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Conserved domains on  [gi|58331148|ref|NP_005931|]
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stromelysin-3 preproprotein [Homo sapiens]

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 ...
 104-258 1.66e-75

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: 234.43  E-value: 1.66e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148   104 RWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFP 183
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331148   184 KTHREGDVHFDYDETWTIGDD--QGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYP--LSLSPDDCRGVQHLYG 258
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.33e-69

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: 218.72  E-value: 6.33e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 291 PDACEA-SFDAVSTIRGELFFFKAGFVWRLRGGqLQPGYPALASRHWQGLPSPVDAAFEDAQ-GHIWFFQGAQYWVYDGE 368
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 369 -KPVLGPAPLTELGLVR--FPVHAALVWGPEKnKIYFFRGRDYWRFHPSTRRVDSPVPRR-ATDWRGVPSEIDAAFQDAD 444
Cdd:cd00094  80 nLEPGYPKPISDLGFPPtvKQIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 58331148 445 GYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGC 480
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
2-86 8.08e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    2 APAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPwhaALPSSPAPAPATQEAPRPASSLRPPRCG 81
Cdd:PRK12323 400 AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP---APAPAPAAAPAAAARPAAAGPRPVAAAA 476


                 ....*
gi 58331148   82 VPDPS 86
Cdd:PRK12323 477 AAAPA 481
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 104-258 1.66e-75

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: 234.43  E-value: 1.66e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148   104 RWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFP 183
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331148   184 KTHREGDVHFDYDETWTIGDD--QGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYP--LSLSPDDCRGVQHLYG 258
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 104-258 1.01e-72

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: 227.09  E-value: 1.01e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 104 RWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEG-RADIMIDFARYWHGDDLPFDGPGGILAHAFF 182
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331148 183 PKTHReGDVHFDYDETWTIGDDQ-GTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPL-SLSPDDCRGVQHLYG 258
Cdd:cd04278  81 PGGIG-GDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.33e-69

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: 218.72  E-value: 6.33e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 291 PDACEA-SFDAVSTIRGELFFFKAGFVWRLRGGqLQPGYPALASRHWQGLPSPVDAAFEDAQ-GHIWFFQGAQYWVYDGE 368
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 369 -KPVLGPAPLTELGLVR--FPVHAALVWGPEKnKIYFFRGRDYWRFHPSTRRVDSPVPRR-ATDWRGVPSEIDAAFQDAD 444
Cdd:cd00094  80 nLEPGYPKPISDLGFPPtvKQIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 58331148 445 GYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGC 480
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-259 1.08e-30

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: 115.91  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    104 RWEKTDLTYRIlrFPWQLVQEQvRQTMAEALKVWSDVTPLTFTEVHEGrADIMIDFARYWHGddlPFdgpggiLAHAFFP 183
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    184 KthreGDVHFDyDETWTIGDDqgtdllqVAAHEFGHVLGLQHTTAAKA---LMSAFYTF--RYPLSLSPDDCRGVQHLYG 258
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138


                   .
gi 58331148    259 Q 259
Cdd:smart00235 139 S 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 298-341 1.66e-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: 1.66e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 58331148    298 FDAVSTIR-GELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPS 341
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 298-341 7.34e-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: 48.72  E-value: 7.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 58331148   298 FDAVSTIR-GELFFFKAGFVWRLRGGQLQPGYPALASrHWQGLPS 341
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-86 8.08e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    2 APAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPwhaALPSSPAPAPATQEAPRPASSLRPPRCG 81
Cdd:PRK12323 400 AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP---APAPAPAAAPAAAARPAAAGPRPVAAAA 476


                 ....*
gi 58331148   82 VPDPS 86
Cdd:PRK12323 477 AAAPA 481
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 104-258 1.66e-75

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: 234.43  E-value: 1.66e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148   104 RWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFP 183
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331148   184 KTHREGDVHFDYDETWTIGDD--QGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYP--LSLSPDDCRGVQHLYG 258
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 104-258 1.01e-72

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: 227.09  E-value: 1.01e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 104 RWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEG-RADIMIDFARYWHGDDLPFDGPGGILAHAFF 182
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331148 183 PKTHReGDVHFDYDETWTIGDDQ-GTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPL-SLSPDDCRGVQHLYG 258
Cdd:cd04278  81 PGGIG-GDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.33e-69

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: 218.72  E-value: 6.33e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 291 PDACEA-SFDAVSTIRGELFFFKAGFVWRLRGGqLQPGYPALASRHWQGLPSPVDAAFEDAQ-GHIWFFQGAQYWVYDGE 368
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 369 -KPVLGPAPLTELGLVR--FPVHAALVWGPEKnKIYFFRGRDYWRFHPSTRRVDSPVPRR-ATDWRGVPSEIDAAFQDAD 444
Cdd:cd00094  80 nLEPGYPKPISDLGFPPtvKQIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 58331148 445 GYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGC 480
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-259 1.08e-30

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: 115.91  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    104 RWEKTDLTYRIlrFPWQLVQEQvRQTMAEALKVWSDVTPLTFTEVHEGrADIMIDFARYWHGddlPFdgpggiLAHAFFP 183
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    184 KthreGDVHFDyDETWTIGDDqgtdllqVAAHEFGHVLGLQHTTAAKA---LMSAFYTF--RYPLSLSPDDCRGVQHLYG 258
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138


