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Conserved domains on  [gi|6678902|ref|NP_032636|]
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72 kDa type IV collagenase preproprotein [Mus musculus]

Protein Classification

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

protein containing domains PG_binding_1, ZnMc_MMP, FN2, and HX

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
468-662 1.30e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 245.68  E-value: 1.30e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  468 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 547
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  548 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 627
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6678902  628 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 662
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-446 4.26e-67

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: 216.71  E-value: 4.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngreyssctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    278 alftmggnadgqpckfpfrfqgtsynscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    358 nkyesctsagrndgkvwcatttnydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSH 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148
                         330
                  ....*....|.
gi 6678902    436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
342-390 6.11e-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: 94.67  E-value: 6.11e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     342 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
284-332 2.99e-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: 92.75  E-value: 2.99e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     284 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
226-274 4.61e-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: 89.28  E-value: 4.61e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     226 GNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
70-97 4.49e-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: 4.49e-04
                          10        20
                  ....*....|....*....|....*...
gi 6678902     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. ...
468-662 1.30e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 245.68  E-value: 1.30e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  468 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 547
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  548 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 627
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6678902  628 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 662
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-446 4.26e-67

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: 216.71  E-value: 4.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngreyssctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    278 alftmggnadgqpckfpfrfqgtsynscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    358 nkyesctsagrndgkvwcatttnydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSH 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148
                         330
                  ....*....|.
gi 6678902    436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
118-446 1.38e-59

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: 196.66  E-value: 1.38e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  197 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngreyssctdtgrsdgflwcsttynfekdgkygfcph 276
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  277 ealftmggnadgqpckfpfrfqgtsynscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 356
Cdd:cd04278     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  357 gnkyesctsagrndgkvwcatttnydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSH 435
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146
                       330
                ....*....|.
gi 6678902  436 DDIKGIQELYG 446
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
342-390 6.11e-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: 94.67  E-value: 6.11e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     342 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
284-332 2.99e-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: 92.75  E-value: 2.99e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     284 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
226-274 4.61e-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: 89.28  E-value: 4.61e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     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 ...
343-390 6.96e-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: 6.96e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  343 NSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
285-332 4.47e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.47e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  285 NADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
115-218 1.08e-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: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902     115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARALKVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67
                           90       100
                   ....*....|....*....|....
gi 6678902     195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
227-274 1.98e-19

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: 81.97  E-value: 1.98e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  227 NADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
291-332 1.59e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.59e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    291 CKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 1.80e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.80e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    233 CKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
349-390 1.27e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 76.45  E-value: 1.27e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    349 CVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
570-616 5.80e-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: 57.64  E-value: 5.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6678902     570 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADSWNAIP 616
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
570-612 8.78e-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: 51.41  E-value: 8.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6678902    570 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADSW 612
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISDFP 40
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
70-97 4.49e-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: 4.49e-04
                          10        20
                  ....*....|....*....|....*...
gi 6678902     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. ...
468-662 1.30e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 245.68  E-value: 1.30e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  468 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSA 547
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  548 STLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQg 627
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6678902  628 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 662
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
118-446 4.26e-67

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: 216.71  E-value: 4.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    198 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngreyssctdtgrsdgflwcsttynfekdgkygfcphe 277
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    278 alftmggnadgqpckfpfrfqgtsynscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 357
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902    358 nkyesctsagrndgkvwcatttnydddrkwgfcPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSH 435
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148
                         330
                  ....*....|.
gi 6678902    436 DDIKGIQELYG 446
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
118-446 1.38e-59

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: 196.66  E-value: 1.38e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  118 KWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  197 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngreyssctdtgrsdgflwcsttynfekdgkygfcph 276
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  277 ealftmggnadgqpckfpfrfqgtsynscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 356
Cdd:cd04278     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  357 gnkyesctsagrndgkvwcatttnydddrkwgfcpDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSH 435
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146
                       330
                ....*....|.
gi 6678902  436 DDIKGIQELYG 446
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
342-390 6.11e-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: 94.67  E-value: 6.11e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     342 GNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
284-332 2.99e-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: 92.75  E-value: 2.99e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     284 GNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
226-274 4.61e-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: 89.28  E-value: 4.61e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678902     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 ...
343-390 6.96e-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: 6.96e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  343 NSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
285-332 4.47e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.47e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  285 NADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
115-218 1.08e-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: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902     115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARALKVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67
                           90       100
                   ....*....|....*....|....
gi 6678902     195 FAPgtgvGGDSHFdDDELWTLGEG 218
Cdd:smart00235  68 GRP----GGDQHL-SLGNGCINTG 86
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
227-274 1.98e-19

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: 81.97  E-value: 1.98e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6678902  227 NADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
291-332 1.59e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.59e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    291 CKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 1.80e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 1.80e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    233 CKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
349-390 1.27e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 76.45  E-value: 1.27e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6678902    349 CVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
570-616 5.80e-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: 57.64  E-value: 5.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6678902     570 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADSWNAIP 616
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
570-612 8.78e-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: 51.41  E-value: 8.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6678902    570 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADSW 612
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 ...
387-446 7.31e-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: 7.31e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678902  387 WGFCPDQG-YSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSHDDIKGIQELYG 446
Cdd:cd04279  93 LGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
522-565 7.66e-07

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 46.02  E-value: 7.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6678902    522 IDAVYEAPQEeKAVFFAGNEYWVYSASTLERGYPKPLTSL-GLPP 565
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
522-565 9.82e-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: 43.00  E-value: 9.82e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 6678902     522 IDAVYEAPqEEKAVFFAGNEYWVYSASTLERGYPKPLTSL--GLPP 565
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
364-446 1.28e-05

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 46.25  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  364 TSAGRNDGKVWCATTTNYDDDRKwgfcPDQGYSLFLvaaHEFGHAMGLEHSQDPGA----------------LMA----P 423
Cdd:cd04277  87 GSGTAYGGDIWFNSSYDTNSDSP----GSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgY 159
                        90       100
                ....*....|....*....|....*..
gi 6678902  424 IYTYTKNFRLSHD----DIKGIQELYG 446
Cdd:cd04277 160 GNGASAGGGYPQTpmllDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
394-445 1.50e-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: 45.59  E-value: 1.50e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678902  394 GYSLFLVAAHEFGHAMGLEHSQD--------------------PGALMAPI---YTYTKNFRLSHDDIKGIQELY 445
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
477-519 1.11e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 39.92  E-value: 1.11e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 6678902     477 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELP 519
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
70-97 4.49e-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: 4.49e-04
                          10        20
                  ....*....|....*....|....*...
gi 6678902     70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
477-519 1.65e-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: 36.78  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 6678902    477 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPTGPLLVATFwPELP 519
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
124-222 2.65e-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: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678902  124 ITYRIIGYTPDLD----PETVDDAFARALKVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 197
Cdd:cd00203   3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74
                        90       100
                ....*....|....*....|....*..
gi 6678902  198 GT--GVGGDSHFDDDELWTLGEGQVVR 222
Cdd:cd00203  75 RVcdSLRGVGVLQDNQSGTKEGAQTIA 101
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
400-445 5.12e-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: 5.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678902  400 VAAHEFGHAMGLEHSQD--------------------------PGALMAPIYTYTKnfrLSHDDIKGIQELY 445
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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