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Conserved domains on  [gi|22218676|pdb|1GXD|B]
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Chain B, KDA TYPE IV COLLAGENASE

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. ...
 437-631 4.12e-76

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


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 241.06  E-value: 4.12e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      437 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 516
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      517 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 596
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
1GXD_B      597 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 631
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 89-417 4.51e-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: 215.94  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B         89 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 168
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        169 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 248
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        249 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 328
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        329 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 406
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
1GXD_B        407 DDIKGIQELYG 417
Cdd:pfam00413 149 DDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 313-361 3.23e-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: 95.44  E-value: 3.23e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         313 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 255-303 2.84e-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: 2.84e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         255 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 197-245 1.34e-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: 90.82  E-value: 1.34e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         197 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-68 4.90e-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: 38.27  E-value: 4.90e-04
                          10        20
                  ....*....|....*....|....*...
1GXD_B         41 LKDTLKKMQKFFGLPQTGDLDQNTIETM 68
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. ...
 437-631 4.12e-76

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


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 241.06  E-value: 4.12e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      437 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 516
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      517 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 596
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
1GXD_B      597 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 631
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 89-417 4.51e-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: 215.94  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B         89 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 168
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        169 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 248
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        249 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 328
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        329 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 406
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
1GXD_B        407 DDIKGIQELYG 417
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 89-417 2.60e-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: 195.50  E-value: 2.60e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B       89 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 167
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      168 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 247
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      248 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 327
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      328 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 406
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                       330
                ....*....|.
1GXD_B      407 DDIKGIQELYG 417
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 313-361 3.23e-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: 95.44  E-value: 3.23e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         313 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 255-303 2.84e-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: 2.84e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         255 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 197-245 1.34e-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: 90.82  E-value: 1.34e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         197 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 314-361 5.50e-22

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 89.29  E-value: 5.50e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      314 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 256-303 7.13e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 85.82  E-value: 7.13e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      256 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 86-189 3.65e-20

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 87.02  E-value: 3.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B          86 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 165
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
1GXD_B         166 FAPgtgvGGDSHFdDDELWTLGEG 189
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 ...
 198-245 5.79e-20

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.51  E-value: 5.79e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      198 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
320-361 7.15e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 7.15e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        320 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
204-245 8.69e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 8.69e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        204 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
262-303 2.21e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 2.21e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        262 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-585 4.36e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.33  E-value: 4.36e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
1GXD_B         539 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 585
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-585 3.23e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.87  E-value: 3.23e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
1GXD_B        539 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 585
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-68 4.90e-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: 38.27  E-value: 4.90e-04
                          10        20
                  ....*....|....*....|....*...
1GXD_B         41 LKDTLKKMQKFFGLPQTGDLDQNTIETM 68
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. ...
 437-631 4.12e-76

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


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 241.06  E-value: 4.12e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      437 PEICKQdIVFDGIAQIRGEIFFFKDRFIWRtVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSA 516
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWR-LSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      517 STLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQg 596
Cdd:cd00094  79 KNLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWL- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
1GXD_B      597 GGHSYFFKGAYYLKLENQSLKS--VKFGSIKSDWLGC 631
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKEVrvGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 89-417 4.51e-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: 215.94  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B         89 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 168
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        169 GTGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcphe 248
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        249 alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftflg 328
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B        329 nkyesctsagrsdgkmwcattanydddrkwgfcPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQ 406
Cdd:pfam00413 102 ---------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldSKKFRLSQ 148

                         330
                  ....*....|.
1GXD_B        407 DDIKGIQELYG 417
Cdd:pfam00413 149 DDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 89-417 2.60e-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: 195.50  E-value: 2.60e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B       89 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 167
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      168 PGtGVGGDSHFDDDELWTLGEGqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph 247
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      248 ealftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpetamstvggnsegapcvfpftfl 327
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      328 gnkyesctsagrsdgkmwcattanydddrkwgfcpDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQ 406
Cdd:cd04278 102 -----------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQ 146

                       330
                ....*....|.
1GXD_B      407 DDIKGIQELYG 417
Cdd:cd04278 147 DDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 313-361 3.23e-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: 95.44  E-value: 3.23e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         313 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 255-303 2.84e-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: 2.84e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         255 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 197-245 1.34e-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: 90.82  E-value: 1.34e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
1GXD_B         197 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 314-361 5.50e-22

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 89.29  E-value: 5.50e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      314 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 256-303 7.13e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 85.82  E-value: 7.13e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      256 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 86-189 3.65e-20

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 87.02  E-value: 3.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B          86 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 165
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
1GXD_B         166 FAPgtgvGGDSHFdDDELWTLGEG 189
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 ...
 198-245 5.79e-20

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.51  E-value: 5.79e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1GXD_B      198 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
320-361 7.15e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 7.15e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        320 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 361
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
204-245 8.69e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 8.69e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        204 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 245
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
262-303 2.21e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 2.21e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1GXD_B        262 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 303
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-585 4.36e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.33  E-value: 4.36e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
1GXD_B         539 VDAAFnWSKNKKTYIFAGDKFWRYNEvkKKMDPGFPKLIADAWNAIP 585
Cdd:smart00120   1 IDAAF-ELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-585 3.23e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.87  E-value: 3.23e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
1GXD_B        539 VDAAFNWSKNKkTYIFAGDKFWRYNEvkKKMDPGFPKLIADaWNAIP 585
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 491-534 3.94e-06

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 44.09  E-value: 3.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
1GXD_B        491 IDAVYEAPQEeKAVFFAGNEYWIYSASTLERGYPKPLTSL-GLPP 534
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 491-534 3.20e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 41.46  E-value: 3.20e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
1GXD_B         491 IDAVYEAPqEEKAVFFAGNEYWIYSASTLERGYPKPLTSL--GLPP 534
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 365-416 3.90e-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: 44.44  E-value: 3.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1GXD_B      365 GYSLFLVAAHAFGHAMGLEHSQD--------------------PGALMAPI---YTYTKNFRLSQDDIKGIQELY 416
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 446-488 3.92e-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: 38.38  E-value: 3.92e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
1GXD_B         446 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELP 488
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-68 4.90e-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: 38.27  E-value: 4.90e-04
                          10        20
                  ....*....|....*....|....*...
1GXD_B         41 LKDTLKKMQKFFGLPQTGDLDQNTIETM 68
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 446-488 1.06e-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: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
1GXD_B        446 FDGIAQIR-GEIFFFKDRFIWRTVTPRDKPMGPLLVATFwPELP 488
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 95-193 1.86e-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: 39.43  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B       95 ITYRIIGYTPDLD----PETVDDAFARAFQVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 168
Cdd:cd00203   3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74

                        90       100
                ....*....|....*....|....*..
1GXD_B      169 GT--GVGGDSHFDDDELWTLGEGQVVR 193
Cdd:cd00203  75 RVcdSLRGVGVLQDNQSGTKEGAQTIA 101
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 335-417 3.63e-03

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: 38.94  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1GXD_B      335 TSAGRSDGKMWCATTANYDDDRKwgfcPDQGYSLFLvaaHAFGHAMGLEHSQDPGA----------------LMA----P 394
Cdd:cd04277  87 GSGTAYGGDIWFNSSYDTNSDSP----GSYGYQTII---HEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgY 159

                        90       100
                ....*....|....*....|....*..
1GXD_B      395 IYTYTKNFRLSQ----DDIKGIQELYG 417
Cdd:cd04277 160 GNGASAGGGYPQtpmlLDIAALQYLYG 186
 
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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