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Conserved domains on  [gi|1088699139|ref|NP_001333542|]
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Peptidase metallopeptidase domain-containing protein [Caenorhabditis elegans]

Protein Classification

ZnMc_MMP and HX domain-containing protein( domain architecture ID 10136642)

ZnMc_MMP and HX domain-containing protein

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 ...
 39-195 3.38e-62

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: 197.43  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  39 WGKSVITYRLKQPSQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEDEqkANIDIVFAAGDHEDGEPFDGKGNILAHAF 118
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQE--ADIRISFARGNHGDGYPFDGPGGTLAHAF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088699139 119 FP-RYGGDVHFDEDELWSA-NKTKGVDLYAVAVHEIGHSLGLKHSSNHLSIMAPFYKQYTGAVmHLHQDDISAVKRLYG 195
Cdd:cd04278    80 FPgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKF-KLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 213-404 2.62e-31

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: 117.80  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 213 ELCTKPYLDAVTTLkNGTILAFRGKMFFELKTTRKWLLPRKINRIFPF-EGPLEAA-TTDRHGNVYFFKKDTYWVMTkHG 290
Cdd:cd00094     2 DACDPLSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSlPSPVDAAfERPDTGKIYFFKGDKYWVYT-GK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 291 DMMNGYPKKISQ-GLTDTPDGINAALYYHEDGKPYFFKKSYFWQYSRygKHKLWPRAIVSIFENQNS--PPEIDAAFQLN 367
Cdd:cd00094    80 NLEPGYPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDE--KTQKMDPGYPKLIETDFPgvPDKVDAAFRWL 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1088699139 368 NTSSFLFHQNKYWKVSGDPMRIEKGFPRSLSRDWFNC 404
Cdd:cd00094   158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 39-195 3.38e-62

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: 197.43  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  39 WGKSVITYRLKQPSQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEDEqkANIDIVFAAGDHEDGEPFDGKGNILAHAF 118
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQE--ADIRISFARGNHGDGYPFDGPGGTLAHAF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088699139 119 FP-RYGGDVHFDEDELWSA-NKTKGVDLYAVAVHEIGHSLGLKHSSNHLSIMAPFYKQYTGAVmHLHQDDISAVKRLYG 195
Cdd:cd04278    80 FPgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKF-KLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 39-195 2.43e-60

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: 192.83  E-value: 2.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  39 WGKSVITYRLKQPSQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEdeqKANIDIVFAAGDHEDGEPFDGKGNILAHAF 118
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG---EADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 119 FP--RYGGDVHFDEDELW--SANKTKGVDLYAVAVHEIGHSLGLKHSSNHLSIMAPFYKQYTGAVMHLHQDDISAVKRLY 194
Cdd:pfam00413  79 FPgpGLGGDIHFDDDETWtvGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLY 158


                  .
gi 1088699139 195 G 195
Cdd:pfam00413 159 G 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 213-404 2.62e-31

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: 117.80  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 213 ELCTKPYLDAVTTLkNGTILAFRGKMFFELKTTRKWLLPRKINRIFPF-EGPLEAA-TTDRHGNVYFFKKDTYWVMTkHG 290
Cdd:cd00094     2 DACDPLSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSlPSPVDAAfERPDTGKIYFFKGDKYWVYT-GK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 291 DMMNGYPKKISQ-GLTDTPDGINAALYYHEDGKPYFFKKSYFWQYSRygKHKLWPRAIVSIFENQNS--PPEIDAAFQLN 367
Cdd:cd00094    80 NLEPGYPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDE--KTQKMDPGYPKLIETDFPgvPDKVDAAFRWL 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1088699139 368 NTSSFLFHQNKYWKVSGDPMRIEKGFPRSLSRDWFNC 404
Cdd:cd00094   158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 39-196 1.16e-22

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: 92.80  E-value: 1.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139   39 WGKSVITYRLKQPSqrmSLSQQKAVFARAFATWEEHTRLWFVAVDDEdeqkANIDIVFAAGDHedgepfdgkGNILAHAF 118
Cdd:smart00235   5 WPKGTVPYVIDSSS---LSPEEREAIAKALAEWSDVTCIRFVERTGT----ADIYISFGSGDS---------GCTLSHAG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  119 FPryGGDVHFDeDELWSANktkgvdlYAVAVHEIGHSLGLKHSSN---HLSIMAPFYKQYTGAVMHLHQDDISAVKRLYG 195
Cdd:smart00235  69 RP--GGDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSrsdRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 1088699139  196 A 196
Cdd:smart00235 139 S 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 360-403 2.07e-07

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.24  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1088699139  360 IDAAFQLNNTSSFLFHQNKYWKVSGDPMriEKGFPRSLSRDWFN 403
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRV--DPGYPKLISSFFPG 42
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 50-198 1.97e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.45  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  50 QPSQRMSLSQQ---KAVFARAFATWEEHTRLWFVavddEDEQKANIDIVFAA---GDHEDGEP----------FDGKGNI 113
Cdd:COG5549    89 DRPPSAAQQRAqqwVAAVLQAIAEWNAYLPLEVV----ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNI 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 114 LAHAFF----PRYGGDvhfdedelwsanktkgvDLYAVAVHEIGHSLGLK-HSSNHLSIMapfYKQYTGAVMHLHQDDIS 188
Cdd:COG5549   165 LSHRFTillsPNQTGK-----------------YLLATARHELGHALGIWgHSPSPTDAM---YFSQVRNPPPISPRDIN 224

