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Conserved domains on  [gi|345799783|ref|XP_546547|]
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neutrophil collagenase [Canis lupus familiaris]

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
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-273 2.25e-90

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: 271.80  E-value: 2.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783  118 KWKQTNLTYRIIKYTPQLSEANVETAIQKAFQVWSNVSPLTFTKVSQGEVDIRISFVQGDHGDNSPFDGPNGILAHAFQP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345799783  198 GQGIGGDVHFDAEETWTENSSN---YNLFLVAAHEVGHSLGLSHSTDPGALMYPNYVFHDPSTYTLPQDDINGIQTIYG 273
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
287-475 4.72e-73

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: 228.74  E-value: 4.72e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 287 PTTCDPrLTFDAIATLRGEILFFKDKYFWRRHPQLPRVELNFISLFWPSLPDGIQAAYEDVDKDLVFLFKGSQYWALSGY 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 367 DIKQGYPKDISDYSFPSSVQAIDAAVYYRR--KTYFFVNDQVWRYDNQRQSMEPGYPKSIASIFPGIESTVDAVFQQNHV 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDngKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 345799783 445 FL-FFSGPRYYAFD--LGAHEVIRVGRSNR-WLNC 475
Cdd:cd00094  160 YYyFFKGDQYWRFDprSKEVRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-97 2.77e-07

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: 426277 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 345799783   42 RVVQDYLEKFYQLPrnrfQSERKNSTSVIMEKLREMQRFFGLNETGKPNQETLEMM 97
Cdd:pfam01471   6 KELQRYLARLGYYS----GPVDGYFGPATEAAVKAFQRAFGLPVDGIVGPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-273 2.25e-90

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: 271.80  E-value: 2.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783  118 KWKQTNLTYRIIKYTPQLSEANVETAIQKAFQVWSNVSPLTFTKVSQGEVDIRISFVQGDHGDNSPFDGPNGILAHAFQP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345799783  198 GQGIGGDVHFDAEETWTENSSN---YNLFLVAAHEVGHSLGLSHSTDPGALMYPNYVFHDPSTYTLPQDDINGIQTIYG 273
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
118-273 2.27e-81

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: 248.66  E-value: 2.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 118 KWKQTNLTYRIIKYTPQLSEANVETAIQKAFQVWSNVSPLTFTKV-SQGEVDIRISFVQGDHGDNSPFDGPNGILAHAFQ 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345799783 197 PGqGIGGDVHFDAEETWTENS--SNYNLFLVAAHEVGHSLGLSHSTDPGALMYPNYVFHDPStYTLPQDDINGIQTIYG 273
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
287-475 4.72e-73

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: 228.74  E-value: 4.72e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 287 PTTCDPrLTFDAIATLRGEILFFKDKYFWRRHPQLPRVELNFISLFWPSLPDGIQAAYEDVDKDLVFLFKGSQYWALSGY 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 367 DIKQGYPKDISDYSFPSSVQAIDAAVYYRR--KTYFFVNDQVWRYDNQRQSMEPGYPKSIASIFPGIESTVDAVFQQNHV 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDngKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 345799783 445 FL-FFSGPRYYAFD--LGAHEVIRVGRSNR-WLNC 475
Cdd:cd00094  160 YYyFFKGDQYWRFDprSKEVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
115-274 5.13e-34

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: 124.77  E-value: 5.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783   115 GNPKWKQTNLTYRIikYTPQLSEANVEtAIQKAFQVWSNVSPLTFTKVSQGEvDIRISFVQGDHGdnsPFdgpngiLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTA-DIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783   195 FQPGqgigGDVHFDaEETWTENSSnynlflVAAHEVGHSLGLSHSTDPGA---LMYPNYVFHDPSTYTLPQDDINGIQTI 271
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ...
gi 345799783   272 YGP 274
Cdd:smart00235 137 YGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
388-433 1.89e-11

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: 58.79  E-value: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 345799783   388 IDAAVYYRR-KTYFFVNDQVWRYDNQRqsMEPGYPKSIASIFPGIES 433
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
388-433 2.21e-09

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: 52.95  E-value: 2.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 345799783  388 IDAAVYYRR-KTYFFVNDQVWRYDNQRqsMEPGYPKSIASiFPGIES 433
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-97 2.77e-07

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: 426277 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 345799783   42 RVVQDYLEKFYQLPrnrfQSERKNSTSVIMEKLREMQRFFGLNETGKPNQETLEMM 97
Cdd:pfam01471   6 KELQRYLARLGYYS----GPVDGYFGPATEAAVKAFQRAFGLPVDGIVGPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-273 2.25e-90

