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Conserved domains on  [gi|700274115|ref|NP_001289439|]
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72 kDa type IV collagenase isoform 3 [Homo sapiens]

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 11995240)

M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases 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
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 390-584 2.88e-76

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: 240.29  E-value: 2.88e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 390 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 469
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 470 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 549
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 700274115 550 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 584
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 42-370 2.91e-68

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: 218.26  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115   42 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  122 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 201
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  202 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 281
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  282 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 359
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 700274115  360 DDIKGIQELYG 370
Cdd:pfam00413 149 DDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 266-314 4.07e-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: 95.06  E-value: 4.07e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   266 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 208-256 3.60e-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: 92.36  E-value: 3.60e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   208 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 150-198 1.69e-22

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: 90.44  E-value: 1.69e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   150 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 390-584 2.88e-76

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: 240.29  E-value: 2.88e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 390 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 469
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 470 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 549
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 700274115 550 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 584
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 42-370 2.91e-68

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: 218.26  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115   42 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  122 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 201
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  202 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 281
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  282 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 359
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 700274115  360 DDIKGIQELYG 370
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 42-370 8.91e-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: 198.58  E-value: 8.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  42 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 120
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 121 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 200
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 201 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 280
Cdd:cd04278      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 281 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 359
Cdd:cd04278  102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                        330
                 ....*....|.
gi 700274115 360 DDIKGIQELYG 370
Cdd:cd04278  147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 266-314 4.07e-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: 95.06  E-value: 4.07e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   266 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 208-256 3.60e-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: 92.36  E-value: 3.60e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   208 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 150-198 1.69e-22

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: 90.44  E-value: 1.69e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   150 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 267-314 6.32e-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: 88.90  E-value: 6.32e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 267 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 209-256 8.22e-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: 85.82  E-value: 8.22e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 209 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 151-198 6.50e-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: 83.12  E-value: 6.50e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 151 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 39-142 6.74e-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: 86.25  E-value: 6.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115    39 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 118
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 700274115   119 FAPgtgvGGDSHFdDDELWTLGEG 142
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
fn2 pfam00040
Fibronectin type II domain;
273-314 7.73e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 7.73e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  273 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
157-198 9.12e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.54  E-value: 9.12e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  157 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
215-256 2.39e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.38  E-value: 2.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  215 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 492-538 4.90e-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: 54.94  E-value: 4.90e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 700274115   492 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 538
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 492-538 3.75e-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: 49.49  E-value: 3.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 700274115  492 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 538
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGLP 43
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 390-584 2.88e-76

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: 240.29  E-value: 2.88e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 390 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 469
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 470 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 549
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 700274115 550 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 584
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 42-370 2.91e-68

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: 218.26  E-value: 2.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115   42 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  122 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 201
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  202 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 281
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  282 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 359
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
gi 700274115  360 DDIKGIQELYG 370
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 42-370 8.91e-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: 198.58  E-value: 8.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  42 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 120
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 121 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 200
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 201 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 280
Cdd:cd04278      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 281 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 359
Cdd:cd04278  102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                        330
                 ....*....|.
gi 700274115 360 DDIKGIQELYG 370
Cdd:cd04278  147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 266-314 4.07e-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: 95.06  E-value: 4.07e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   266 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 208-256 3.60e-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: 92.36  E-value: 3.60e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   208 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 150-198 1.69e-22

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: 90.44  E-value: 1.69e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 700274115   150 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 267-314 6.32e-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: 88.90  E-value: 6.32e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 267 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 209-256 8.22e-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: 85.82  E-value: 8.22e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 209 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 151-198 6.50e-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: 83.12  E-value: 6.50e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 700274115 151 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 39-142 6.74e-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: 86.25  E-value: 6.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115    39 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 118
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 700274115   119 FAPgtgvGGDSHFdDDELWTLGEG 142
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
fn2 pfam00040
Fibronectin type II domain;
273-314 7.73e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 7.73e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  273 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 314
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
157-198 9.12e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.54  E-value: 9.12e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  157 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 198
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
215-256 2.39e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.38  E-value: 2.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 700274115  215 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 256
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 492-538 4.90e-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: 54.94  E-value: 4.90e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 700274115   492 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 538
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 492-538 3.75e-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: 49.49  E-value: 3.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 700274115  492 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 538
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 ...
 311-370 1.53e-07

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: 51.30  E-value: 1.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700274115 311 WGFCPDQG-YSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSQDDIKGIQELYG 370
Cdd:cd04279   93 LGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 318-369 1.62e-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: 48.29  E-value: 1.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 700274115 318 GYSLFLVAAHEFGHAMGLEHSQD--------------------PGALMAPI---YTYTKNFRLSQDDIKGIQELY 369
Cdd:cd00203   93 TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 444-487 4.44e-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: 43.71  E-value: 4.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 700274115  444 IDAVYEAPQEeKAVFFAGNEYWIYSASTLERGYPKPLTSL-GLPP 487
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 444-487 3.53e-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: 41.07  E-value: 3.53e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 700274115   444 IDAVYEAPqEEKAVFFAGNEYWIYSASTLERGYPKPLTSL--GLPP 487
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 288-370 1.45e-04

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 43.17  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115 288 TSAGRSDGKMWCATTANYDDDRKwgfcPDQGYSLFLvaaHEFGHAMGLEHSQDPGA----------------LMA----P 347
Cdd:cd04277   87 GSGTAYGGDIWFNSSYDTNSDSP----GSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgY 159

                         90       100
                 ....*....|....*....|....*..
gi 700274115 348 IYTYTKNFRLSQ----DDIKGIQELYG 370
Cdd:cd04277  160 GNGASAGGGYPQtpmlLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 399-441 4.29e-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: 37.99  E-value: 4.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 700274115   399 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELP 441
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 324-369 9.94e-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: 40.17  E-value: 9.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700274115 324 VAAHEFGHAMGLEHSQD--------------------------PGALMAPIYTYTKnfrLSQDDIKGIQELY 369
Cdd:cd04268   97 TAEHELGHALGLRHNFAasdrddnvdllaekgdtssvmdyapsNFSIQLGDGQKYT---IGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 399-441 1.10e-03

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: 37.16  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 700274115  399 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFwPELP 441
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 323-370 1.11e-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: 1.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 700274115 323 LVAAHEFGHAMGLEHS----------QDPGALMAPIYTYTKNFRLSQDDIKGIQELYG 370
Cdd:cd04267  135 LTMAHELGHNLGAEHDggdelafecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 48-146 2.29e-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: 39.04  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274115  48 ITYRIIGYTPDLD----PETVDDAFARAFQVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 121
Cdd:cd00203    3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74

                         90       100
                 ....*....|....*....|....*..
gi 700274115 122 GT--GVGGDSHFDDDELWTLGEGQVVR 146
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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