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Conserved domains on  [gi|21693575|gb|AAM75352|]
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matrix metalloproteinase-21 [Homo sapiens]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 171-327 4.62e-66

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: 212.06  E-value: 4.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 171 FSKRTLSWRLLGEalSSQLSAADQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278   2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 251 HAW----RLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 21693575 327 G 327
Cdd:cd04278 157 G 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-536 1.86e-28

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: 112.02  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIQILTGWPGIPThNIDAFVhiWTWKRDERYFFQGNQYWRYDSDKDQALte 429
Cdd:cd00094  13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094  85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                       170       180
                ....*....|....*....|....*...
gi 21693575 509 AYYsYAYNSIFFFKGNAYWKvVNDKDKQ 536
Cdd:cd00094 153 AFR-WLDGYYYFFKGDQYWR-FDPRSKE 178
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-112 2.15e-10

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: 56.37  E-value: 2.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21693575    48 ADLHAAQRFLSRYGWSgvwaawgpspEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAM 112
Cdd:pfam01471   3 EDVKELQRYLNRLGYY----------PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 171-327 4.62e-66

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: 212.06  E-value: 4.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 171 FSKRTLSWRLLGEalSSQLSAADQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278   2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 251 HAW----RLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 21693575 327 G 327
Cdd:cd04278 157 G 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 170-327 1.68e-58

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: 192.06  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575   170 AFSKRTLSWRLLGEalSSQLSAADQRRIVALAFRMWSEVTPLDFREdlaAPGAAVDIKLGFGRGRHlGCPRAFDGSGQEF 249
Cdd:pfam00413   1 KWRKKNLTYRILNY--TPDLPRAEVRRAIRRAFKVWSEVTPLTFTE---VSTGEADIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575   250 AHAW-----RLGDIHFDDDEHFTPPTSDT-GISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPA-FELDWSDRKAI 322
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSDPPhGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 21693575   323 QKLYG 327
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-536 1.86e-28

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: 112.02  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIQILTGWPGIPThNIDAFVhiWTWKRDERYFFQGNQYWRYDSDKDQALte 429
Cdd:cd00094  13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094  85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                       170       180
                ....*....|....*....|....*...
gi 21693575 509 AYYsYAYNSIFFFKGNAYWKvVNDKDKQ 536
Cdd:cd00094 153 AFR-WLDGYYYFFKGDQYWR-FDPRSKE 178
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 171-328 1.36e-19

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: 85.09  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575    171 FSKRTLSWRLLGEALSSqlsaaDQRRIVALAFRMWSEVTPLDFREDlaapGAAVDIKLGFGRGRHlGCPRAfdgsgqefa 250
Cdd:smart00235   5 WPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVER----TGTADIYISFGSGDS-GCTLS--------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575    251 HAWR-LGDIHFDDDehftpptsdTGISLLKVAVHEIGHVLGLPHT-YRT--GSIMQPNYIPQEP-AFELDWSDRKAIQKL 325
Cdd:smart00235  66 HAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRSdrDNYMYINYTNIDTrNFDLSEDDSLGIPYD 136


                   ...
gi 21693575    326 YGS 328
Cdd:smart00235 137 YGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-112 2.15e-10

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: 56.37  E-value: 2.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21693575    48 ADLHAAQRFLSRYGWSgvwaawgpspEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAM 112
Cdd:pfam01471   3 EDVKELQRYLNRLGYY----------PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 1.37e-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: 48.01  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21693575    394 IDAFVhiwTWKRDERYFFQGNQYWRYDSDKDQaltedeqgKSYPKLISEGFPGIPS 449
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 82-114 2.39e-06

