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Conserved domains on  [gi|1783384083|ref|NP_001180685|]
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matrix metalloproteinase-21 precursor [Macaca mulatta]

Protein Classification

S41 family peptidase( domain architecture ID 10477998)

peptidase family S41 such as C-terminal processing protease (CTPase or CtpA) that contains the PDZ domain; active site consists of a serine/lysine catalytic dyad

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 2.08e-65

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: 210.14  E-value: 2.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 171 FSKRTLSWRLLGEalSSQLSAAEQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278     2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 251 HAW----RLGDIHFDDDEHFTPPTSDMGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278    77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                  .
gi 1783384083 327 G 327
Cdd:cd04278   157 G 157
HX super family cl02471
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-536 3.45e-26

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.


The actual alignment was detected with superfamily member cd00094:

Pssm-ID: 413329 [Multi-domain]  Cd Length: 194  Bit Score: 105.86  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIEILTGWHGIPTyNIDAFVhiWTWKRDERYFFRGNQYWRYDSDKDQALte 429
Cdd:cd00094    13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKKITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094    85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                         170       180
                  ....*....|....*....|....*...
gi 1783384083 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 6.83e-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: 54.83  E-value: 6.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1783384083  48 ADLHAAQRFLSRYGWSglraawgpssEGPPETPEGAALAAAVRRFQRANALPASGELDAATLAAM 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 2.08e-65

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: 210.14  E-value: 2.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 171 FSKRTLSWRLLGEalSSQLSAAEQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278     2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 251 HAW----RLGDIHFDDDEHFTPPTSDMGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278    77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                  .
gi 1783384083 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 5.26e-59

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: 193.60  E-value: 5.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 170 AFSKRTLSWRLLGEalSSQLSAAEQRRIVALAFRMWSEVTPLDFREdlaAPGAAVDIKLGFGRGRHlGCPRAFDGSGQEF 249
Cdd:pfam00413   1 KWRKKNLTYRILNY--TPDLPRAEVRRAIRRAFKVWSEVTPLTFTE---VSTGEADIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 250 AHAW-----RLGDIHFDDDEHFTPPT-SDMGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPA-FELDWSDRKAI 322
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 1783384083 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 3.45e-26

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: 105.86  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIEILTGWHGIPTyNIDAFVhiWTWKRDERYFFRGNQYWRYDSDKDQALte 429
Cdd:cd00094    13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKKITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094    85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                         170       180
                  ....*....|....*....|....*...
gi 1783384083 509 AYYsYAYNSIFFFKGNAYWKvVNDKDKQ 536
Cdd:cd00094   153 AFR-WLDGYYYFFKGDQYWR-FDPRSKE 178
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 171-328 3.11e-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: 84.32  E-value: 3.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083  171 FSKRTLSWRLLGEALSSqlsaaEQRRIVALAFRMWSEVTPLDFREDlaapGAAVDIKLGFGRGRHlGCPRAfdgsgqefa 250
Cdd:smart00235   5 WPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVER----TGTADIYISFGSGDS-GCTLS--------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083  251 HAWR-LGDIHFDDDehftpptsdMGISLLKVAVHEIGHVLGLPHT-YRT--GSIMQPNYIPQEP-AFELDWSDRKAIQKL 325
Cdd:smart00235  66 HAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRSdrDNYMYINYTNIDTrNFDLSEDDSLGIPYD 136


                   ...
gi 1783384083  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 6.83e-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: 54.83  E-value: 6.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1783384083  48 ADLHAAQRFLSRYGWSglraawgpssEGPPETPEGAALAAAVRRFQRANALPASGELDAATLAAM 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 5.19e-08

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: 49.16  E-value: 5.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1783384083  394 IDAFVhiwTWKRDERYFFRGNQYWRYDSDKDQaltedeqgKSYPKLISEGFPGIPS 449
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 82-114 1.34e-06

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 46.05  E-value: 1.34e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1783384083  82 GAALAAAVRRFQRANALPASGELDAATLAAMNR 114
Cdd:COG3409    37 GPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 2.26e-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: 44.48  E-value: 2.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1783384083 394 IDAFVhiwTWKRDERYFFRGNQYWRYDSDKDQaltedeqgKSYPKLISEgFPGIPS 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 1783384083 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 1783384083 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 2.08e-65

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: 210.14  E-value: 2.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 171 FSKRTLSWRLLGEalSSQLSAAEQRRIVALAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGRHlGCPRAFDGSGQEFA 250
Cdd:cd04278     2 WSKTNLTYRILNY--PPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEA--DIRISFARGNH-GDGYPFDGPGGTLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 251 HAW----RLGDIHFDDDEHFTPPTSDMGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLY 326
Cdd:cd04278    77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                  .
gi 1783384083 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 5.26e-59