                         170
                  ....*....|
gi 1088699139 189 AVKRLYGAPV 198
Cdd:COG5549   225 TLKRIYQQPT 234
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 264-301 1.08e-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: 1.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1088699139 264 LEAATTDRHGNVYFFKKDTYWVMTkHGDMMNGYPKKIS 301
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFD-PQRVEPGYPKLIS 37
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 39-195 3.38e-62

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: 197.43  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  39 WGKSVITYRLKQPSQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEDEqkANIDIVFAAGDHEDGEPFDGKGNILAHAF 118
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQE--ADIRISFARGNHGDGYPFDGPGGTLAHAF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088699139 119 FP-RYGGDVHFDEDELWSA-NKTKGVDLYAVAVHEIGHSLGLKHSSNHLSIMAPFYKQYTGAVmHLHQDDISAVKRLYG 195
Cdd:cd04278    80 FPgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKF-KLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 39-195 2.43e-60

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: 192.83  E-value: 2.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  39 WGKSVITYRLKQPSQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEdeqKANIDIVFAAGDHEDGEPFDGKGNILAHAF 118
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG---EADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 119 FP--RYGGDVHFDEDELW--SANKTKGVDLYAVAVHEIGHSLGLKHSSNHLSIMAPFYKQYTGAVMHLHQDDISAVKRLY 194
Cdd:pfam00413  79 FPgpGLGGDIHFDDDETWtvGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLY 158


                  .
gi 1088699139 195 G 195
Cdd:pfam00413 159 G 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 213-404 2.62e-31

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: 117.80  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 213 ELCTKPYLDAVTTLkNGTILAFRGKMFFELKTTRKWLLPRKINRIFPF-EGPLEAA-TTDRHGNVYFFKKDTYWVMTkHG 290
Cdd:cd00094     2 DACDPLSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSlPSPVDAAfERPDTGKIYFFKGDKYWVYT-GK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 291 DMMNGYPKKISQ-GLTDTPDGINAALYYHEDGKPYFFKKSYFWQYSRygKHKLWPRAIVSIFENQNS--PPEIDAAFQLN 367
Cdd:cd00094    80 NLEPGYPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDE--KTQKMDPGYPKLIETDFPgvPDKVDAAFRWL 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1088699139 368 NTSSFLFHQNKYWKVSGDPMRIEKGFPRSLSRDWFNC 404
Cdd:cd00094   158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 39-196 1.16e-22

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: 92.80  E-value: 1.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139   39 WGKSVITYRLKQPSqrmSLSQQKAVFARAFATWEEHTRLWFVAVDDEdeqkANIDIVFAAGDHedgepfdgkGNILAHAF 118
Cdd:smart00235   5 WPKGTVPYVIDSSS---LSPEEREAIAKALAEWSDVTCIRFVERTGT----ADIYISFGSGDS---------GCTLSHAG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  119 FPryGGDVHFDeDELWSANktkgvdlYAVAVHEIGHSLGLKHSSN---HLSIMAPFYKQYTGAVMHLHQDDISAVKRLYG 195
Cdd:smart00235  69 RP--GGDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSrsdRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 1088699139  196 A 196
Cdd:smart00235 139 S 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 50-195 5.36e-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: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  50 QPSQRMSLSQQKAVFArAFATWEEHTRLWFVAVDDEDEQkANIDIVFAagdheDGEPFDGKGNILAHAFFPR--YGGDVH 127
Cdd:cd04279    13 APPDSRAQSWLQAVKQ-AAAEWENVGPLKFVYNPEEDND-ADIVIFFD-----RPPPVGGAGGGLARAGFPLisDGNRKL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1088699139 128 FDEDELWSANKTKGVDLY--AVAVHEIGHSLGLKHSSNH-LSIMAPFYKQYTGAVMHLHQDDISAVKRLYG 195
Cdd:cd04279    86 FNRTDINLGPGQPRGAENlqAIALHELGHALGLWHHSDRpEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 32-195 1.47e-14