                   .
gi 58331148    259 Q 259
Cdd:smart00235 139 S 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 117-258 1.50e-12

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: 65.90  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 117 FPWQLVQEQVRQTMAEALKVWSDVTPLTFTEV-HEGRADIMIDFarywhgDDLPFDGPGGIlahAFFPK----THREGDV 191
Cdd:cd04277  26 TNTAALSAAQQAAARDALEAWEDVADIDFVEVsDNSGADIRFGN------SSDPDGNTAGY---AYYPGsgsgTAYGGDI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 192 HFDYDETWTiGDDQGTDLLQVAAHEFGHVLGLQH-----------TTAAKA-----LMS--------AFYTFRYPLSLSP 247
Cdd:cd04277  97 WFNSSYDTN-SDSPGSYGYQTIIHEIGHALGLEHpgdynggdpvpPTYALDsreytVMSynsgygngASAGGGYPQTPML 175

                       170
                ....*....|.
gi 58331148 248 DDCRGVQHLYG 258
Cdd:cd04277 176 LDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 123-258 2.38e-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: 64.79  E-value: 2.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 123 QEQVRQTMAEALKVWSDVTPLTFteVHEGRADIMIDFARYWhGDDLPFDGPGGILAHAFFPKTHREGDVHFD-YDETWTI 201
Cdd:cd04279  19 AQSWLQAVKQAAAEWENVGPLKF--VYNPEEDNDADIVIFF-DRPPPVGGAGGGLARAGFPLISDGNRKLFNrTDINLGP 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58331148 202 GDDQG-TDLLQVAAHEFGHVLGLQHTTAAKALMSAF---YTFRYPLSLSPDDCRGVQHLYG 258
Cdd:cd04279  96 GQPRGaENLQAIALHELGHALGLWHHSDRPEDAMYPsqgQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 123-257 1.08e-11

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: 63.31  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 123 QEQVRQTMAEALKVWSDVTPLTFTEVHEG--RADIMIDFARYwhgddlpfDGPGGILAHAFFPKT--HREGDVHFDYDET 198
Cdd:cd00203  20 SAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQ--------DFDGGTGGWAYLGRVcdSLRGVGVLQDNQS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 199 WTIgddqgtDLLQVAAHEFGHVLGLQH--------------------TTAAKALMSAFYTFR---YPLSLSPDDCRGVQH 255
Cdd:cd00203  92 GTK------EGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTKGSFsdgQRKDFSQCDIDQINK 165


                ..
gi 58331148 256 LY 257
Cdd:cd00203 166 LY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 107-231 3.01e-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: 55.97  E-value: 3.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148 107 KTDLTYRILRfpwqLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGR-ADIMIDFARYWHGDDlpfdGPGGILAHAFFPKT 185
Cdd:cd04268   1 KKPITYYIDD----SVPDKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYND----GTWSYGPSQVDPLT 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58331148 186 H--REGDVHFDYDETWTIGDDqgtdLLQVAAHEFGHVLGLQHTTAAKA 231
Cdd:cd04268  73 GeiLLARVYLYSSFVEYSGAR----LRNTAEHELGHALGLRHNFAASD 116
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 298-341 1.66e-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: 1.66e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 58331148    298 FDAVSTIR-GELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPS 341
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 298-341 7.34e-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: 48.72  E-value: 7.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 58331148   298 FDAVSTIR-GELFFFKAGFVWRLRGGQLQPGYPALASrHWQGLPS 341
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 1.01e-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: 48.33  E-value: 1.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 58331148   387 VHAALVWGPekNKIYFFRGRDYWRFHPstRRVDSPVPRRATDWRGVPS 434
Cdd:pfam00045   1 IDAAFEDRD--GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 436-479 1.83e-07

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.62  E-value: 1.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 58331148    436 IDAAFQDADGYAYFLRGRLYWKFDPVKVKalEGFPRLVGPDFFG 479
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVD--PGYPKLISSFFPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 436-480 3.66e-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: 46.41  E-value: 3.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 58331148   436 IDAAFQDADGYAYFLRGRLYWKFDPVKVkaLEGFPRLVGPD-FFGC 480
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRV--EPGYPKLISDFpGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 343-380 7.87e-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: 45.64  E-value: 7.87e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 58331148   343 VDAAFEDAQGHIWFFQGAQYWVYDGEKPVLG-PAPLTEL 380
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGyPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 2.16e-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: 2.16e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 58331148    387 VHAALVWgpEKNKIYFFRGRDYWRFHPstRRVDSPVPRR-ATDWRGVPS 434
Cdd:smart00120   1 IDAAFEL--RDGKTYFFKGDKYWRFDP--KRVDPGYPKLiSSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 343-373 2.26e-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: 2.26e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 58331148    343 VDAAFEDAQGHIWFFQGAQYWVYDGEKPVLG 373
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPG 31
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-86 8.08e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331148    2 APAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPwhaALPSSPAPAPATQEAPRPASSLRPPRCG 81
Cdd:PRK12323 400 AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP---APAPAPAAAPAAAARPAAAGPRPVAAAA 476


                 ....*
gi 58331148   82 VPDPS 86
Cdd:PRK12323 477 AAAPA 481
 
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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