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: 193.60  E-value: 5.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 170 AFSKRTLSWRLLGEalSSQLSAAEQRRIVALAFRMWSEVTPLDFREdlaAPGAAVDIKLGFGRGRHlGCPRAFDGSGQEF 249
Cdd:pfam00413   1 KWRKKNLTYRILNY--TPDLPRAEVRRAIRRAFKVWSEVTPLTFTE---VSTGEADIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 250 AHAW-----RLGDIHFDDDEHFTPPT-SDMGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPA-FELDWSDRKAI 322
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 1783384083 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 3.45e-26

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: 105.86  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 350 VMVRFSTYFFRNSWYWLyenRNNRTRYGDPIEILTGWHGIPTyNIDAFVhiWTWKRDERYFFRGNQYWRYDSDKDQALte 429
Cdd:cd00094    13 TTLRGELYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLPS-PVDAAF--ERPDTGKIYFFKGDKYWVYTGKNLEPG-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 430 deqgksYPKLISE-GFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKKITEVFPAVIPqnhpfrNIDS 508
Cdd:cd00094    85 ------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPD------KVDA 152

                         170       180
                  ....*....|....*....|....*...
gi 1783384083 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 1.72e-21

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: 92.37  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 322 IQKLYGSCEGSFDTAFDWIRKERnqygevmvrfsTYFFRNSWYWLYENRNNRTRYGDPIEILtGWhGIPTYNIDAFVHiw 401
Cdd:cd00094    42 ISSFWPSLPSPVDAAFERPDTGK-----------IYFFKGDKYWVYTGKNLEPGYPKPISDL-GF-PPTVKQIDAALR-- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 402 tWKRDER-YFFRGNQYWRYDSDKDQaltedeQGKSYPKLISEGFPGIPSPLDTAFYDRRQKlIYFFKESLVFAFDVNRNR 480
Cdd:cd00094   107 -WPDNGKtYFFKGDKYWRYDEKTQK------MDPGYPKLIETDFPGVPDKVDAAFRWLDGY-YYFFKGDQYWRFDPRSKE 178

                         170
                  ....*....|....*
gi 1783384083 481 VLNSYPKKITEVFPA 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 3.02e-21

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: 91.60  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 393 NIDAFVHIwtwkRDERYFFRGNQYWRYDSDKdqaltedeqGKSYPKLISEGFPGIPSPLDTAFYDRRQKLIYFFKESLVF 472
Cdd:cd00094     8 SFDAVTTL----RGELYFFKGRYFWRLSPGK---------PPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYW 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1783384083 473 AFDVNRNRVLnsYPKKITEV-FPAVIPQnhpfrnIDSAYYSYAYNSIFFFKGNAYWK 528
Cdd:cd00094    75 VYTGKNLEPG--YPKPISDLgFPPTVKQ------IDAALRWPDNGKTYFFKGDKYWR 123
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 171-328 3.11e-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: 84.32  E-value: 3.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083  171 FSKRTLSWRLLGEALSSqlsaaEQRRIVALAFRMWSEVTPLDFREDlaapGAAVDIKLGFGRGRHlGCPRAfdgsgqefa 250
Cdd:smart00235   5 WPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVER----TGTADIYISFGSGDS-GCTLS--------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083  251 HAWR-LGDIHFDDDehftpptsdMGISLLKVAVHEIGHVLGLPHT-YRT--GSIMQPNYIPQEP-AFELDWSDRKAIQKL 325
Cdd:smart00235  66 HAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRSdrDNYMYINYTNIDTrNFDLSEDDSLGIPYD 136


                   ...
gi 1783384083  326 YGS 328
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 185-326 7.97e-11

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 60.97  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 185 LSSQLSAAEQRRIVAlAFRMWSEVTPLDFREdlAAPGAAVDIKLGFGRGRHLGCP-RAFDGSGQEFAHawrlGDIHFDDD 263
Cdd:cd04268     8 IDDSVPDKLRAAILD-AIEAWNKAFAIGFKN--ANDVDPADIRYSVIRWIPYNDGtWSYGPSQVDPLT----GEILLARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 264 EHFTPPTSDMGISLLKVAVHEIGHVLGLPH----------------TYRTGSIMQP----NYIPQEPAFELDWS--DRKA 321
Cdd:cd04268    81 YLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaeKGDTSSVMDYapsnFSIQLGDGQKYTIGpyDIAA 160


