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Conserved domains on  [gi|568915670|ref|XP_006498924|]
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matrix metalloproteinase-9 isoform X1 [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. ...
 472-669 4.27e-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: 202.54  E-value: 4.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 472 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 550
Cdd:cd00094    2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 551 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 627
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568915670 628 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 669
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 55-384 2.68e-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: 199.00  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670   55 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 134
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  135 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 214
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  215 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 294
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  295 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 372
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 568915670  373 KDDIDGIQYLYG 384
Cdd:pfam00413 148 QDDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 163-211 1.17e-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: 93.90  E-value: 1.17e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   163 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 221-269 4.24e-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: 89.67  E-value: 4.24e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   221 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 280-328 7.10e-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: 88.90  E-value: 7.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   280 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 414-465 5.01e-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: 49.40  E-value: 5.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915670  414 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 465
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PT super family cl04822
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 393-424 3.30e-03

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.


The actual alignment was detected with superfamily member pfam04886:

Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 35.53  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568915670  393 PPATTTTEP--QPTAPPTMCPTIPPTAYPTVGPT 424
Cdd:pfam04886   2 PTAQPTAQPtvQPTGQPTAQPTDQPTAQPTDAPT 35
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 472-669 4.27e-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: 202.54  E-value: 4.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 472 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 550
Cdd:cd00094    2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 551 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 627
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568915670 628 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 669
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 55-384 2.68e-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: 199.00  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670   55 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 134
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  135 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 214
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  215 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 294
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  295 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 372
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 568915670  373 KDDIDGIQYLYG 384
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 55-384 1.80e-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: 172.39  E-value: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  55 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRV-YGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 133
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 134 PGaGVQGDAHFDDDELWSLGkgvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcps 213
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 214 erlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvf 293
Cdd:cd04278      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 294 lgkqyssctSDGRrdgrlwcattsnfdtdkkwgfcpdqGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLEG-FPLN 372
Cdd:cd04278  100 ---------SDSG-------------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPkFKLS 145

                        330
                 ....*....|..
gi 568915670 373 KDDIDGIQYLYG 384
Cdd:cd04278  146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 163-211 1.17e-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: 93.90  E-value: 1.17e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   163 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 164-211 2.77e-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: 90.06  E-value: 2.77e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 164 NSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 221-269 4.24e-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: 89.67  E-value: 4.24e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   221 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 280-328 7.10e-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: 88.90  E-value: 7.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   280 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
287-328 3.61e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 86.85  E-value: 3.61e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  287 CVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 222-269 1.43e-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: 85.05  E-value: 1.43e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 222 NGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 281-328 2.72e-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: 84.28  E-value: 2.72e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 281 NSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
228-269 1.85e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.85  E-value: 1.85e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  228 CVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
170-211 2.43e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.46  E-value: 2.43e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  170 CHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 52-158 8.31e-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: 71.61  E-value: 8.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670    52 KGLKWDHHNITYWIqnYSEDLPRDmIDDAFARAFAVWGEVAPLTFTRVYgPEADIVIQFGVaehGDGYPFdgkdglLAHA 131
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERT-GTADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 568915670   132 FPPGagvqGDAHFdDDELWSLGKGVVI 158
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 ...
 414-465 5.01e-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: 49.40  E-value: 5.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915670  414 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 465
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 391-470 1.05e-05

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 48.41  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 391 PRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPtsspspgptgapSPGPTAPPTAGSSEASTESLSPA 470
Cdd:PHA03291 208 PRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPE------------AEGTPAPPTPGGGEAPPANATPA 275
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 479-522 9.34e-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: 9.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568915670   479 FDAIAEIQ-GALHFFKDGWYWKFLNHRGSPlQGPFLTARTWPALP 522
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDP-GYPKLISSFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 329-361 4.07e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 42.36  E-value: 4.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568915670 329 PDQ-GYSLFLVAAHEFGHALGL-DHSSVPEALMYP 361
Cdd:COG5549  175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYF 209
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 387-463 2.07e-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: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915670  387 SKPDPRPPATTTTEPQPTAPPTmcPTIPPTAYPTVGPTVGPTGApspgpTSSPSPGPTGAPSPGPTAPPTAGSSEAS 463
Cdd:TIGR00601  75 SKPKTGTGKVAPPAATPTSAPT--PTPSPPASPASGMSAAPASA-----VEEKSPSEESATATAPESPSTSVPSSGS 144
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 393-424 3.30e-03

