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Conserved domains on  [gi|119603232|gb|EAW82826|]
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matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), isoform CRA_c [Homo sapiens]

Protein Classification

ZnMc_MMP and FN2 domain-containing protein( domain architecture ID 12021232)

protein containing domains PG_binding_1, ZnMc_MMP, and FN2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 3.65e-58

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: 187.82  E-value: 3.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232  118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 119603232  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 5.74e-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: 93.90  E-value: 5.74e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 5.06e-23

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


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 5.06e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.43e-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: 2.43e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 2.88e-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: 2.88e-04
                          10        20
                  ....*....|....*....|....*...
gi 119603232   70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 400-416 5.63e-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.


The actual alignment was detected with superfamily member cd04268:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 165  Bit Score: 37.48  E-value: 5.63e-03
                         10
                 ....*....|....*..
gi 119603232 400 VAAHEFGHAMGLEHSQT 416
Cdd:cd04268   97 TAEHELGHALGLRHNFA 113
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 3.65e-58

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: 187.82  E-value: 3.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232  118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 119603232  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-216 2.35e-52

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: 172.77  E-value: 2.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232 118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100
                 ....*....|....*....|
gi 119603232 197 PGtGVGGDSHFDDDELWTLG 216
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG 99
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 5.74e-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: 93.90  E-value: 5.74e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 5.06e-23

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 5.06e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.43e-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: 2.43e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 343-390 8.89e-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: 87.75  E-value: 8.89e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 343 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.18e-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: 87.41  E-value: 1.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232   115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 119603232   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 ...
 285-332 1.21e-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: 84.66  E-value: 1.21e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 285 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 9.51e-20

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 81.97  E-value: 9.51e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 227 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
349-390 1.11e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 1.11e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  349 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 1.36e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 1.36e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  233 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
291-332 3.43e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 77.61  E-value: 3.43e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  291 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 2.88e-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: 2.88e-04
                          10        20
                  ....*....|....*....|....*...
gi 119603232   70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 400-416 5.63e-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: 37.48  E-value: 5.63e-03
                         10
                 ....*....|....*..
gi 119603232 400 VAAHEFGHAMGLEHSQT 416
Cdd:cd04268   97 TAEHELGHALGLRHNFA 113
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 118-218 3.65e-58

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: 187.82  E-value: 3.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232  118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100
                  ....*....|....*....|.
gi 119603232  198 GTGVGGDSHFDDDELWTLGEG 218
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD 101
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-216 2.35e-52

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: 172.77  E-value: 2.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232 118 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 196
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100
                 ....*....|....*....|
gi 119603232 197 PGtGVGGDSHFDDDELWTLG 216
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG 99
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 342-390 5.74e-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: 93.90  E-value: 5.74e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   342 GNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 284-332 5.06e-23

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 5.06e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   284 GNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 226-274 2.43e-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: 2.43e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119603232   226 GNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 343-390 8.89e-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: 87.75  E-value: 8.89e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 343 NSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-218 1.18e-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: 87.41  E-value: 1.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232   115 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 194
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67

                           90       100
                   ....*....|....*....|....
gi 119603232   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 ...
 285-332 1.21e-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: 84.66  E-value: 1.21e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 285 NAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 227-274 9.51e-20

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 81.97  E-value: 9.51e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119603232 227 NADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
349-390 1.11e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 1.11e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  349 CVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFC 390
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
233-274 1.36e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 78.77  E-value: 1.36e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  233 CKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFC 274
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
291-332 3.43e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 77.61  E-value: 3.43e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119603232  291 CKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFC 332
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 70-97 2.88e-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: 2.88e-04
                          10        20
                  ....*....|....*....|....*...
gi 119603232   70 LKDTLKKMQKFFGLPQTGDLDQNTIETM 97
Cdd:pfam01471  30 TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 124-222 1.23e-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: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119603232 124 ITYRIIGYTPDLD----PETVDDAFARAFQVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 197
Cdd:cd00203    3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74

                         90       100
                 ....*....|....*....|....*..
gi 119603232 198 GT--GVGGDSHFDDDELWTLGEGQVVR 222
Cdd:cd00203   75 RVcdSLRGVGVLQDNQSGTKEGAQTIA 101
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 400-416 5.63e-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: 37.48  E-value: 5.63e-03
                         10
                 ....*....|....*..
gi 119603232 400 VAAHEFGHAMGLEHSQT 416
Cdd:cd04268   97 TAEHELGHALGLRHNFA 113
 
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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