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Conserved domains on  [gi|7305277|ref|NP_038627|]
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matrix metalloproteinase-9 preproprotein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 532-729 6.25e-61

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: 202.93  E-value: 6.25e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  532 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 610
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  611 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 687
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7305277  688 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 729
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 1.87e-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: 200.54  E-value: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    115 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    195 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    275 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    355 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 7305277    433 KDDIDGIQYLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 9.32e-24

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


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 94.29  E-value: 9.32e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     223 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 3.42e-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: 90.05  E-value: 3.42e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     281 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 5.78e-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: 5.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     340 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 474-525 7.47e-08

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


:

Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 49.01  E-value: 7.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7305277    474 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 525
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-95 1.30e-03

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: 37.49  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305277     42 DTQLAEAYLYRYGYTRAAQMM--GEKqsLRPALLMLQKQLSLPQTGELDSQTLKAI 95
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGyfGPS--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. ...
 532-729 6.25e-61

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: 202.93  E-value: 6.25e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  532 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 610
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  611 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 687
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7305277  688 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 729
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 1.87e-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: 200.54  E-value: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    115 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    195 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    275 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    355 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 7305277    433 KDDIDGIQYLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-444 1.29e-50

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 173.54  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  115 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRV-YGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  194 PGaGVQGDAHFDDDELWSLGkgvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  274 erlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvf 353
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  354 lgkqyssctSDGRrdgrlwcattsnfdtdkkwgfcpdqGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLEG-FPLN 432
Cdd:cd04278 100 ---------SDSG-------------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPkFKLS 145

                       330
                ....*....|..
gi 7305277  433 KDDIDGIQYLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 9.32e-24

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 94.29  E-value: 9.32e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     223 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 224-271 2.27e-22

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 90.44  E-value: 2.27e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  224 NSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 3.42e-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: 90.05  E-value: 3.42e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     281 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 5.78e-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: 5.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     340 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
347-388 3.00e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 86.85  E-value: 3.00e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    347 CVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 282-329 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: 85.43  E-value: 1.21e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  282 NGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 341-388 2.27e-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: 2.27e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  341 NSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
288-329 1.56e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 82.23  E-value: 1.56e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    288 CVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
230-271 2.05e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.85  E-value: 2.05e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    230 CHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-218 6.34e-15

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: 72.38  E-value: 6.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277     112 KGLKWDHHNITYWIqnYSEDLPRDmIDDAFARAFAVWGEVAPLTFTRVYgPEADIVIQFGVaehGDGYPFdgkdglLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERT-GTADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 7305277     192 FPPGagvqGDAHFdDDELWSLGKGVVI 218
Cdd:smart00235  68 GRPG----GDQHL-SLGNGCINTGVAA 89
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 474-525 7.47e-08

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 49.01  E-value: 7.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7305277    474 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 525
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 451-530 1.42e-05

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 48.03  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277   451 PRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPtsspspgptgapSPGPTAPPTAGSSEASTESLSPA 530
Cdd:PHA03291 208 PRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPE------------AEGTPAPPTPGGGEAPPANATPA 275
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-582 8.96e-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: 8.96e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 7305277     539 FDAIAEIQ-GALHFFKDGWYWKFLNHRGSPlQGPFLTARTWPALP 582
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDP-GYPKLISSFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 399-421 4.77e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 42.36  E-value: 4.77e-04
                        10        20
                ....*....|....*....|....
gi 7305277  399 AAHEFGHALGL-DHSSVPEALMYP 421
Cdd:COG5549 186 ARHELGHALGIwGHSPSPTDAMYF 209
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-95 1.30e-03

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: 37.49  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305277     42 DTQLAEAYLYRYGYTRAAQMM--GEKqsLRPALLMLQKQLSLPQTGELDSQTLKAI 95
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGyfGPS--TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 447-523 2.30e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 41.03  E-value: 2.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305277    447 SKPDPRPPATTTTEPQPTAPPTmcPTIPPTAYPTVGPTVGPTGApspgpTSSPSPGPTGAPSPGPTAPPTAGSSEAS 523
Cdd:TIGR00601  75 SKPKTGTGKVAPPAATPTSAPT--PTPSPPASPASGMSAAPASA-----VEEKSPSEESATATAPESPSTSVPSSGS 144
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 532-729 6.25e-61

