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Conserved domains on  [gi|1705983|sp|P52176|]
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RecName: Full=Matrix metalloproteinase-9; Short=MMP-9; AltName: Full=92 kDa gelatinase; AltName: Full=92 kDa type IV collagenase; AltName: Full=Gelatinase B; Short=GELB; Flags: Precursor

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. ...
519-709 3.62e-68

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: 221.80  E-value: 3.62e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  519 DVCNVDIFDAIAEIRNRLHFFKAGKYWRLSEGggRRVQGPFLVKSKWPALPRKLDSAFEDPLTKKIFFFSGRQVWVYTGA 598
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  599 SL--LGPRRLDKLGLGPEVAQVTGALPRP-EGKVLLFSGQSFWRFDVKTQKVDPQSVTPVDQMFPGVPISTHDIFQYQ-E 674
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 1705983  675 KAYFCQDHFYWRVSSQNEVNQVDYVGYVTFDLLKC 709
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
115-444 6.35e-60

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: 198.61  E-value: 6.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    195 GKGIQGDAHFDDEELWSLGKGvviptyfgnakgaachfpftfegrsysacttdgrsddmlwcsttadydadrqfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    275 rlytqdgnadgkpcvfpftfqgrtysactsdgrsdgyrwcattanydqdklygfcptrvdatvtggnaagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    355 gkeysactregrndghlwcattsnfdkdkkwgfcPDQGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEH--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147
                         330
                  ....*....|..
gi 1705983    433 RDDVQGIQHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
340-388 1.92e-23

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


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.92e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     340 GNAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
281-329 6.75e-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: 91.98  E-value: 6.75e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     281 GNADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
223-271 4.78e-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: 4.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     223 GNAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
41-94 7.66e-11

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: 57.91  E-value: 7.66e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705983     41 NRQLAEEYLYRYGYTPGAELSEDGQSLQRALLRFQRRLSLPETGELDSTTLNAM 94
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
519-709 3.62e-68

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: 221.80  E-value: 3.62e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  519 DVCNVDIFDAIAEIRNRLHFFKAGKYWRLSEGggRRVQGPFLVKSKWPALPRKLDSAFEDPLTKKIFFFSGRQVWVYTGA 598
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  599 SL--LGPRRLDKLGLGPEVAQVTGALPRP-EGKVLLFSGQSFWRFDVKTQKVDPQSVTPVDQMFPGVPISTHDIFQYQ-E 674
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 1705983  675 KAYFCQDHFYWRVSSQNEVNQVDYVGYVTFDLLKC 709
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
115-444 6.35e-60

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: 198.61  E-value: 6.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    195 GKGIQGDAHFDDEELWSLGKGvviptyfgnakgaachfpftfegrsysacttdgrsddmlwcsttadydadrqfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    275 rlytqdgnadgkpcvfpftfqgrtysactsdgrsdgyrwcattanydqdklygfcptrvdatvtggnaagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    355 gkeysactregrndghlwcattsnfdkdkkwgfcPDQGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEH--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147
                         330
                  ....*....|..
gi 1705983    433 RDDVQGIQHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
115-444 7.92e-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: 176.63  E-value: 7.92e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRV-YGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  194 PGkGIQGDAHFDDEELWSLGkgvviptyfgnakgaachfpftfegrsysacttdgrsddmlwcsttadydadrqfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  274 erlytqdgnadgkpcvfpftfqgrtysactsdgrsdgyrwcattanydqdklygfcptrvdatvtggnaagelcvfpftf 353
Cdd:cd04278     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  354 lgkeysactregrNDGHlwcattsnfdkdkkwgfcpdqGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEHP-LH 432
Cdd:cd04278 100 -------------SDSG---------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFkLS 145
                       330
                ....*....|..
gi 1705983  433 RDDVQGIQHLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
340-388 1.92e-23

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.92e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     340 GNAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
281-329 6.75e-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: 91.98  E-value: 6.75e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     281 GNADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
223-271 4.78e-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: 4.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     223 GNAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
341-388 2.27e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 87.36  E-value: 2.27e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  341 NAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
282-329 2.43e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 87.36  E-value: 2.43e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  282 NADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
224-271 5.56e-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: 86.21  E-value: 5.56e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  224 NAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
347-388 1.36e-20

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 84.93  E-value: 1.36e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    347 CVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
288-329 3.75e-20

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 83.77  E-value: 3.75e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    288 CVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
230-271 9.24e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.24e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    230 CHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
112-218 1.32e-17

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: 79.70  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983     112 GELKWHHHNITYWIqnYSEDLPRAViDDAFARAFALWSAVTPLTFTRVYgPEADIVIQFGVREHGdgypfdgknGLLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---------CTLSHA 67
                           90       100
                   ....*....|....*....|....*..
gi 1705983     192 FPPGkgiqGDAHFDDEElWSLGKGVVI 218
Cdd:smart00235  68 GRPG----GDQHLSLGN-GCINTGVAA 89
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
41-94 7.66e-11

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: 57.91  E-value: 7.66e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705983     41 NRQLAEEYLYRYGYTPGAELSEDGQSLQRALLRFQRRLSLPETGELDSTTLNAM 94
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
618-663 1.40e-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: 42.61  E-value: 1.40e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1705983     618 VTGALPRPEGKVLLFSGQSFWRFDVktQKVDPQSVTPVDQMFPGVP 663
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
389-421 2.52e-03

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 40.05  E-value: 2.52e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 1705983  389 PDQ-GYSLFLVAAHEFGHALGL-DHTSVPEALMYP 421
Cdd:COG5549 175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYF 209
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
519-709 3.62e-68

