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Conserved domains on  [gi|51831776|gb|AAU10089|]
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matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) [Homo sapiens]

Protein Classification

ZnMc_MMP and HX domain-containing protein( domain architecture ID 12021233)

protein containing domains PG_binding_1, ZnMc_MMP, FN2, and HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-660 4.53e-77

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: 244.14  E-value: 4.53e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 466 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 545
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 546 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 625
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 51831776 626 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 660
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-446 7.77e-69

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: 221.34  E-value: 7.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   278 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   358 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 51831776   436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 1.91e-24

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 96.21  E-value: 1.91e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 1.71e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.71e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 8.29e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.59  E-value: 8.29e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.84e-04

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 38.65  E-value: 4.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 51831776    70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-660 4.53e-77

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: 244.14  E-value: 4.53e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 466 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 545
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 546 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 625
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 51831776 626 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 660
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-446 7.77e-69

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: 221.34  E-value: 7.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   278 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   358 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 51831776   436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-446 2.39e-61

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: 201.66  E-value: 2.39e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 197 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 276
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 277 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 356
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 357 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 435
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                       330
                ....*....|.
gi 51831776 436 DDIKGIQELYG 446
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 1.91e-24

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 96.21  E-value: 1.91e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 1.71e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.71e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 8.29e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.59  E-value: 8.29e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 343-390 3.24e-22

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 89.67  E-value: 3.24e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 343 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 285-332 4.29e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.29e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 285 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.82e-20

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: 87.79  E-value: 1.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776    115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 51831776    195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 3.51e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.89  E-value: 3.51e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 227 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
349-390 4.29e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 80.69  E-value: 4.29e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   349 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 5.32e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 80.31  E-value: 5.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   233 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
291-332 1.34e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.34e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   291 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 568-614 2.19e-10

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: 56.10  E-value: 2.19e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 51831776    568 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 614
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 568-614 1.72e-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: 50.64  E-value: 1.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 51831776   568 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 614
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.84e-04

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 38.65  E-value: 4.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 51831776    70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-660 4.53e-77

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: 244.14  E-value: 4.53e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 466 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 545
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 546 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 625
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 51831776 626 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 660
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-446 7.77e-69

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: 221.34  E-value: 7.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   278 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776   358 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 51831776   436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-446 2.39e-61

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: 201.66  E-value: 2.39e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 197 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 276
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 277 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 356
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 357 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 435
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                       330
                ....*....|.
gi 51831776 436 DDIKGIQELYG 446
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 1.91e-24

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 96.21  E-value: 1.91e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 1.71e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.71e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 8.29e-23

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.59  E-value: 8.29e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51831776    226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 343-390 3.24e-22

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 89.67  E-value: 3.24e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 343 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 285-332 4.29e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.29e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 285 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.82e-20

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: 87.79  E-value: 1.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776    115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 51831776    195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 3.51e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.89  E-value: 3.51e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 51831776 227 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
349-390 4.29e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 80.69  E-value: 4.29e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   349 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 5.32e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 80.31  E-value: 5.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   233 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
291-332 1.34e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.34e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 51831776   291 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 568-614 2.19e-10

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: 56.10  E-value: 2.19e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 51831776    568 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 614
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 568-614 1.72e-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: 50.64  E-value: 1.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 51831776   568 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 614
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGLP 43
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 387-446 9.87e-08

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 51.69  E-value: 9.87e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51831776 387 WGFCPDQG-YSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSQDDIKGIQELYG 446
Cdd:cd04279  93 LGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 394-445 1.09e-06

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: 49.06  E-value: 1.09e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51831776 394 GYSLFLVAAHEFGHAMGLEHSQD--------------------PGALMAPI---YTYTKNFRLSQDDIKGIQELY 445
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 520-563 2.41e-06

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 44.48  E-value: 2.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 51831776   520 IDAVYEAPQEeKAVFFAGNEYWIYSASTLERGYPKPLTSL-GLPP 563
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 520-563 1.93e-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: 42.23  E-value: 1.93e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 51831776    520 IDAVYEAPqEEKAVFFAGNEYWIYSASTLERGYPKPLTSL--GLPP 563
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 364-446 5.75e-05

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 44.33  E-value: 5.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 364 TSAGRSDGKMWCATTANYDDDRKwgfcPDQGYSLFLvaaHEFGHAMGLEHSQDPGA----------------LMA----P 423
Cdd:cd04277  87 GSGTAYGGDIWFNSSYDTNSDSP----GSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgY 159

                        90       100
                ....*....|....*....|....*..
gi 51831776 424 IYTYTKNFRLSQ----DDIKGIQELYG 446
Cdd:cd04277 160 GNGASAGGGYPQtpmlLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-517 2.53e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 39.15  E-value: 2.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 51831776    475 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELP 517
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.84e-04

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 38.65  E-value: 4.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 51831776    70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 400-445 6.77e-04

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: 40.94  E-value: 6.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51831776 400 VAAHEFGHAMGLEHSQD--------------------------PGALMAPIYTYTKnfrLSQDDIKGIQELY 445
Cdd:cd04268  97 TAEHELGHALGLRHNFAasdrddnvdllaekgdtssvmdyapsNFSIQLGDGQKYT---IGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-517 6.84e-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: 6.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 51831776   475 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFwPELP 517
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 399-446 1.29e-03

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 40.48  E-value: 1.29e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51831776 399 LVAAHEFGHAMGLEHS----------QDPGALMAPIYTYTKNFRLSQDDIKGIQELYG 446
Cdd:cd04267 135 LTMAHELGHNLGAEHDggdelafecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 124-222 1.64e-03

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: 39.81  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51831776 124 ITYRIIGYTPDLD----PETVDDAFARAFQVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 197
Cdd:cd00203   3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74

                        90       100
                ....*....|....*....|....*..
gi 51831776 198 GT--GVGGDSHFDDDELWTLGEGQVVR 222
Cdd:cd00203  75 RVcdSLRGVGVLQDNQSGTKEGAQTIA 101
 
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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