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 45.28  E-value: 2.39e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 21693575  82 GAALAEAVRRFQRANALPASGELDAATLAAMNR 114
Cdd:COG3409  37 GPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 2.84e-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: 2.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21693575   394 IDAFVhiwTWKRDERYFFQGNQYWRYDSDKDQaltedeqgKSYPKLISEgFPGIPS 449
Cdd:pfam00045   1 IDAAF---EDRDGKTYFFKGRKYWRFDPQRVE--------PGYPKLISD-FPGLPC 44
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
277-293 1.92e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 1.92e-04
                         10
                 ....*....|....*..
gi 21693575  277 LLKVAVHEIGHVLGLPH 293
Cdd:NF033823 122 LAKEAVHELGHLLGLGH 138
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
277-293 2.44e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 2.44e-04
                        10
                ....*....|....*..
gi 21693575 277 LLKVAVHEIGHVLGLPH 293
Cdd:COG1913 123 VLKEAVHELGHLFGLGH 139
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 171-327 4.62e-66

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: 212.06  E-value: 4.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 171 FSKRTLSWRLLGEalSSQLSAADQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278   2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 251 HAW----RLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 21693575 327 G 327
Cdd:cd04278 157 G 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 170-327 1.68e-58

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: 192.06  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575   170 AFSKRTLSWRLLGEalSSQLSAADQRRIVALAFRMWSEVTPLDFREdlaAPGAAVDIKLGFGRGRHlGCPRAFDGSGQEF 249
Cdd:pfam00413   1 KWRKKNLTYRILNY--TPDLPRAEVRRAIRRAFKVWSEVTPLTFTE---VSTGEADIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575   250 AHAW-----RLGDIHFDDDEHFTPPTSDT-GISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPA-FELDWSDRKAI 322
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSDPPhGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 21693575   323 QKLYG 327
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-536 1.86e-28

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: 112.02  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIQILTGWPGIPThNIDAFVhiWTWKRDERYFFQGNQYWRYDSDKDQALte 429
Cdd:cd00094  13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094  85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                       170       180
                ....*....|....*....|....*...
gi 21693575 509 AYYsYAYNSIFFFKGNAYWKvVNDKDKQ 536
Cdd:cd00094 153 AFR-WLDGYYYFFKGDQYWR-FDPRSKE 178
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 322-495 6.76e-22

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: 93.53  E-value: 6.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 322 IQKLYGSCEGSFDTAFDWIRKERnqygevmvrfsTYFFRNSWYWLYENRNNRTRYGDPIQILtGWPGIPTHnIDAFVHiw 401
Cdd:cd00094  42 ISSFWPSLPSPVDAAFERPDTGK-----------IYFFKGDKYWVYTGKNLEPGYPKPISDL-GFPPTVKQ-IDAALR-- 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 402 tWKRDER-YFFQGNQYWRYDSDKDQaltedeQGKSYPKLISEGFPGIPSPLDTAFYDRRQKlIYFFKESLVFAFDVNRNR 480
Cdd:cd00094 107 -WPDNGKtYFFKGDKYWRYDEKTQK------MDPGYPKLIETDFPGVPDKVDAAFRWLDGY-YYFFKGDQYWRFDPRSKE 178

                       170
                ....*....|....*
gi 21693575 481 VLNSYPKRITEVFPA 495
Cdd:cd00094 179 VRVGYPLKISSDWLG 193
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-528 2.64e-20

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: 88.91  E-value: 2.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 393 NIDAFVHIwtwkRDERYFFQGNQYWRYDSDKdqaltedeqGKSYPKLISEGFPGIPSPLDTAFYDRRQKLIYFFKESLVF 472
Cdd:cd00094   8 SFDAVTTL----RGELYFFKGRYFWRLSPGK---------PPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYW 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21693575 473 AFDVNRNRVLnsYPKRITEV-FPAVIPQnhpfrnIDSAYYSYAYNSIFFFKGNAYWK 528
Cdd:cd00094  75 VYTGKNLEPG--YPKPISDLgFPPTVKQ------IDAALRWPDNGKTYFFKGDKYWR 123
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 171-328 1.36e-19