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: 202.93  E-value: 6.25e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  532 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 610
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  611 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 687
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7305277  688 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 729
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 1.87e-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: 200.54  E-value: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    115 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    195 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    275 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    355 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 7305277    433 KDDIDGIQYLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-444 1.29e-50

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 173.54  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  115 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRV-YGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  194 PGaGVQGDAHFDDDELWSLGkgvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  274 erlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvf 353
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  354 lgkqyssctSDGRrdgrlwcattsnfdtdkkwgfcpdqGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLEG-FPLN 432
Cdd:cd04278 100 ---------SDSG-------------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPkFKLS 145

                       330
                ....*....|..
gi 7305277  433 KDDIDGIQYLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 9.32e-24

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 94.29  E-value: 9.32e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     223 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 224-271 2.27e-22

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 90.44  E-value: 2.27e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  224 NSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 3.42e-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: 90.05  E-value: 3.42e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     281 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 5.78e-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: 5.78e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 7305277     340 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
347-388 3.00e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 86.85  E-value: 3.00e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    347 CVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 282-329 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: 85.43  E-value: 1.21e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  282 NGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 341-388 2.27e-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: 2.27e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7305277  341 NSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
288-329 1.56e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 82.23  E-value: 1.56e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    288 CVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
230-271 2.05e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.85  E-value: 2.05e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305277    230 CHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-218 6.34e-15

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: 72.38  E-value: 6.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277     112 KGLKWDHHNITYWIqnYSEDLPRDmIDDAFARAFAVWGEVAPLTFTRVYgPEADIVIQFGVaehGDGYPFdgkdglLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERT-GTADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 7305277     192 FPPGagvqGDAHFdDDELWSLGKGVVI 218
Cdd:smart00235  68 GRPG----GDQHL-SLGNGCINTGVAA 89
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 398-444 7.88e-12

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


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 63.52  E-value: 7.88e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 7305277     398 VAAHEFGHALGLDHSSVPEA---LMYPLYSY--LEGFPLNKDDIDGIQYLYG 444
Cdd:smart00235  87 VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 381-444 6.55e-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: 6.55e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7305277  381 TDKKWGFCPDQG-YSLFLVAAHEFGHALGLDHSSV-PEALMYPLYSYLE--GFPLNKDDIDGIQYLYG 444
Cdd:cd04279  89 TDINLGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPdgNPTLSARDVATLKRLYG 156
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 474-525 7.47e-08

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 49.01  E-value: 7.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7305277    474 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 525
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 451-530 1.42e-05

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 48.03  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277   451 PRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPtsspspgptgapSPGPTAPPTAGSSEASTESLSPA 530
Cdd:PHA03291 208 PRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPE------------AEGTPAPPTPGGGEAPPANATPA 275
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 358-444 4.01e-05

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 45.10  E-value: 4.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277  358 YSSCTSDGRRDGRLWcattsnFDTDKKWGFCPDQGYSlFLVAAHEFGHALGLDHS-----SVPEALMYPLYSYL------ 426
Cdd:cd04277  83 YPGSGSGTAYGGDIW------FNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHPgdyngGDPVPPTYALDSREytvmsy 155

                        90       100       110
                ....*....|....*....|....*....|.
gi 7305277  427 EGFPLNK-------------DDIDGIQYLYG 444
Cdd:cd04277 156 NSGYGNGasagggypqtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 398-443 5.56e-05

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: 44.02  E-value: 5.56e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305277  398 VAAHEFGHALGLDHSS----------------VPEALMYPLYSYL-------EGFPLNKDDIDGIQYLY 443
Cdd:cd04268  97 TAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFsiqlgdgQKYTIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 539-582 8.96e-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: 8.96e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 7305277     539 FDAIAEIQ-GALHFFKDGWYWKFLNHRGSPlQGPFLTARTWPALP 582
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDP-GYPKLISSFFPGLP 44
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 392-443 2.45e-04