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 71.68  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  32 YSIEGSYWGKSVITYRLKQPSQRMSLS-QQKAVFARAFATWEEHTRLWFVAVDDEDeqkaNIDIVFAAGDhedgepfDGK 110
Cdd:cd04277     6 YSFSNTGGPYSYGYGREEDTTNTAALSaAQQAAARDALEAWEDVADIDFVEVSDNS----GADIRFGNSS-------DPD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 111 GNILAHAFFP------RYGGDVHFDEDELWSaNKTKGVDLYAVAVHEIGHSLGLKHS----------------SNHLSIM 168
Cdd:cd04277    75 GNTAGYAYYPgsgsgtAYGGDIWFNSSYDTN-SDSPGSYGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYTVM 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1088699139 169 APFYKQYTGAVMHLH------QDDISAVKRLYG 195
Cdd:cd04277   154 SYNSGYGNGASAGGGypqtpmLLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 42-194 2.23e-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: 55.99  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  42 SVITYRLKQPSQRMSLsQQKAVFARAFATWEEHTRLWFVAVDdEDEQKANIDIVFAAGDHEdgepfdgkGNILAHAFFPR 121
Cdd:cd00203     6 VVVADDRDVEEENLSA-QIQSLILIAMQIWRDYLNIRFVLVG-VEIDKADIAILVTRQDFD--------GGTGGWAYLGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 122 ----YGGDVHFDEDELWsanktkGVDLYAVAVHEIGHSLGLKHSSNHL--------------------SIMAPFYKQYTG 177
Cdd:cd00203    76 vcdsLRGVGVLQDNQSG------TKEGAQTIAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKGSFSD 149

                         170
                  ....*....|....*...
gi 1088699139 178 AVM-HLHQDDISAVKRLY 194
Cdd:cd00203   150 GQRkDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 360-403 2.07e-07

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.24  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1088699139  360 IDAAFQLNNTSSFLFHQNKYWKVSGDPMriEKGFPRSLSRDWFN 403
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRV--DPGYPKLISSFFPG 42
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 41-194 6.42e-07

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: 49.03  E-value: 6.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  41 KSVITYRLkqpsQRMSLSQQKAVFARAFATWEEHTRLWFVAVDDEDEQkaniDIVFAAGDheDGEPFDGKGNILAHAFFP 120
Cdd:cd04268     1 KKPITYYI----DDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPA----DIRYSVIR--WIPYNDGTWSYGPSQVDP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 121 RyGGDVHFDEDELWSAN-KTKGVDLYAVAVHEIGHSLGLKH----SSNHLSIMAPFYKQYTGAVMH-------------- 181
Cdd:cd04268    71 L-TGEILLARVYLYSSFvEYSGARLRNTAEHELGHALGLRHnfaaSDRDDNVDLLAEKGDTSSVMDyapsnfsiqlgdgq 149

                         170
                  ....*....|....*.
gi 1088699139 182 ---LHQDDISAVKRLY 194
Cdd:cd04268   150 kytIGPYDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 50-198 1.97e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.45  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  50 QPSQRMSLSQQ---KAVFARAFATWEEHTRLWFVavddEDEQKANIDIVFAA---GDHEDGEP----------FDGKGNI 113
Cdd:COG5549    89 DRPPSAAQQRAqqwVAAVLQAIAEWNAYLPLEVV----ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNI 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 114 LAHAFF----PRYGGDvhfdedelwsanktkgvDLYAVAVHEIGHSLGLK-HSSNHLSIMapfYKQYTGAVMHLHQDDIS 188
Cdd:COG5549   165 LSHRFTillsPNQTGK-----------------YLLATARHELGHALGIWgHSPSPTDAM---YFSQVRNPPPISPRDIN 224

                         170
                  ....*....|
gi 1088699139 189 AVKRLYGAPV 198
Cdd:COG5549   225 TLKRIYQQPT 234
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 266-301 4.23e-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: 40.69  E-value: 4.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1088699139  266 AATTDRHGNVYFFKKDTYWVMTKHgDMMNGYPKKIS 301
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPK-RVDPGYPKLIS 37
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 264-301 1.08e-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: 1.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1088699139 264 LEAATTDRHGNVYFFKKDTYWVMTkHGDMMNGYPKKIS 301
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFD-PQRVEPGYPKLIS 37
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 360-404 1.13e-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: 1.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1088699139 360 IDAAFQLNNTSSFLFHQNKYWKVsgDPMRIEKGFPRSLSRD-WFNC 404
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRF--DPQRVEPGYPKLISDFpGLPC 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 38-199 1.12e-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: 40.06  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139  38 YW--GKSVITYRLKQPSQrmslSQQKAVFARAfATWEEHTRLWFVAVDDEDeqkANIDIVFAAGDheDGEPFDGKGNILA 115
Cdd:cd04327     2 LWrnGTVLRIAFLGGPDA----FLKDKVRAAA-REWLPYANLKFKFVTDAD---ADIRISFTPGD--GYWSYVGTDALLI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088699139 116 HAFFP--RYGGDVHFDEDElwsanktkgvDLYAVAVHEIGHSLGLKHSsnHLSimaPFykqytgavmHLHQDDISAVKRL 193
Cdd:cd04327    72 GADAPtmNLGWFTDDTPDP----------EFSRVVLHEFGHALGFIHE--HQS---PA---------ANIPWDKEAVYAY 127


                  ....*.
gi 1088699139 194 YGAPVK 199
Cdd:cd04327   128 FSGPPN 133
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
144-163 9.27e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.86  E-value: 9.27e-03
                          10        20
                  ....*....|....*....|
gi 1088699139 144 LYAVAVHEIGHSLGLKHSSN 163
Cdd:COG1913   123 VLKEAVHELGHLFGLGHCPN 142
 
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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