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: 85.09  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575    171 FSKRTLSWRLLGEALSSqlsaaDQRRIVALAFRMWSEVTPLDFREDlaapGAAVDIKLGFGRGRHlGCPRAfdgsgqefa 250
Cdd:smart00235   5 WPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVER----TGTADIYISFGSGDS-GCTLS--------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575    251 HAWR-LGDIHFDDDehftpptsdTGISLLKVAVHEIGHVLGLPHT-YRT--GSIMQPNYIPQEP-AFELDWSDRKAIQKL 325
Cdd:smart00235  66 HAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRSdrDNYMYINYTNIDTrNFDLSEDDSLGIPYD 136


                   ...
gi 21693575    326 YGS 328
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 185-326 1.91e-10

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: 59.82  E-value: 1.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 185 LSSQLSAADQRRIVAlAFRMWSEVTPLDFREdlAAPGAAVDIKLGFGRGRHLGCP-RAFDGSGQEFAHawrlGDIHFDDD 263
Cdd:cd04268   8 IDDSVPDKLRAAILD-AIEAWNKAFAIGFKN--ANDVDPADIRYSVIRWIPYNDGtWSYGPSQVDPLT----GEILLARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 264 EHFTPPTSDTGISLLKVAVHEIGHVLGLPH----------------TYRTGSIMQP----NYIPQEPAFELDWS--DRKA 321
Cdd:cd04268  81 YLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaeKGDTSSVMDYapsnFSIQLGDGQKYTIGpyDIAA 160


                ....*
gi 21693575 322 IQKLY 326
Cdd:cd04268 161 IKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-112 2.15e-10

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: 56.37  E-value: 2.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21693575    48 ADLHAAQRFLSRYGWSgvwaawgpspEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAM 112
Cdd:pfam01471   3 EDVKELQRYLNRLGYY----------PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 186-326 1.32e-08

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: 54.45  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 186 SSQLSAADQRRIVALAFRMWSEVTPLDFREDLAAPGAAvDIKLGFGRGrhlgcprAFDGSGQefAHAW-------RLGDI 258
Cdd:cd00203  15 EEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKA-DIAILVTRQ-------DFDGGTG--GWAYlgrvcdsLRGVG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 259 HFDDdehftppTSDTGISLLKVAVHEIGHVLGLPH--------------------TYRTGSIMQPNYIPQEPAFELDWS- 317
Cdd:cd00203  85 VLQD-------NQSGTKEGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTKGSFSDGQRKDFSq 157

                       170
                ....*....|
gi 21693575 318 -DRKAIQKLY 326
Cdd:cd00203 158 cDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 201-327 2.87e-08

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: 53.23  E-value: 2.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 201 AFRMWSEVTPLDFREDLAAPGAAvDIKLGFGRGRHLG-----CPRAFDGSGQEFAhaWRLGDIHFDDDEHFTPPTSDTgi 275
Cdd:cd04279  29 AAAEWENVGPLKFVYNPEEDNDA-DIVIFFDRPPPVGgagggLARAGFPLISDGN--RKLFNRTDINLGPGQPRGAEN-- 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21693575 276 sLLKVAVHEIGHVLGLPHTYRTGS-IMQPNYIPQEP-AFELDWSDRKAIQKLYG 327
Cdd:cd04279 104 -LQAIALHELGHALGLWHHSDRPEdAMYPSQGQGPDgNPTLSARDVATLKRLYG 156
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 1.37e-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: 48.01  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21693575    394 IDAFVhiwTWKRDERYFFQGNQYWRYDSDKDQaltedeqgKSYPKLISEGFPGIPS 449
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 186-327 2.81e-07

