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Conserved domains on  [gi|767970481|ref|XP_011541250|]
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matrix metalloproteinase-27 isoform X2 [Homo sapiens]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 233-422 2.26e-65

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: 208.70  E-value: 2.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 233 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 311
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 312 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 390
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767970481 391 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 422
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-218 4.51e-56

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: 183.59  E-value: 4.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481  106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAF------------------------- 160
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFgrgdhgdgypfdgpggvlahaffpg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767970481  161 --------------------RTRGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:pfam00413  82 pglggdihfdddetwtvgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.23e-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: 55.21  E-value: 4.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970481   26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 233-422 2.26e-65

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: 208.70  E-value: 2.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 233 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 311
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 312 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 390
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767970481 391 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 422
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-218 4.51e-56

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: 183.59  E-value: 4.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481  106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAF------------------------- 160
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFgrgdhgdgypfdgpggvlahaffpg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767970481  161 --------------------RTRGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:pfam00413  82 pglggdihfdddetwtvgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-218 3.60e-43

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: 149.66  E-value: 3.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI-ADIMIAF------------------------ 160
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFargnhgdgypfdgpggtlahaffp 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767970481 161 -------------------RTRGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPrKYPLSQDDINGIQSIYG 218
Cdd:cd04278   82 ggiggdihfdddeqwtlgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-218 3.23e-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: 92.03  E-value: 3.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481   106 WRKYNLTYRIinYTPDMARAAvDEAIQEGLEVWSKVTPLKFTKISKGiADIMIAFRTRGFNLFL---------------- 169
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCTLshagrpggdqhlslgn 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767970481   170 ------VAAHEFGHALGLSHS---NDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:smart00235  81 gcintgVAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.23e-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: 55.21  E-value: 4.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970481   26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 156-217 9.50e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767970481 156 IMIAFRTRGFNLFLVAA--HEFGHALGL-SHSNDQTALMFPNYVSLDPrkyPLSQDDINGIQSIY 217
Cdd:COG5549  169 FTILLSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-378 3.47e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.77  E-value: 3.47e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767970481   333 IDAAVCDKTTrKTYFFVGIWCWRFDEmtQTMDKGFPQRVVKHFPGI 378
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-327 5.43e-05

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: 40.24  E-value: 5.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767970481  286 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTL-GFP 327
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 233-422 2.26e-65

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: 208.70  E-value: 2.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 233 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 311
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 312 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 390
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767970481 391 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 422
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-218 4.51e-56

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: 183.59  E-value: 4.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481  106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAF------------------------- 160
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFgrgdhgdgypfdgpggvlahaffpg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767970481  161 --------------------RTRGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:pfam00413  82 pglggdihfdddetwtvgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-218 3.60e-43

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: 149.66  E-value: 3.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI-ADIMIAF------------------------ 160
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFargnhgdgypfdgpggtlahaffp 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767970481 161 -------------------RTRGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPrKYPLSQDDINGIQSIYG 218
Cdd:cd04278   82 ggiggdihfdddeqwtlgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-218 3.23e-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: 92.03  E-value: 3.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481   106 WRKYNLTYRIinYTPDMARAAvDEAIQEGLEVWSKVTPLKFTKISKGiADIMIAFRTRGFNLFL---------------- 169
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCTLshagrpggdqhlslgn 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767970481   170 ------VAAHEFGHALGLSHS---NDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:smart00235  81 gcintgVAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 160-218 5.94e-12

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: 63.63  E-value: 5.94e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 160 FRTRGFNLFLVAAHEFGHALGLSHSNDQ-TALMFPNYVSLDPRKYPLSQDDINGIQSIYG 218
Cdd:cd04279   97 QPRGAENLQAIALHELGHALGLWHHSDRpEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.23e-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: 55.21  E-value: 4.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970481   26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-217 1.50e-09

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: 56.74  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 108 KYNLTYRIINYTPDMARAAVDEAIQEglevWSKVTPLKFTKISKGI-ADIMI-----AFRTRGFNLFL------------ 169
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEA----WNKAFAIGFKNANDVDpADIRYsvirwIPYNDGTWSYGpsqvdpltgeil 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 170 --------------------VAAHEFGHALGLSHSN----------------DQTALMFPNYVSL-----DPRKYPLSQD 208
Cdd:cd04268   77 larvylyssfveysgarlrnTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFsiqlgDGQKYTIGPY 156


                 ....*....
gi 767970481 209 DINGIQSIY 217
Cdd:cd04268  157 DIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 156-217 9.50e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767970481 156 IMIAFRTRGFNLFLVAA--HEFGHALGL-SHSNDQTALMFPNYVSLDPrkyPLSQDDINGIQSIY 217
Cdd:COG5549  169 FTILLSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 121-217 1.04e-07

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: 51.37  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 121 DMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI--ADIMI--------------AFRTR-----------------GFNL 167
Cdd:cd00203   17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAIlvtrqdfdggtggwAYLGRvcdslrgvgvlqdnqsgTKEG 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970481 168 FLVAAHEFGHALGLSHSNDQTA--------------------LMFPNYVS-LDPRKYPLSQDDINGIQSIY 217
Cdd:cd00203   97 AQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSfSDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-378 3.47e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.77  E-value: 3.47e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767970481   333 IDAAVCDKTTrKTYFFVGIWCWRFDEmtQTMDKGFPQRVVKHFPGI 378
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-328 5.32e-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: 40.30  E-value: 5.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 767970481   286 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLgFPG 328
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF-FPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-327 5.43e-05

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: 40.24  E-value: 5.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767970481  286 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTL-GFP 327
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 129-218 7.56e-05

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: 43.56  E-value: 7.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 129 EAIQEGLEVWSKVTPLKFTKISKG-IADIMIAFRTRGFNL-------------------------------------FLV 170
Cdd:cd04277   37 AAARDALEAWEDVADIDFVEVSDNsGADIRFGNSSDPDGNtagyayypgsgsgtayggdiwfnssydtnsdspgsygYQT 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 171 AAHEFGHALGLSHSND----------------QTALM----FPNYVSLDPRKYP--LSQDDINGIQSIYG 218
Cdd:cd04277  117 IIHEIGHALGLEHPGDynggdpvpptyaldsrEYTVMsynsGYGNGASAGGGYPqtPMLLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 242-283 2.26e-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: 38.76  E-value: 2.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767970481   242 FDAITTFRR-EVMFFKGRHLWRIYYDITDVEF-ELIASFWPSLP 283
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-378 5.58e-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: 37.55  E-value: 5.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767970481  333 IDAAVCDKTtRKTYFFVGIWCWRFDEmtQTMDKGFPQRvVKHFPGI 378
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKL-ISDFPGL 42
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
160-196 1.80e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.17  E-value: 1.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767970481 160 FRTRgfnLFLVAAHEFGHALGLSHSNDQTALM-FPNYV 196
Cdd:COG1913  119 FLER---VLKEAVHELGHLFGLGHCPNPRCVMhFSNSL 153
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 125-183 7.76e-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: 37.74  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970481 125 AAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFR---------------------TRGFNLFL----------VAAH 173
Cdd:cd04327   19 AFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTpgdgywsyvgtdalligadapTMNLGWFTddtpdpefsrVVLH 98

                         90
                 ....*....|
gi 767970481 174 EFGHALGLSH 183
Cdd:cd04327   99 EFGHALGFIH 108
 
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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