                  ....*
gi 1783384083 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 6.83e-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: 54.83  E-value: 6.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1783384083  48 ADLHAAQRFLSRYGWSglraawgpssEGPPETPEGAALAAAVRRFQRANALPASGELDAATLAAM 112
Cdd:pfam01471   3 EDVKELQRYLNRLGYY----------PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 201-327 2.51e-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: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 201 AFRMWSEVTPLDFREDLAAPGAAvDIKLGFGRGRHLG-----CPRAFDGSGQEFAhaWRLGDIHFDDDEHFTPPTsdmGI 275
Cdd:cd04279    29 AAAEWENVGPLKFVYNPEEDNDA-DIVIFFDRPPPVGgagggLARAGFPLISDGN--RKLFNRTDINLGPGQPRG---AE 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1783384083 276 SLLKVAVHEIGHVLGLPHTYRTGS-IMQPNYIPQEP-AFELDWSDRKAIQKLYG 327
Cdd:cd04279   103 NLQAIALHELGHALGLWHHSDRPEdAMYPSQGQGPDgNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 186-326 3.06e-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: 53.29  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 186 SSQLSAAEQRRIVALAFRMWSEVTPLDFREDLAAPGAAvDIKLGFGRGrhlgcprAFDGSGQefAHAW-------RLGDI 258
Cdd:cd00203    15 EEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKA-DIAILVTRQ-------DFDGGTG--GWAYlgrvcdsLRGVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 259 HFDDdehftppTSDMGISLLKVAVHEIGHVLGLPH--------------------TYRTGSIMQPNYIPQEPAFELDWS- 317
Cdd:cd00203    85 VLQD-------NQSGTKEGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTKGSFSDGQRKDFSq 157

                         170
                  ....*....|
gi 1783384083 318 -DRKAIQKLY 326
Cdd:cd00203   158 cDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 5.19e-08

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: 49.16  E-value: 5.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1783384083  394 IDAFVhiwTWKRDERYFFRGNQYWRYDSDKDQaltedeqgKSYPKLISEGFPGIPS 449
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 186-327 6.38e-08

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: 52.80  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 186 SSQLSAAEQRRIVAlAFRMWSEVTPLDFREDLAAPGAavDIKLGFGRGrHLGCPRAFDGSGQEFAHAWRLGDIHFDDDEH 265
Cdd:cd04277    28 TAALSAAQQAAARD-ALEAWEDVADIDFVEVSDNSGA--DIRFGNSSD-PDGNTAGYAYYPGSGSGTAYGGDIWFNSSYD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384083 266 -FTPPTSDMGislLKVAVHEIGHVLGL--PHTYRTG--------------SIM----QPNYIPQEPAFELDW---SDRKA 321
Cdd:cd04277   104 tNSDSPGSYG---YQTIIHEIGHALGLehPGDYNGGdpvpptyaldsreyTVMsynsGYGNGASAGGGYPQTpmlLDIAA 180


                  ....*.
gi 1783384083 322 IQKLYG 327
Cdd:cd04277   181 LQYLYG 186
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 82-114 1.34e-06

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 46.05  E-value: 1.34e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1783384083  82 GAALAAAVRRFQRANALPASGELDAATLAAMNR 114
Cdd:COG3409    37 GPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-449 2.26e-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: 44.48  E-value: 2.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1783384083 394 IDAFVhiwTWKRDERYFFRGNQYWRYDSDKDQaltedeqgKSYPKLISEgFPGIPS 449
Cdd:pfam00045   1 IDAAF---EDRDGKTYFFKGRKYWRFDPQRVE--------PGYPKLISD-FPGLPC 44
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
83-124 1.50e-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: 1.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1783384083  83 AALAAAVRRFQRANALPASGELDAATLAAMNRPrcgvPDTRL 124
Cdd:COG2989   239 AELVEAVKRFQARHGLKADGVIGPATLAALNVS----PEERI 276
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 1783384083 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 1783384083 277 LLKVAVHEIGHVLGLPH 293
Cdd:COG1913   123 VLKEAVHELGHLFGLGH 139
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 277-293 6.85e-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: 6.85e-04
                          10
                  ....*....|....*..
gi 1783384083 277 LLKVAVHEIGHVLGLPH 293
Cdd:cd11375   123 LLKEAVHELGHLFGLDH 139
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 267-309 1.01e-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: 41.47  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1783384083 267 TPPTSDMGISLLKVAVHEIGHVLGLPHTYR---------------------TGSIM---QPNYIPQE 309
Cdd:pfam16313   3 PFPDELMGALLRFVSAHEVGHTLGLRHNFAassaypvdslrdksftrkygtTPSIMdyaRFNYVAQP 69
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 451-494 1.12e-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: 36.84  E-value: 1.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1783384083  451 LDTAFYDRRQKlIYFFKESLVFAFDVnrNRVLNSYPKKITEVFP 494
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDP--KRVDPGYPKLISSFFP 41
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 273-312 2.04e-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: 39.62  E-value: 2.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1783384083 273 MGISLLKVAVHEIGHVLGLPHTYRtGSIMQPNYIPQEPAF 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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