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: 50.88  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 186 SSQLSAADQRRIVAlAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGrHLGCPRAFDGSGQEFAHAWRLGDIHFDD--D 263
Cdd:cd04277  28 TAALSAAQQAAARD-ALEAWEDVADIDFVEVSDNSGA--DIRFGNSSD-PDGNTAGYAYYPGSGSGTAYGGDIWFNSsyD 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21693575 264 EHFTPPTSDTGisllKVAVHEIGHVLGL--PHTYRTG--------------SIM----QPNYIPQEPAFELDW---SDRK 320
Cdd:cd04277 104 TNSDSPGSYGY----QTIIHEIGHALGLehPGDYNGGdpvpptyaldsreyTVMsynsGYGNGASAGGGYPQTpmlLDIA 179


                ....*..
gi 21693575 321 AIQKLYG 327
Cdd:cd04277 180 ALQYLYG 186
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 82-114 2.39e-06

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 45.28  E-value: 2.39e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 21693575  82 GAALAEAVRRFQRANALPASGELDAATLAAMNR 114
Cdd:COG3409  37 GPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 2.84e-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: 2.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21693575   394 IDAFVhiwTWKRDERYFFQGNQYWRYDSDKDQaltedeqgKSYPKLISEgFPGIPS 449
Cdd:pfam00045   1 IDAAF---EDRDGKTYFFKGRKYWRFDPQRVE--------PGYPKLISD-FPGLPC 44
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
83-115 1.80e-05

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 47.63  E-value: 1.80e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 21693575  83 AALAEAVRRFQRANALPASGELDAATLAAMNRP 115
Cdd:COG2989 239 AELVEAVKRFQARHGLKADGVIGPATLAALNVS 271
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
277-293 1.92e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 1.92e-04
                         10
                 ....*....|....*..
gi 21693575  277 LLKVAVHEIGHVLGLPH 293
Cdd:NF033823 122 LAKEAVHELGHLLGLGH 138
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
277-293 2.44e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 2.44e-04
                        10
                ....*....|....*..
gi 21693575 277 LLKVAVHEIGHVLGLPH 293
Cdd:COG1913 123 VLKEAVHELGHLFGLGH 139
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 277-293 6.23e-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: 40.74  E-value: 6.23e-04
                        10
                ....*....|....*..
gi 21693575 277 LLKVAVHEIGHVLGLPH 293
Cdd:cd11375 123 LLKEAVHELGHLFGLDH 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 451-494 7.55e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 37.61  E-value: 7.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 21693575    451 LDTAFYDRRQKlIYFFKESLVFAFDVnrNRVLNSYPKRITEVFP 494
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDP--KRVDPGYPKLISSFFP 41
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 280-309 1.28e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 41.08  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21693575   280 VAVHEIGHVLGLPHTYR---------------------TGSIM---QPNYIPQE 309
Cdd:pfam16313  16 VSAHEVGHTLGLRHNFAassaypvdslrdksftrkygtTPSIMdyaRFNYVAQP 69
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 272-329 1.70e-03

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 39.91  E-value: 1.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21693575 272 DTGISLLKVAVHEIGHVLGLPH---------TYRTGSIMQP--NYIpqepAFELDWSD--RKAI----QKLYGSC 329
Cdd:cd04273 135 DTGLSSAFTIAHELGHVLGMPHdgdgnscgpEGKDGHIMSPtlGAN----TGPFTWSKcsRRYLtsflDTGDGNC 205
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-390 2.44e-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: 36.07  E-value: 2.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21693575    333 FDTAFDWIRKErnqygevmvrfsTYFFRNSWYWLYENRNNRTRYgdPIQILTGWPGIP 390
Cdd:smart00120   1 IDAAFELRDGK------------TYFFKGDKYWRFDPKRVDPGY--PKLISSFFPGLP 44
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 273-312 2.74e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 39.23  E-value: 2.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21693575 273 TGISLLKVAVHEIGHVLGLPHTYRtGSIMQPNYIPQEPAF 312
Cdd:cd04276 112 LAASLRYLLAHEVGHTLGLRHNFK-ASSDGSNEELEDPLG 150
 
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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