEkkhFTRKNGSPFSEKLREMQEFFGLEVTGRLDSETLEVM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP---VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
108-262 2.63e-95

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: 284.51  E-value: 2.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645   108 WKHTEITYRILNYTPDMAKADVDAAIQRALNVWADVTPLTFTRLYEGTADIQISFAAGDHRDNSPFDGPDGLLAHAFEPG 187
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60207645   188 RGIGGDAHFDEDERWTKGSER---YNLFLMAAHEFGHSLGLSHSNDPGALMYPTYSSTDPDEFRLPQDDINGIQSLYG 262
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
276-466 5.46e-85

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: 259.17  E-value: 5.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 276 PSICDTKViFDAVATLRGEMLFLKERFFWRRHAQYPEAELHFIKSFWPSLPSDIEAAYENPEQDEVLIFKGSKYWALNGY 355
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 356 DIVQGYPKNIHTLGFPTTVKKIDAAVYNEETGKTFFFVGNQYWSYDESTRTMDQGFPKETINDFPGIGQKVHAVFQSN-G 434
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 60207645 435 FLYFFSGKYQFEFSMKSKRVM--RVLRNNS-WLGC 466
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRvgYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
108-262 1.34e-81

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: 249.04  E-value: 1.34e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 108 WKHTEITYRILNYTPDMAKADVDAAIQRALNVWADVTPLTFTRL-YEGTADIQISFAAGDHRDNSPFDGPDGLLAHAFEP 186
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60207645 187 GrGIGGDAHFDEDERWTKGSER--YNLFLMAAHEFGHSLGLSHSNDPGALMYPTYSSTDPDeFRLPQDDINGIQSLYG 262
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSDSggTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
104-262 3.36e-32

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: 119.76  E-value: 3.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    104 GNPVWKHTEITYRIlnYTPDMAKaDVDAAIQRALNVWADVTPLTFTRLYeGTADIQISFAAGDHrdnspfdGPdgLLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDS-------GC--TLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    184 FEPGrgigGDAHFDeDERWTKGSErynlflMAAHEFGHSLGLSHSNDPGA---LMYPTYSSTDPDEFRLPQDDINGIQSL 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 60207645    261 YG 262
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
377-423 2.00e-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: 53.02  E-value: 2.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 60207645    377 IDAAVYNEEtGKTFFFVGNQYWSYDEstRTMDQGFPKETINDFPGIG 423
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
27-86 3.89e-09

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: 52.52  E-value: 3.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    27 EESDIQRAEAYLKRFYGLDTEkkhFTRKNGSPFSEKLREMQEFFGLEVTGRLDSETLEVM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP---VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
377-423 2.50e-07

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: 47.18  E-value: 2.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 60207645   377 IDAAVYNEEtGKTFFFVGNQYWSYDEstRTMDQGFPKEtINDFPGIG 423
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKL-ISDFPGLP 43
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
213-271 7.70e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.99  E-value: 7.70e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60207645 213 LMAA-HEFGHSLGL-SHSNDPGALMYPTYSSTDPdefRLPQDDINGIQSLYGesknpvQPT 271
Cdd:COG5549 183 LATArHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIYQ------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 ...
108-262 2.63e-95

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: 284.51  E-value: 2.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645   108 WKHTEITYRILNYTPDMAKADVDAAIQRALNVWADVTPLTFTRLYEGTADIQISFAAGDHRDNSPFDGPDGLLAHAFEPG 187
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60207645   188 RGIGGDAHFDEDERWTKGSER---YNLFLMAAHEFGHSLGLSHSNDPGALMYPTYSSTDPDEFRLPQDDINGIQSLYG 262
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
276-466 5.46e-85

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: 259.17  E-value: 5.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 276 PSICDTKViFDAVATLRGEMLFLKERFFWRRHAQYPEAELHFIKSFWPSLPSDIEAAYENPEQDEVLIFKGSKYWALNGY 355
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 356 DIVQGYPKNIHTLGFPTTVKKIDAAVYNEETGKTFFFVGNQYWSYDESTRTMDQGFPKETINDFPGIGQKVHAVFQSN-G 434
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 60207645 435 FLYFFSGKYQFEFSMKSKRVM--RVLRNNS-WLGC 466
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRvgYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
108-262 1.34e-81

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: 249.04  E-value: 1.34e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 108 WKHTEITYRILNYTPDMAKADVDAAIQRALNVWADVTPLTFTRL-YEGTADIQISFAAGDHRDNSPFDGPDGLLAHAFEP 186
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60207645 187 GrGIGGDAHFDEDERWTKGSER--YNLFLMAAHEFGHSLGLSHSNDPGALMYPTYSSTDPDeFRLPQDDINGIQSLYG 262
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSDSggTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
104-262 3.36e-32

