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Conserved domains on  [gi|688575181|ref|XP_009303831|]
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matrix metalloproteinase 13a isoform X1 [Danio rerio]

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 ...
 112-268 1.45e-93

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: 280.27  E-value: 1.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181  112 KWKKHQLTYRIENYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSGTADIMIFFATGDHGDGYPFDGPNGFLAHAYPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688575181  192 YEGVGGDAHFDDDE--TFSYRSPQYYTLFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDRFILPRDDVNGIQSLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDEtwTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-475 8.75e-63

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: 202.16  E-value: 8.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 286 PNTCDPnLVLDAVTMLRGEIMFFKNSFFWRSYPQSPDVELQLIQSFWPEIPDNIDAAFESVIQDKVFLIKGEKVWALYGY 365
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 366 DIVQGYPKSLSMFRLRKNVKKIDAVLYKEDSNTILFFANNQVYSYNERMKKMDKGFPKPVQKVFPGMTGKVTAAFQYR-G 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 688575181 445 FNYLFSGSKMLEFGSNNKLLRV----LNNNYFLPC 475
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVgyplKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-91 1.55e-05

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: 42.50  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688575181   28 GDQDTLAENYLTRLYGLPkqpaQSPSSSGGEKrssdMSLRLKEMQQFFKLKVTGKLDQETLEVM 91
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYP----GPVDGYFGPS----TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-268 1.45e-93

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: 280.27  E-value: 1.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181  112 KWKKHQLTYRIENYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSGTADIMIFFATGDHGDGYPFDGPNGFLAHAYPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688575181  192 YEGVGGDAHFDDDE--TFSYRSPQYYTLFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDRFILPRDDVNGIQSLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDEtwTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-268 8.21e-83

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: 252.51  E-value: 8.21e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 112 KWKKHQLTYRIENYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSG-TADIMIFFATGDHGDGYPFDGPNGFLAHAYP 190
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688575181 191 PyEGVGGDAHFDDDETFSYRSPQYYT-LFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDrFILPRDDVNGIQSLYG 268
Cdd:cd04278   81 P-GGIGGDIHFDDDEQWTLGSDSGGTdLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-475 8.75e-63

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: 202.16  E-value: 8.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 286 PNTCDPnLVLDAVTMLRGEIMFFKNSFFWRSYPQSPDVELQLIQSFWPEIPDNIDAAFESVIQDKVFLIKGEKVWALYGY 365
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 366 DIVQGYPKSLSMFRLRKNVKKIDAVLYKEDSNTILFFANNQVYSYNERMKKMDKGFPKPVQKVFPGMTGKVTAAFQYR-G 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 688575181 445 FNYLFSGSKMLEFGSNNKLLRV----LNNNYFLPC 475
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVgyplKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 109-269 1.61e-36

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: 131.32  E-value: 1.61e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181   109 GDYKWKKHQLTYRIENYTLDmsvAEVDDSISRALKVWADVTPLRFTRIySGTADIMIFFATGDHGdgypfdgpnGFLAHA 188
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181   189 YPPyegvGGDAHFDDdETFSYRspqyytlFSVAAHEFGHSLGLGHSRDPGA---LMYPTYVYRDMDRFILPRDDVNGIQS 265
Cdd:smart00235  68 GRP----GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 688575181   266 LYGP 269
Cdd:smart00235 136 DYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-432 8.84e-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: 8.84e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 688575181   387 IDAVLYKEDsNTILFFANNQVYSYNErmKKMDKGFPKPVQKVFPGM 432
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-91 1.55e-05

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: 42.50  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688575181   28 GDQDTLAENYLTRLYGLPkqpaQSPSSSGGEKrssdMSLRLKEMQQFFKLKVTGKLDQETLEVM 91
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYP----GPVDGYFGPS----TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 215-267 5.84e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 44.29  E-value: 5.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 688575181 215 YTLfSVAAHEFGHSLGL-GHSRDPGALMYPTYVyRDmDRFILPRdDVNGIQSLY 267
Cdd:COG5549  181 YLL-ATARHELGHALGIwGHSPSPTDAMYFSQV-RN-PPPISPR-DINTLKRIY 230
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-376 7.41e-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: 7.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 688575181  339 IDAAFESvIQDKVFLIKGEKVWALYGYDIVQGYPKSLS 376
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLIS 37
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-268 1.45e-93

