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Conserved domains on  [gi|568956296|ref|XP_006530814|]
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72 kDa type IV collagenase isoform X1 [Mus musculus]

Protein Classification

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. ...
 510-704 4.99e-78

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: 248.00  E-value: 4.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 510 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 589
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 590 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 669
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568956296 670 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 704
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 2.47e-55

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: 186.28  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296  118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 568956296  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 384-432 2.56e-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: 95.83  E-value: 2.56e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   384 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 326-374 1.30e-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: 93.90  E-value: 1.30e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   326 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.06e-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: 2.06e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   226 GNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 408-489 1.14e-12

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: 65.83  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296   408 AGRNDGKVWcatttnYDDDRkwgFCPDQGyslflVAAHEFGHAMGLEHSQDPGA---LMAPIYTY--TKNFRLSHDDIKG 482
Cdd:smart00235  67 AGRPGGDQH------LSLGN---GCINTG-----VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLG 132


                   ....*..
gi 568956296   483 IQELYGP 489
Cdd:smart00235 133 IPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.78e-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: 4.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 568956296   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. ...
 510-704 4.99e-78

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: 248.00  E-value: 4.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 510 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 589
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 590 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 669
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568956296 670 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 704
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 2.47e-55

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: 186.28  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296  118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 568956296  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-216 8.64e-50

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: 171.23  E-value: 8.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100
                 ....*....|....*....|
gi 568956296 197 PGtGVGGDSHFDDDELWTLG 216
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG 99
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 384-432 2.56e-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: 95.83  E-value: 2.56e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   384 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 326-374 1.30e-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: 93.90  E-value: 1.30e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   326 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.06e-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: 2.06e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   226 GNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 385-432 3.27e-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: 90.06  E-value: 3.27e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 385 NSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 327-374 2.14e-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: 87.75  E-value: 2.14e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 327 NADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 9.83e-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: 82.74  E-value: 9.83e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 227 NADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.10e-19

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: 85.87  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296   115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARALKVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 568956296   195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
fn2 pfam00040
Fibronectin type II domain;
333-374 8.13e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 8.13e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  333 CKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 9.32e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  233 CKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
391-432 6.87e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 77.22  E-value: 6.87e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  391 CVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 408-489 1.14e-12

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: 65.83  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296   408 AGRNDGKVWcatttnYDDDRkwgFCPDQGyslflVAAHEFGHAMGLEHSQDPGA---LMAPIYTY--TKNFRLSHDDIKG 482
Cdd:smart00235  67 AGRPGGDQH------LSLGN---GCINTG-----VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLG 132


                   ....*..
gi 568956296   483 IQELYGP 489
Cdd:smart00235 133 IPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 612-658 4.17e-11

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 58.41  E-value: 4.17e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568956296   612 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADSWNAIP 658
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 612-654 6.37e-09

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.18  E-value: 6.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568956296  612 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADSW 654
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISDFP 40
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 429-488 7.55e-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: 49.38  E-value: 7.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956296 429 WGFCPDQG-YSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSHDDIKGIQELYG 488
Cdd:cd04279   93 LGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.78e-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: 4.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 568956296   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. ...
 510-704 4.99e-78

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: 248.00  E-value: 4.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 510 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 589
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 590 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 669
Cdd:cd00094   79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568956296 670 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 704
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 2.47e-55

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: 186.28  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296  118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 568956296  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-216 8.64e-50

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: 171.23  E-value: 8.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100
                 ....*....|....*....|
gi 568956296 197 PGtGVGGDSHFDDDELWTLG 216
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG 99
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 384-432 2.56e-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: 95.83  E-value: 2.56e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   384 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 326-374 1.30e-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: 93.90  E-value: 1.30e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   326 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.06e-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: 2.06e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568956296   226 GNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 385-432 3.27e-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: 90.06  E-value: 3.27e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 385 NSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 327-374 2.14e-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: 87.75  E-value: 2.14e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 327 NADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 9.83e-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: 82.74  E-value: 9.83e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568956296 227 NADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.10e-19

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: 85.87  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296   115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARALKVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 568956296   195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
fn2 pfam00040
Fibronectin type II domain;
333-374 8.13e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 8.13e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  333 CKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 374
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 9.32e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.32e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  233 CKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
391-432 6.87e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 77.22  E-value: 6.87e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568956296  391 CVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 432
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 408-489 1.14e-12

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: 65.83  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296   408 AGRNDGKVWcatttnYDDDRkwgFCPDQGyslflVAAHEFGHAMGLEHSQDPGA---LMAPIYTY--TKNFRLSHDDIKG 482
Cdd:smart00235  67 AGRPGGDQH------LSLGN---GCINTG-----VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLG 132


                   ....*..
gi 568956296   483 IQELYGP 489
Cdd:smart00235 133 IPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 612-658 4.17e-11

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 58.41  E-value: 4.17e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568956296   612 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADSWNAIP 658
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 612-654 6.37e-09

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.18  E-value: 6.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568956296  612 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADSW 654
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISDFP 40
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 564-607 6.07e-07

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 46.41  E-value: 6.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568956296  564 IDAVYEAPQEeKAVFFAGNEYWVYSASTLERGYPKPLTSL-GLPP 607
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 429-488 7.55e-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: 49.38  E-value: 7.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956296 429 WGFCPDQG-YSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSHDDIKGIQELYG 488
Cdd:cd04279   93 LGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 564-607 7.56e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.39  E-value: 7.56e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568956296   564 IDAVYEAPqEEKAVFFAGNEYWVYSASTLERGYPKPLTSL--GLPP 607
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 406-488 9.70e-06

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: 46.64  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 406 TSAGRNDGKVWCATTTNYDDDRKwgfcPDQGYSLFLvaaHEFGHAMGLEHSQDPGA----------------LMA----P 465
Cdd:cd04277   87 GSGTAYGGDIWFNSSYDTNSDSP----GSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgY 159

                         90       100
                 ....*....|....*....|....*..
gi 568956296 466 IYTYTKNFRLSHD----DIKGIQELYG 488
Cdd:cd04277  160 GNGASAGGGYPQTpmllDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 436-487 1.55e-05

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: 45.98  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956296 436 GYSLFLVAAHEFGHAMGLEHSQD--------------------PGALMAPI---YTYTKNFRLSHDDIKGIQELY 487
Cdd:cd00203   93 TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 519-561 9.16e-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: 40.30  E-value: 9.16e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568956296   519 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELP 561
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 4.78e-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: 4.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 568956296   70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 519-561 1.32e-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: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568956296  519 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPTGPLLVATFwPELP 561
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 124-222 2.76e-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: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956296 124 ITYRIIGYTPDLD----PETVDDAFARALKVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 197
Cdd:cd00203    3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74

                         90       100
                 ....*....|....*....|....*..
gi 568956296 198 GT--GVGGDSHFDDDELWTLGEGQVVR 222
Cdd:cd00203   75 RVcdSLRGVGVLQDNQSGTKEGAQTIA 101
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 442-487 5.05e-03

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: 38.25  E-value: 5.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956296 442 VAAHEFGHAMGLEHSQD--------------------------PGALMAPIYTYTKnfrLSHDDIKGIQELY 487
Cdd:cd04268   97 TAEHELGHALGLRHNFAasdrddnvdllaekgdtssvmdyapsNFSIQLGDGQKYT---IGPYDIAAIKKLY 165
 
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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