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: 221.80  E-value: 3.62e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  519 DVCNVDIFDAIAEIRNRLHFFKAGKYWRLSEGggRRVQGPFLVKSKWPALPRKLDSAFEDPLTKKIFFFSGRQVWVYTGA 598
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  599 SL--LGPRRLDKLGLGPEVAQVTGALPRP-EGKVLLFSGQSFWRFDVKTQKVDPQSVTPVDQMFPGVPISTHDIFQYQ-E 674
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 1705983  675 KAYFCQDHFYWRVSSQNEVNQVDYVGYVTFDLLKC 709
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
115-444 6.35e-60

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: 198.61  E-value: 6.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    195 GKGIQGDAHFDDEELWSLGKGvviptyfgnakgaachfpftfegrsysacttdgrsddmlwcsttadydadrqfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    275 rlytqdgnadgkpcvfpftfqgrtysactsdgrsdgyrwcattanydqdklygfcptrvdatvtggnaagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983    355 gkeysactregrndghlwcattsnfdkdkkwgfcPDQGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEH--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147
                         330
                  ....*....|..
gi 1705983    433 RDDVQGIQHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
115-444 7.92e-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: 176.63  E-value: 7.92e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRV-YGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  194 PGkGIQGDAHFDDEELWSLGkgvviptyfgnakgaachfpftfegrsysacttdgrsddmlwcsttadydadrqfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  274 erlytqdgnadgkpcvfpftfqgrtysactsdgrsdgyrwcattanydqdklygfcptrvdatvtggnaagelcvfpftf 353
Cdd:cd04278     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  354 lgkeysactregrNDGHlwcattsnfdkdkkwgfcpdqGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEHP-LH 432
Cdd:cd04278 100 -------------SDSG---------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFkLS 145
                       330
                ....*....|..
gi 1705983  433 RDDVQGIQHLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
340-388 1.92e-23

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 93.52  E-value: 1.92e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     340 GNAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
281-329 6.75e-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: 91.98  E-value: 6.75e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     281 GNADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
223-271 4.78e-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: 4.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1705983     223 GNAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
341-388 2.27e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 87.36  E-value: 2.27e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  341 NAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
282-329 2.43e-21

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 87.36  E-value: 2.43e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  282 NADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
224-271 5.56e-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: 86.21  E-value: 5.56e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 1705983  224 NAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
347-388 1.36e-20

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 84.93  E-value: 1.36e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    347 CVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
288-329 3.75e-20

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 83.77  E-value: 3.75e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    288 CVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
230-271 9.24e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.24e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705983    230 CHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
112-218 1.32e-17

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: 79.70  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983     112 GELKWHHHNITYWIqnYSEDLPRAViDDAFARAFALWSAVTPLTFTRVYgPEADIVIQFGVREHGdgypfdgknGLLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSG---------CTLSHA 67
                           90       100
                   ....*....|....*....|....*..
gi 1705983     192 FPPGkgiqGDAHFDDEElWSLGKGVVI 218
Cdd:smart00235  68 GRPG----GDQHLSLGN-GCINTGVAA 89
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
382-444 6.13e-11

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: 61.32  E-value: 6.13e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705983  382 DKKWGFCPDQG-YSLFLVAAHEFGHALGLDHTSV-PEALMYPMY--RFTEEHPLHRDDVQGIQHLYG 444
Cdd:cd04279  90 DINLGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
41-94 7.66e-11

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: 57.91  E-value: 7.66e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705983     41 NRQLAEEYLYRYGYTPGAELSEDGQSLQRALLRFQRRLSLPETGELDSTTLNAM 94
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
618-663 1.40e-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: 42.61  E-value: 1.40e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1705983     618 VTGALPRPEGKVLLFSGQSFWRFDVktQKVDPQSVTPVDQMFPGVP 663
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
526-570 8.82e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 40.30  E-value: 8.82e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1705983     526 FDAIAEIRN-RLHFFKAGKYWRLSEGGGRRVqGPFLVKSKWPALPR 570
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVDPG-YPKLISSFFPGLPC 45
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
374-444 1.11e-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: 40.48  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705983  374 ATTSNFDKDKKWGFCPDQGYSlFLVAAHEFGHALGLDHT-----SVPEALMYP--------M-YRFTEEHPLHRD----- 434
Cdd:cd04277  93 GGDIWFNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHPgdyngGDPVPPTYAldsreytvMsYNSGYGNGASAGggypq 171
                        90
                ....*....|....*
gi 1705983  435 -----DVQGIQHLYG 444
Cdd:cd04277 172 tpmllDIAALQYLYG 186
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
389-421 2.52e-03

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 40.05  E-value: 2.52e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 1705983  389 PDQ-GYSLFLVAAHEFGHALGL-DHTSVPEALMYP 421
Cdd:COG5549 175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYF 209
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
392-443 4.60e-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: 38.66  E-value: 4.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705983  392 GYSLFLVAAHEFGHALGLDHTSVPEA--------------------LMYPMY-RFTEEHPLH--RDDVQGIQHLY 443
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDfsQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
398-413 6.29e-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: 6.29e-03
                        10
                ....*....|....*.
gi 1705983  398 VAAHEFGHALGLDHTS 413
Cdd:cd04268  97 TAEHELGHALGLRHNF 112
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
398-421 6.82e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 6.82e-03
                        10        20
                ....*....|....*....|....
gi 1705983  398 VAAHEFGHALGLDHTSVPEALMYP 421
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
 
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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