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: 35.53  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568915670  393 PPATTTTEP--QPTAPPTMCPTIPPTAYPTVGPT 424
Cdd:pfam04886   2 PTAQPTAQPtvQPTGQPTAQPTDQPTAQPTDAPT 35
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 472-669 4.27e-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: 202.54  E-value: 4.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 472 NPCNVDVFDAIAEIQGALHFFKDGWYWKFlnHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTG- 550
Cdd:cd00094    2 DACDPLSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 551 -KTVLGPRSLDKLGLGPEVTHVSGLLPR-RLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQD- 627
Cdd:cd00094   80 nLEPGYPKPISDLGFPPTVKQIDAALRWpDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDg 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568915670 628 KAYFCHGKFFWRVSFQNEVNKVDHevnqvddVGYVTYDLLQC 669
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKEVRVGY-------PLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 55-384 2.68e-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: 199.00  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670   55 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 134
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  135 GAGVQGDAHFDDDELWSLGKGvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcpse 214
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  215 rlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvfl 294
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  295 gkqyssctsdgrrdgrlwcattsnfdtdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLE--GFPLN 372
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDskKFRLS 147

                         330
                  ....*....|..
gi 568915670  373 KDDIDGIQYLYG 384
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 55-384 1.80e-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: 172.39  E-value: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  55 KWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRV-YGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 133
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 134 PGaGVQGDAHFDDDELWSLGkgvviptyygnsngapchfpftfegrsysacttdgrndgtpwcsttadydkdgkfgfcps 213
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLG------------------------------------------------------------ 99

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 214 erlytehgngegkpcvfpfifegrsysacttkgrsdgyrwcattanydqdklygfcptrvdatvvggnsagelcvfpfvf 293
Cdd:cd04278      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 294 lgkqyssctSDGRrdgrlwcattsnfdtdkkwgfcpdqGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLEG-FPLN 372
Cdd:cd04278  100 ---------SDSG-------------------------GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPkFKLS 145

                        330
                 ....*....|..
gi 568915670 373 KDDIDGIQYLYG 384
Cdd:cd04278  146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 163-211 1.17e-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: 93.90  E-value: 1.17e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   163 GNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 164-211 2.77e-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: 90.06  E-value: 2.77e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 164 NSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 221-269 4.24e-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: 89.67  E-value: 4.24e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   221 GNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 280-328 7.10e-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: 88.90  E-value: 7.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568915670   280 GNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
287-328 3.61e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 86.85  E-value: 3.61e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  287 CVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 222-269 1.43e-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: 85.05  E-value: 1.43e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 222 NGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 281-328 2.72e-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: 84.28  E-value: 2.72e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568915670 281 NSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFC 328
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
228-269 1.85e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.85  E-value: 1.85e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  228 CVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFC 269
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
170-211 2.43e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.46  E-value: 2.43e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568915670  170 CHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFC 211
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 52-158 8.31e-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: 71.61  E-value: 8.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670    52 KGLKWDHHNITYWIqnYSEDLPRDmIDDAFARAFAVWGEVAPLTFTRVYgPEADIVIQFGVaehGDGYPFdgkdglLAHA 131
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERT-GTADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 568915670   132 FPPGagvqGDAHFdDDELWSLGKGVVI 158
Cdd:smart00235  68 GRPG----GDQHL-SLGNGCINTGVAA 89
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 338-384 8.77e-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: 63.14  E-value: 8.77e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915670   338 VAAHEFGHALGLDHSSVPEA---LMYPLYSY--LEGFPLNKDDIDGIQYLYG 384
Cdd:smart00235  87 VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 321-384 5.99e-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: 5.99e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915670 321 TDKKWGFCPDQG-YSLFLVAAHEFGHALGLDHSSV-PEALMYPLYSYLE--GFPLNKDDIDGIQYLYG 384
Cdd:cd04279   89 TDINLGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPdgNPTLSARDVATLKRLYG 156
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 414-465 5.01e-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: 49.40  E-value: 5.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915670  414 PPTAYPTVGPTVGPTGApspgptsspspgptgaPSPGPTAPPTAGSSEASTE 465
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQ----------------PTAQPTDQPTAQPTDAPTA 36
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 391-470 1.05e-05

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 48.41  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 391 PRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPtsspspgptgapSPGPTAPPTAGSSEASTESLSPA 470
Cdd:PHA03291 208 PRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPE------------AEGTPAPPTPGGGEAPPANATPA 275
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 298-384 3.31e-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: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 298 YSSCTSDGRRDGRLWcattsnFDTDKKWGFCPDQGYSlFLVAAHEFGHALGLDHS-----SVPEALMYPLYSYL------ 366
Cdd:cd04277   83 YPGSGSGTAYGGDIW------FNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHPgdyngGDPVPPTYALDSREytvmsy 155