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: 280.27  E-value: 1.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181  112 KWKKHQLTYRIENYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSGTADIMIFFATGDHGDGYPFDGPNGFLAHAYPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688575181  192 YEGVGGDAHFDDDE--TFSYRSPQYYTLFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDRFILPRDDVNGIQSLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDEtwTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-268 8.21e-83

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: 252.51  E-value: 8.21e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 112 KWKKHQLTYRIENYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSG-TADIMIFFATGDHGDGYPFDGPNGFLAHAYP 190
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688575181 191 PyEGVGGDAHFDDDETFSYRSPQYYT-LFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDrFILPRDDVNGIQSLYG 268
Cdd:cd04278   81 P-GGIGGDIHFDDDEQWTLGSDSGGTdLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-475 8.75e-63

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: 202.16  E-value: 8.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 286 PNTCDPnLVLDAVTMLRGEIMFFKNSFFWRSYPQSPDVELQLIQSFWPEIPDNIDAAFESVIQDKVFLIKGEKVWALYGY 365
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 366 DIVQGYPKSLSMFRLRKNVKKIDAVLYKEDSNTILFFANNQVYSYNERMKKMDKGFPKPVQKVFPGMTGKVTAAFQYR-G 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 688575181 445 FNYLFSGSKMLEFGSNNKLLRV----LNNNYFLPC 475
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVgyplKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 109-269 1.61e-36

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: 131.32  E-value: 1.61e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181   109 GDYKWKKHQLTYRIENYTLDmsvAEVDDSISRALKVWADVTPLRFTRIySGTADIMIFFATGDHGdgypfdgpnGFLAHA 188
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181   189 YPPyegvGGDAHFDDdETFSYRspqyytlFSVAAHEFGHSLGLGHSRDPGA---LMYPTYVYRDMDRFILPRDDVNGIQS 265
Cdd:smart00235  68 GRP----GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPY 135


                   ....
gi 688575181   266 LYGP 269
Cdd:smart00235 136 DYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 133-268 1.59e-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: 73.64  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 133 EVDDSISRALKVWADVTPLRFtrIYSGT----ADIMIFFATGDHGDGYPfdgpnGFLAHAYPPYEGVGGDAHFDD-DETF 207
Cdd:cd04279   21 SWLQAVKQAAAEWENVGPLKF--VYNPEedndADIVIFFDRPPPVGGAG-----GGLARAGFPLISDGNRKLFNRtDINL 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688575181 208 SYRSPQY-YTLFSVAAHEFGHSLGLGHSRD-PGALMYPTYVYRDMDRFILPRDDVNGIQSLYG 268
Cdd:cd04279   94 GPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 104-268 3.01e-15

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: 73.99  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 104 YSTFPGDYKWKKHQLTYRIENYTLDMSVAEVDDsISRALKVWADVTPLRFTRIYSGT-ADIMIFFATGDHGDGYpfdgpn 182
Cdd:cd04277    6 YSFSNTGGPYSYGYGREEDTTNTAALSAAQQAA-ARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 183 gflAHAYPP----YEGVGGDAHFDDDETFSYRSPQYYTlFSVAAHEFGHSLGLGHSRDPGA----------------LM- 241
Cdd:cd04277   79 ---GYAYYPgsgsGTAYGGDIWFNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMs 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 688575181 242 -------YPTYVYRDMDRFILprDDVNGIQSLYG 268
Cdd:cd04277  155 ynsgygnGASAGGGYPQTPML--LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 118-267 1.15e-09

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: 57.15  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 118 LTYRIENYTLDMSV----AEVDDSISRALKVWADVTPLRFT--RIYSGTADIMIFFATGDHgdgypfdgPNGFLAHAYPP 191
Cdd:cd00203    3 IPYVVVADDRDVEEenlsAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILVTRQDF--------DGGTGGWAYLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 192 --YEGVGGDAHFDDDETFSYRSPQyytlfsVAAHEFGHSLGLGHSRD--------------------PGALMYPTYV-YR 248
Cdd:cd00203   75 rvCDSLRGVGVLQDNQSGTKEGAQ------TIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTKGsFS 148