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: 42.51  E-value: 2.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305277  392 GYSLFLVAAHEFGHALGLDHSSVPEA--------------------LMYPL---YSYLEGFPLNKDDIDGIQYLY 443
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 445-533 3.74e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.93  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277   445 RGSKPDPRP----PATTTTEPQPTAPPTMCPTIPPtayptvgPTVGPTGAPSPGPTSSPSPGPTGAPsPGPTAPPT-AGS 519
Cdd:PHA02682  92 APACPACAPaapaPAVTCPAPAPACPPATAPTCPP-------PAVCPAPARPAPACPPSTRQCPPAP-PLPTPKPApAAK 163

                         90
                 ....*....|....
gi 7305277   520 SEASTESLSPADNP 533
Cdd:PHA02682 164 PIFLHNQLPPPDYP 177
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 399-421 4.77e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 42.36  E-value: 4.77e-04
                        10        20
                ....*....|....*....|....
gi 7305277  399 AAHEFGHALGL-DHSSVPEALMYP 421
Cdd:COG5549 186 ARHELGHALGIwGHSPSPTDAMYF 209
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 462-490 4.82e-04

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 38.23  E-value: 4.82e-04
                          10        20
                  ....*....|....*....|....*....
gi 7305277    462 QPTAPPTMCPTIPPTAYPTVGPTVGPTGA 490
Cdd:pfam04886   5 QPTAQPTVQPTGQPTAQPTDQPTAQPTDA 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 449-530 7.75e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    449 PDPRPPATTTTEP----QPTAPPTmcPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPGPTAPPTA---GSSE 521
Cdd:PHA03247 2739 PAPPAVPAGPATPggpaRPARPPT--TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAavlAPAA 2816


                  ....*....
gi 7305277    522 ASTESLSPA 530
Cdd:PHA03247 2817 ALPPAASPA 2825
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 441-533 9.22e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.41  E-value: 9.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277   441 YLYGRGSKPDPRPPAT--TTTEPQPTAPPTMC------PTIPPT--AYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPG 510
Cdd:PHA03269  32 HTSAATQKPDPAPAPHqaASRAPDPAVAPTSAasrkpdLAQAPTpaASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPD 111

                         90       100
                 ....*....|....*....|...
gi 7305277   511 PTAPPTAgsseASTESLSPADNP 533
Cdd:PHA03269 112 AAEAFTS----AAQAHEAPADAG 130
PHA03247 PHA03247
large tegument protein UL36; Provisional
 445-529 9.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    445 RGSKPDPRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPS----PGPTAPPTAGSS 520
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGrvavPRFRVPQPAPSR 2986


                  ....*....
gi 7305277    521 EASTESLSP 529
Cdd:PHA03247 2987 EAPASSTPP 2995
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 42-95 1.30e-03

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: 37.49  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305277     42 DTQLAEAYLYRYGYTRAAQMM--GEKqsLRPALLMLQKQLSLPQTGELDSQTLKAI 95
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPVDGyfGPS--TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 447-523 2.30e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 41.03  E-value: 2.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305277    447 SKPDPRPPATTTTEPQPTAPPTmcPTIPPTAYPTVGPTVGPTGApspgpTSSPSPGPTGAPSPGPTAPPTAGSSEAS 523
Cdd:TIGR00601  75 SKPKTGTGKVAPPAATPTSAPT--PTPSPPASPASGMSAAPASA-----VEEKSPSEESATATAPESPSTSVPSSGS 144
PHA03247 PHA03247
large tegument protein UL36; Provisional
 446-536 2.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305277    446 GSKPDPRPPATTTTEPQPTAP---------PTMCPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPGP---TA 513
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPaaarqaspaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrLT 2784

                          90       100
                  ....*....|....*....|....*..
gi 7305277    514 PPTAGSSEASTESL----SPADNPCNV 536
Cdd:PHA03247 2785 RPAVASLSESRESLpspwDPADPPAAV 2811
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
398-437 6.57e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 6.57e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 7305277  398 VAAHEFGHALGLDHSSVPEALMYplysylegFPLNKDDID 437
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMH--------FSNSLEELD 157
 
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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