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568915670 367 EGFPLNK-------------DDIDGIQYLYG 384
Cdd:cd04277  156 NSGYGNGasagggypqtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 338-383 5.09e-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: 5.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915670 338 VAAHEFGHALGLDHSS----------------VPEALMYPLYSYL-------EGFPLNKDDIDGIQYLY 383
Cdd:cd04268   97 TAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFsiqlgdgQKYTIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 479-522 9.34e-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: 9.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568915670   479 FDAIAEIQ-GALHFFKDGWYWKFLNHRGSPlQGPFLTARTWPALP 522
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDP-GYPKLISSFFPGLP 44
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 385-473 2.49e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 385 RGSKPDPRP----PATTTTEPQPTAPPTMCPTIPPtayptvgPTVGPTGAPSPGPTSSPSPGPTGAPsPGPTAPPT-AGS 459
Cdd:PHA02682  92 APACPACAPaapaPAVTCPAPAPACPPATAPTCPP-------PAVCPAPARPAPACPPSTRQCPPAP-PLPTPKPApAAK 163

                         90
                 ....*....|....
gi 568915670 460 SEASTESLSPADNP 473
Cdd:PHA02682 164 PIFLHNQLPPPDYP 177
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 332-383 2.69e-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: 42.12  E-value: 2.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915670 332 GYSLFLVAAHEFGHALGLDHSSVPEA--------------------LMYPL---YSYLEGFPLNKDDIDGIQYLY 383
Cdd:cd00203   93 TKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTkgsFSDGQRKDFSQCDIDQINKLY 167
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 402-430 3.71e-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: 3.71e-04
                          10        20
                  ....*....|....*....|....*....
gi 568915670  402 QPTAPPTMCPTIPPTAYPTVGPTVGPTGA 430
Cdd:pfam04886   5 QPTAQPTVQPTGQPTAQPTDQPTAQPTDA 33
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 329-361 4.07e-04

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 42.36  E-value: 4.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568915670 329 PDQ-GYSLFLVAAHEFGHALGL-DHSSVPEALMYP 361
Cdd:COG5549  175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYF 209
PHA03247 PHA03247
large tegument protein UL36; Provisional
 389-470 5.80e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  389 PDPRPPATTTTEP----QPTAPPTmcPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPGPTAPPTA---GSSE 461
Cdd:PHA03247 2739 PAPPAVPAGPATPggpaRPARPPT--TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAavlAPAA 2816


                  ....*....
gi 568915670  462 ASTESLSPA 470
Cdd:PHA03247 2817 ALPPAASPA 2825
PHA03247 PHA03247
large tegument protein UL36; Provisional
 385-469 7.22e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  385 RGSKPDPRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPS----PGPTAPPTAGSS 460
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGrvavPRFRVPQPAPSR 2986


                  ....*....
gi 568915670  461 EASTESLSP 469
Cdd:PHA03247 2987 EAPASSTPP 2995
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 381-473 7.32e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.79  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670 381 YLYGRGSKPDPRPPAT--TTTEPQPTAPPTMC------PTIPPT--AYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPG 450
Cdd:PHA03269  32 HTSAATQKPDPAPAPHqaASRAPDPAVAPTSAasrkpdLAQAPTpaASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPD 111

                         90       100
                 ....*....|....*....|...
gi 568915670 451 PTAPPTAgsseASTESLSPADNP 473
Cdd:PHA03269 112 AAEAFTS----AAQAHEAPADAG 130
PHA03247 PHA03247
large tegument protein UL36; Provisional
 386-476 1.76e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  386 GSKPDPRPPATTTTEPQPTAP---------PTMCPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPGP---TA 453
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPaaarqaspaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrLT 2784

                          90       100
                  ....*....|....*....|....*..
gi 568915670  454 PPTAGSSEASTESL----SPADNPCNV 476
Cdd:PHA03247 2785 RPAVASLSESRESLpspwDPADPPAAV 2811
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 387-463 2.07e-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: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915670  387 SKPDPRPPATTTTEPQPTAPPTmcPTIPPTAYPTVGPTVGPTGApspgpTSSPSPGPTGAPSPGPTAPPTAGSSEAS 463
Cdd:TIGR00601  75 SKPKTGTGKVAPPAATPTSAPT--PTPSPPASPASGMSAAPASA-----VEEKSPSEESATATAPESPSTSVPSSGS 144
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 393-424 3.30e-03

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: 35.53  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568915670  393 PPATTTTEP--QPTAPPTMCPTIPPTAYPTVGPT 424
Cdd:pfam04886   2 PTAQPTAQPtvQPTGQPTAQPTDQPTAQPTDAPT 35
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
338-377 5.95e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 5.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568915670 338 VAAHEFGHALGLDHSSVPEALMYplysylegFPLNKDDID 377
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMH--------FSNSLEELD 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 386-473 8.23e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915670  386 GSKPDPRPPATTTtePQPTAPPTMCPTIPPTAYPTvgPTVGPTGAPSPGPTSSPSPGPTGAPSPGPTAPPTAGSSEASTE 465
Cdd:PHA03247 2753 GPARPARPPTTAG--PPAPAPPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828


                  ....*...
gi 568915670  466 SLSPADNP 473
Cdd:PHA03247 2829 PPPTSAQP 2836
 
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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