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Conserved domains on  [gi|398650618|ref|NP_037112|]
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stromelysin-3 precursor [Rattus norvegicus]

Protein Classification

M10A family metallopeptidase( domain architecture ID 11995186)

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
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-261 3.66e-79

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: 243.68  E-value: 3.66e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618  108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650618  188 KTHREGDVHFDYDETWTIGDK---GTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 294-483 1.85e-66

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: 212.17  E-value: 1.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 294 PEVCET-SFDAVSTIRGELFFFKAGFVWRLrSGQLQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 371
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL-SPGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 372 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRRT-TDWRGVPSEIDAAFQDAE 447
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398650618 448 GYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDC 483
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-261 3.66e-79

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: 243.68  E-value: 3.66e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618  108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650618  188 KTHREGDVHFDYDETWTIGDK---GTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-261 1.29e-76

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: 237.10  E-value: 1.29e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEG-RADIMIDFTRYWHGDNLPFDGPGGILAHAFF 186
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398650618 187 PKTHReGDVHFDYDETWTIGD--KGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPL-SLSPDDRRGIQHLYG 261
Cdd:cd04278   81 PGGIG-GDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 294-483 1.85e-66

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: 212.17  E-value: 1.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 294 PEVCET-SFDAVSTIRGELFFFKAGFVWRLrSGQLQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 371
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL-SPGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 372 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRRT-TDWRGVPSEIDAAFQDAE 447
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398650618 448 GYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDC 483
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 108-261 6.38e-32

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: 118.99  E-value: 6.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618   108 RWEKTDLTYRIlrFPWQLVREQvRQTVAEALRVWSEVTPLTFTEVHEGrADIMIDFTRYWHGdnlPFdgpggiLAHAFFP 187
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650618   188 KthreGDVHFDyDETWTIGDkgtdllQVAAHEFGHVLGLQHTTAAKA---LMSPFYTF--RYPLSLSPDDRRGIQHLYG 261
Cdd:smart00235  71 G----GDQHLS-LGNGCINT------GVAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 1.91e-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: 50.32  E-value: 1.91e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 398650618   301 FDAVSTIR-GELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPS 344
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 7.54e-08

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: 48.33  E-value: 7.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 398650618  301 FDAVSTIR-GELFFFKAGFVWRLRSGQLQPGYPALASrHWQGLPS 344
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
212-255 5.19e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 398650618 212 LLQVAAHEFGHVLGLQHTTAAKALMspfytfRYPLSLSPDDRRG 255
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVM------HFSNSLEELDRKP 160
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-261 3.66e-79

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: 243.68  E-value: 3.66e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618  108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650618  188 KTHREGDVHFDYDETWTIGDK---GTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-261 1.29e-76

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: 237.10  E-value: 1.29e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEG-RADIMIDFTRYWHGDNLPFDGPGGILAHAFF 186
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398650618 187 PKTHReGDVHFDYDETWTIGD--KGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPL-SLSPDDRRGIQHLYG 261
Cdd:cd04278   81 PGGIG-GDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 294-483 1.85e-66

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: 212.17  E-value: 1.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 294 PEVCET-SFDAVSTIRGELFFFKAGFVWRLrSGQLQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 371
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL-SPGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 372 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRRT-TDWRGVPSEIDAAFQDAE 447
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398650618 448 GYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDC 483
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 108-261 6.38e-32

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: 118.99  E-value: 6.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618   108 RWEKTDLTYRIlrFPWQLVREQvRQTVAEALRVWSEVTPLTFTEVHEGrADIMIDFTRYWHGdnlPFdgpggiLAHAFFP 187
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650618   188 KthreGDVHFDyDETWTIGDkgtdllQVAAHEFGHVLGLQHTTAAKA---LMSPFYTF--RYPLSLSPDDRRGIQHLYG 261
Cdd:smart00235  71 G----GDQHLS-LGNGCINT------GVAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 129-261 3.54e-16

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: 75.57  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 129 QVRQTVAEALRVWSEVTPLTF--TEVHEGRADIMIDFTRYWHGDNLpfdgpGGILAHAFFPKTHREGDV---HFDYDETW 203
Cdd:cd04279   21 SWLQAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKlfnRTDINLGP 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398650618 204 TIGDKGTDLLQVAAHEFGHVLGLQHTTAAKA-LMSPFY--TFRYPLSLSPDDRRGIQHLYG 261
Cdd:cd04279   96 GQPRGAENLQAIALHELGHALGLWHHSDRPEdAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 121-261 3.57e-14