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: 271.80  E-value: 2.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783  118 KWKQTNLTYRIIKYTPQLSEANVETAIQKAFQVWSNVSPLTFTKVSQGEVDIRISFVQGDHGDNSPFDGPNGILAHAFQP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345799783  198 GQGIGGDVHFDAEETWTENSSN---YNLFLVAAHEVGHSLGLSHSTDPGALMYPNYVFHDPSTYTLPQDDINGIQTIYG 273
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
118-273 2.27e-81

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: 248.66  E-value: 2.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 118 KWKQTNLTYRIIKYTPQLSEANVETAIQKAFQVWSNVSPLTFTKV-SQGEVDIRISFVQGDHGDNSPFDGPNGILAHAFQ 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345799783 197 PGqGIGGDVHFDAEETWTENS--SNYNLFLVAAHEVGHSLGLSHSTDPGALMYPNYVFHDPStYTLPQDDINGIQTIYG 273
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
287-475 4.72e-73

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: 228.74  E-value: 4.72e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 287 PTTCDPrLTFDAIATLRGEILFFKDKYFWRRHPQLPRVELNFISLFWPSLPDGIQAAYEDVDKDLVFLFKGSQYWALSGY 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 367 DIKQGYPKDISDYSFPSSVQAIDAAVYYRR--KTYFFVNDQVWRYDNQRQSMEPGYPKSIASIFPGIESTVDAVFQQNHV 444
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDngKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 345799783 445 FL-FFSGPRYYAFD--LGAHEVIRVGRSNR-WLNC 475
Cdd:cd00094  160 YYyFFKGDQYWRFDprSKEVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
115-274 5.13e-34

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: 124.77  E-value: 5.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783   115 GNPKWKQTNLTYRIikYTPQLSEANVEtAIQKAFQVWSNVSPLTFTKVSQGEvDIRISFVQGDHGdnsPFdgpngiLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTA-DIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783   195 FQPGqgigGDVHFDaEETWTENSSnynlflVAAHEVGHSLGLSHSTDPGA---LMYPNYVFHDPSTYTLPQDDINGIQTI 271
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ...
gi 345799783   272 YGP 274
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
142-273 1.15e-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: 77.11  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 142 TAIQKAFQVWSNVSPLTFtkVSQGEV----DIRISFVQGDHGDNSPfdgpnGILAHAFQPGQGIGGDV---HFDAEETWT 214
Cdd:cd04279   24 QAVKQAAAEWENVGPLKF--VYNPEEdndaDIVIFFDRPPPVGGAG-----GGLARAGFPLISDGNRKlfnRTDINLGPG 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 215 ENSSNYNLFLVAAHEVGHSLGLSHSTD-PGALMYPNYVFHDPSTYTLPQDDINGIQTIYG 273
Cdd:cd04279   97 QPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
143-273 8.67e-16

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: 75.53  E-value: 8.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 143 AIQKAFQVWSNVSPLTFTKVSQGEV-DIRIsfvqgdhGDNSPFDGPNGilAHAFQPG----QGIGGDVHFDAEETWTENS 217
Cdd:cd04277   38 AARDALEAWEDVADIDFVEVSDNSGaDIRF-------GNSSDPDGNTA--GYAYYPGsgsgTAYGGDIWFNSSYDTNSDS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 218 -SNYNlFLVAAHEVGHSLGLSHSTDPGA----------------LM--------YPNYVFHDPSTYTLpqDDINGIQTIY 272
Cdd:cd04277  109 pGSYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgygnGASAGGGYPQTPML--LDIAALQYLY 185

                 .
gi 345799783 273 G 273
Cdd:cd04277  186 G 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
138-272 1.18e-12

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: 66.01  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 138 ANVETAIQKAFQVWSNVSPLTFTKVSQGE--VDIRISFVQGDHgdnspfdgPNGILAHAFQPG--QGIGGDVHFDAEETW 213
Cdd:cd00203   21 AQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGVGVLQDNQSG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 214 tenssNYNLFLVAAHEVGHSLGLSHS--------------------TDPGALMYPNYV-FHDPSTYTLPQDDINGIQTIY 272
Cdd:cd00203   93 -----TKEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGsFSDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
388-433 1.89e-11