                        170
                 ....*....|....*....
gi 688575181 249 DMDRFILPRDDVNGIQSLY 267
Cdd:cd00203  149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 117-267 3.67e-08

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: 52.88  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 117 QLTYRIENYTLDmsvaEVDDSISRALKVWADVTPLRFTRIYSG-TADIMIFFATGDHGDgypfDGPNGFLAHAYPPYEGV 195
Cdd:cd04268    3 PITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 196 GGDAHFDDDETFSYRSPQYYTlfSVAAHEFGHSLGLGHS----------------RDPGALMYPTYVY-----RDMDRFI 254
Cdd:cd04268   75 ILLARVYLYSSFVEYSGARLR--NTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNfsiqlGDGQKYT 152

                        170
                 ....*....|...
gi 688575181 255 LPRDDVNGIQSLY 267
Cdd:cd04268  153 IGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-432 8.84e-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: 8.84e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 688575181   387 IDAVLYKEDsNTILFFANNQVYSYNErmKKMDKGFPKPVQKVFPGM 432
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 28-91 1.55e-05

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: 42.50  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688575181   28 GDQDTLAENYLTRLYGLPkqpaQSPSSSGGEKrssdMSLRLKEMQQFFKLKVTGKLDQETLEVM 91
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYP----GPVDGYFGPS----TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-336 2.08e-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: 41.46  E-value: 2.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 688575181   295 LDAVTMLR-GEIMFFKNSFFWRSYPQSPD-VELQLIQSFWPEIP 336
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDpGYPKLISSFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 215-267 5.84e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 44.29  E-value: 5.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 688575181 215 YTLfSVAAHEFGHSLGL-GHSRDPGALMYPTYVyRDmDRFILPRdDVNGIQSLY 267
Cdd:COG5549  181 YLL-ATARHELGHALGIwGHSPSPTDAMYFSQV-RN-PPPISPR-DINTLKRIY 230
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 202-252 6.90e-04

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 40.36  E-value: 6.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 688575181 202 DDDETFSYRspqyytLFSVAAHEFGHSLGLGHSRDPGALMYPTYVYRDMDR 252
Cdd:cd11375  114 PDEGLFLER------LLKEAVHELGHLFGLDHCPYYACVMNFSNSLEETDR 158
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
203-244 8.08e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 8.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 688575181 203 DDETFSYRspqyytLFSVAAHEFGHSLGLGHSRDPGALMYPT 244
Cdd:COG1913  115 DEELFLER------VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-376 1.39e-03

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 36.45  E-value: 1.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 688575181   339 IDAAFESvIQDKVFLIKGEKVWALYGYDIVQGYPKSLS 376
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLIS 37
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 111-233 1.89e-03

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 39.67  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181 111 YKWKK-HQLTYrienYTLDMSVAEVDDSISRALKVWADVTPLRFTRIYSGTADIMIFFatgDHGDGY-PFDGPNGFLAHA 188
Cdd:cd04327    1 KLWRNgTVLRI----AFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF---TPGDGYwSYVGTDALLIGA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 688575181 189 YPPYEGVGGDAHFDDDETFSyrspqyytlfSVAAHEFGHSLGLGH 233
Cdd:cd04327   74 DAPTMNLGWFTDDTPDPEFS----------RVVLHEFGHALGFIH 108
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 154-234 5.01e-03

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 36.96  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688575181  154 TRIYSGTADIMIFFATGDHGDGypfdGPNGFLAHAYPPYEGVGGdahfdddetfsYRSPQYYTLF--SVAAHEFGHSLGL 231
Cdd:pfam13582  55 TRIGQYGYDLGHLFTGRDGGGG----GGIAYVGGVCNSGSKFGV-----------NSGSGPVGDTgaDTFAHEIGHNFGL 119


                  ...
gi 688575181  232 GHS 234
Cdd:pfam13582 120 NHT 122
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-376 7.41e-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: 7.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 688575181  339 IDAAFESvIQDKVFLIKGEKVWALYGYDIVQGYPKSLS 376
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLIS 37
 
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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