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 70.91  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 121 FPWQLVREQVRQTVAEALRVWSEVTPLTFTEV-HEGRADIMIDFTrywhgdnlpFDGPGGILAHAFFPK----THREGDV 195
Cdd:cd04277   26 TNTAALSAAQQAAARDALEAWEDVADIDFVEVsDNSGADIRFGNS---------SDPDGNTAGYAYYPGsgsgTAYGGDI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 196 HFDYDETWTIGDKGTDLLQVAAHEFGHVLGLQH-----------TTAAKA-----LMS--------PFYTFRYPLSLSPD 251
Cdd:cd04277   97 WFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHpgdynggdpvpPTYALDsreytVMSynsgygngASAGGGYPQTPMLL 176

                        170
                 ....*....|
gi 398650618 252 DRRGIQHLYG 261
Cdd:cd04277  177 DIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 127-260 1.39e-13

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: 68.70  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 127 REQVRQTVAEALRVWSEVTPLTFTEVHEG--RADIMIDFTRYwhgdnlpfDGPGGILAHAFFPKT--HREGDVHFDYDET 202
Cdd:cd00203   20 SAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQ--------DFDGGTGGWAYLGRVcdSLRGVGVLQDNQS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 203 WTIgdkgtDLLQVAAHEFGHVLGLQH--------------------TTAAKALMSPFYTFR---YPLSLSPDDRRGIQHL 259
Cdd:cd00203   92 GTK-----EGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTKGSFsdgQRKDFSQCDIDQINKL 166


                 .
gi 398650618 260 Y 260
Cdd:cd00203  167 Y 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 111-260 1.96e-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: 59.43  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 111 KTDLTYRILR-FPwqlvrEQVRQTVAEALRVWSEVTPLTFTEVHEGR-ADIMIDFTRYWHGDnlpfDGPGGILAHAFFPK 188
Cdd:cd04268    1 KKPITYYIDDsVP-----DKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650618 189 ThreGDVHFD--YDETWTIGDKGTDLLQVAAHEFGHVLGLQHTTAAKAL----------------M-------SPFYTFR 243
Cdd:cd04268   72 T---GEILLArvYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRddnvdllaekgdtssvMdyapsnfSIQLGDG 148

                        170
                 ....*....|....*..
gi 398650618 244 YPLSLSPDDRRGIQHLY 260
Cdd:cd04268  149 QKYTIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 1.91e-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: 50.32  E-value: 1.91e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 398650618   301 FDAVSTIR-GELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPS 344
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 7.54e-08

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: 48.33  E-value: 7.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 398650618  301 FDAVSTIR-GELFFFKAGFVWRLRSGQLQPGYPALASrHWQGLPS 344
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 390-437 2.57e-07

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: 47.18  E-value: 2.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 398650618  390 VHAALVWGPekNKIYFFRGGDYWRFHPrtQRVDNPVPRRTTDWRGVPS 437
Cdd:pfam00045   1 IDAAFEDRD--GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-383 1.02e-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: 45.25  E-value: 1.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 398650618  346 VDAAFEDAQGQIWFFQGAQYWVYDGEKPVLG-PAPLSKL 383
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGyPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-481 1.77e-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: 44.54  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 398650618   439 IDAAFQDAEGYAYFLRGHLYWKFDPVKVKvlESFPRPIGPDFF 481
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVD--PGYPKLISSFFP 41
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 390-437 4.08e-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: 4.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 398650618   390 VHAALVWgpEKNKIYFFRGGDYWRFHPrtQRVDNPVPRR-TTDWRGVPS 437
Cdd:smart00120   1 IDAAFEL--RDGKTYFFKGDKYWRFDP--KRVDPGYPKLiSSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-383 2.30e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 41.46  E-value: 2.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 398650618   346 VDAAFEDAQGQIWFFQGAQYWVYDGEKPVLG-PAPLSKL 383
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGyPKLISSF 39
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-476 2.77e-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: 41.40  E-value: 2.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 398650618  439 IDAAFQDAEGYAYFLRGHLYWKFDPvkVKVLESFPRPI 476
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDP--QRVEPGYPKLI 36
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
212-255 5.19e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 398650618 212 LLQVAAHEFGHVLGLQHTTAAKALMspfytfRYPLSLSPDDRRG 255
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVM------HFSNSLEELDRKP 160
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 212-241 8.68e-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: 37.69  E-value: 8.68e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 398650618 212 LLQVAAHEFGHVLGLQHTTAAKALMSPFYT 241
Cdd:cd04276  116 LRYLLAHEVGHTLGLRHNFKASSDGSNEEL 145
 
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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