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: 119.76  E-value: 3.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    104 GNPVWKHTEITYRIlnYTPDMAKaDVDAAIQRALNVWADVTPLTFTRLYeGTADIQISFAAGDHrdnspfdGPdgLLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDS-------GC--TLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    184 FEPGrgigGDAHFDeDERWTKGSErynlflMAAHEFGHSLGLSHSNDPGA---LMYPTYSSTDPDEFRLPQDDINGIQSL 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 60207645    261 YG 262
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
132-262 1.64e-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: 79.42  E-value: 1.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 132 AIQRALNVWADVTPLTFtrLYEGT----ADIQISFaagdhRDNSPFDGPDGLLAHAFEPGRGIGGDA---HFDEDERWTK 204
Cdd:cd04279  25 AVKQAAAEWENVGPLKF--VYNPEedndADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlfnRTDINLGPGQ 97
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 60207645 205 GSERYNLFLMAAHEFGHSLGLSHSND-PGALMYPTYSSTDPDEFRLPQDDINGIQSLYG 262
Cdd:cd04279  98 PRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
112-261 1.70e-13

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: 68.32  E-value: 1.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 112 EITYRILNYTPDM----AKADVDAAIQRALNVWADVTPLTFT--RLYEGTADIQISFAAGDhrdnspFDGPDGllAHAFE 185
Cdd:cd00203   2 VIPYVVVADDRDVeeenLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILVTRQD------FDGGTG--GWAYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 186 PG--RGIGGDAHFDEDERWTKgseryNLFLMAAHEFGHSLGLSHSND--------------------PGALMYPTYSS-T 242
Cdd:cd00203  74 GRvcDSLRGVGVLQDNQSGTK-----EGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTKGSfS 148
                       170
                ....*....|....*....
gi 60207645 243 DPDEFRLPQDDINGIQSLY 261
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
131-262 2.02e-13

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: 68.60  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 131 AAIQRALNVWADVTPLTFTRLYEGT-ADIQISFaagdhrdnspFDGPD-GLLAHAFEPGRGI----GGDAHFDEDERW-- 202
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPDgNTAGYAYYPGSGSgtayGGDIWFNSSYDTns 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 203 -TKGSERYNLFLmaaHEFGHSLGLSHSNDPGA----------------LM-YPTYSSTDPDE-FRLPQ----DDINGIQS 259
Cdd:cd04277 107 dSPGSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsYNSGYGNGASAgGGYPQtpmlLDIAALQY 183

                ...
gi 60207645 260 LYG 262
Cdd:cd04277 184 LYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
112-261 9.74e-12

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 63.28  E-value: 9.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 112 EITYRILNYTPDmakaDVDAAIQRALNVWADVTPLTFTRLYEG-TADIQISFaagdHRDNSPFDGPDGLLAHAFEPGRG- 189
Cdd:cd04268   3 PITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSV----IRWIPYNDGTWSYGPSQVDPLTGe 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 190 -IGGDAHFDEDERWTKGSERYNLflmAAHEFGHSLGLSHSN----------------DPGALMYPTYSS-----TDPDEF 247
Cdd:cd04268  75 iLLARVYLYSSFVEYSGARLRNT---AEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNfsiqlGDGQKY 151
                       170
                ....*....|....
gi 60207645 248 RLPQDDINGIQSLY 261
Cdd:cd04268 152 TIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
377-423 2.00e-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: 53.02  E-value: 2.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 60207645    377 IDAAVYNEEtGKTFFFVGNQYWSYDEstRTMDQGFPKETINDFPGIG 423
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
27-86 3.89e-09

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: 52.52  E-value: 3.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645    27 EESDIQRAEAYLKRFYGLDTEkkhFTRKNGSPFSEKLREMQEFFGLEVTGRLDSETLEVM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP---VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
377-423 2.50e-07

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: 47.18  E-value: 2.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 60207645   377 IDAAVYNEEtGKTFFFVGNQYWSYDEstRTMDQGFPKEtINDFPGIG 423
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKL-ISDFPGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
329-371 2.43e-06

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: 44.09  E-value: 2.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 60207645   329 IEAAYENPeQDEVLIFKGSKYWALNGYDIVQGYPKNIHTL-GFP 371
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
213-271 7.70e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.99  E-value: 7.70e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60207645 213 LMAA-HEFGHSLGL-SHSNDPGALMYPTYSSTDPdefRLPQDDINGIQSLYGesknpvQPT 271
Cdd:COG5549 183 LATArHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIYQ------QPT 234
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
329-371 8.54e-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: 42.61  E-value: 8.54e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 60207645    329 IEAAYENPEqDEVLIFKGSKYWALNGYDIVQGYPKNIHTL--GFP 371
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
127-227 7.13e-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: 43.91  E-value: 7.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60207645 127 ADVDAAIQRALNVWADVTPLTFTRLYEGTADIQISFAAGDhrDNSPFDGPDGLLAHAFEPGRGIGGDAHFDEDerwtkgS 206
Cdd:cd04327  19 AFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWFTDDTPD------P 90
                        90       100
                ....*....|....*....|.
gi 60207645 207 ERYNLFLmaaHEFGHSLGLSH 227
Cdd:cd04327  91 EFSRVVL---HEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
215-238 9.30e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 9.30e-04
                        10        20
                ....*....|....*....|....
gi 60207645 215 AAHEFGHSLGLSHSNDPGALMYPT 238
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMHFS 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
285-327 3.06e-03

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 35.68  E-value: 3.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 60207645    285 FDAVATLR-GEMLFLKERFFWRRHAQYPEA-ELHFIKSFWPSLPS 327
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
285-327 7.15e-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: 34.46  E-value: 7.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 60207645   285 FDAVATLR-GEMLFLKERFFWRRHAQYPEAELHFIKSFWPSLPS 327
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLPC 44
 
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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