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: 58.79  E-value: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 345799783   388 IDAAVYYRR-KTYFFVNDQVWRYDNQRqsMEPGYPKSIASIFPGIES 433
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
143-272 1.10e-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: 60.20  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 143 AIQKAFQVWSNVSPLTFTKVSQGEV-DIRISFVQgdhgDNSPFDGPNGILAHAFQPGQG--IGGDVHFDAEETWTENSSN 219
Cdd:cd04268   19 AILDAIEAWNKAFAIGFKNANDVDPaDIRYSVIR----WIPYNDGTWSYGPSQVDPLTGeiLLARVYLYSSFVEYSGARL 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345799783 220 YNlflVAAHEVGHSLGLSHS----------------TDPGALMYP-----NYVFHDPSTYTLPQDDINGIQTIY 272
Cdd:cd04268   95 RN---TAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYapsnfSIQLGDGQKYTIGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
388-433 2.21e-09

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: 52.95  E-value: 2.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 345799783  388 IDAAVYYRR-KTYFFVNDQVWRYDNQRqsMEPGYPKSIASiFPGIES 433
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-97 2.77e-07

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: 426277 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 345799783   42 RVVQDYLEKFYQLPrnrfQSERKNSTSVIMEKLREMQRFFGLNETGKPNQETLEMM 97
Cdd:pfam01471   6 KELQRYLARLGYYS----GPVDGYFGPATEAAVKAFQRAFGLPVDGIVGPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
340-383 1.13e-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: 1.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 345799783  340 IQAAYEDvDKDLVFLFKGSQYWALSGYDIKQGYPKDISDY-SFPS 383
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
296-337 5.40e-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: 43.39  E-value: 5.40e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 345799783   296 FDAIATLR-GEILFFKDKYFWRRHPQ-LPRVELNFISLFWPSLP 337
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
340-379 7.91e-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: 42.61  E-value: 7.91e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 345799783   340 IQAAYEDvDKDLVFLFKGSQYWALSGYDIKQGYPKDISDY 379
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF 39
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
146-278 1.62e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.49  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783  146 KAFQVWSNVSPLTFTKVSQGEVDIRISFVQ------GDHGDN-----SPFDGPNGILAHAFQP-GQGIGGDVHFDAEETw 213
Cdd:pfam13688  50 VNLTISDSTCPYTPPACSTGDSSDRLSEFQdfsawrGTQNDDlaylfLMTNCSGGGLAWLGQLcNSGSAGSVSTRVSGN- 128
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345799783  214 TENSSNYNLFLVAAHEVGHSLGLSHstDPGALMYPNYVFhdPSTYTLPqddiNGIQTIYGPSSNP 278
Cdd:pfam13688 129 NVVVSTATEWQVFAHEIGHNFGAVH--DCDSSTSSQCCP--PSNSTCP----AGGRYIMNPSSSP 185
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
136-238 2.67e-05

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: 45.06  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 136 SEANVETAIQKAFQVWSNVSPLTFTKVSQGEVDIRISFVQGDhgDNSPFDGPNGILAHAFQPGQGIGGDvhfdaeetwTE 215
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWF---------TD 85
                         90       100
                 ....*....|....*....|...
gi 345799783 216 NSSNYNLFLVAAHEVGHSLGLSH 238
Cdd:cd04327   86 DTPDPEFSRVVLHEFGHALGFIH 108
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
296-337 5.53e-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: 5.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 345799783  296 FDAIATLR-GEILFFKDKYFWRRHPQ-LPRVELNFISLFwPSLP 337
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQrVEPGYPKLISDF-PGLP 43
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
215-264 1.46e-03

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 40.03  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 345799783 215 ENSSNYNLFLVAAHEVGHSLGLSHSTDPGalmyPNYVFHDPSTYTLPQDD 264
Cdd:cd04272  138 DTPGSYYGVYTMTHELAHLLGAPHDGSPP----PSWVKGHPGSLDCPWDD 183
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
218-248 1.91e-03

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: 39.20  E-value: 1.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 345799783 218 SNYNLFL-----VAAHEVGHSLGLSHSTDPGALMYP 248
Cdd:cd11375  114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
168-258 2.37e-03

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


Pssm-ID: 239803  Cd Length: 197  Bit Score: 39.23  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345799783 168 DIRISFVQGDHGDNspfdGPNGILAHAFQP--GQGIGGDVHFDAeeTWTENSSN-YNLFL------VAAHEVGHSLGLSH 238
Cdd:cd04276   59 DIRYNVIRWIHSPN----GGWAYGPSVVDPrtGEILKADVILYS--GFLRQDQLwYEDLLaaslryLLAHEVGHTLGLRH 132
                         90       100
                 ....*....|....*....|
gi 345799783 239 STdPGALMYPNYVFHDPSTY 258
Cdd:cd04276  133 NF-KASSDGSNEELEDPLGT 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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