NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568913826|ref|XP_006498167|]
View 

A disintegrin and metalloproteinase with thrombospondin motifs 13 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 82-286 6.71e-75

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 244.07  E-value: 6.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  82 LHLELLVAVGPDVSR-AHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWS 160
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 161 QTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDgap 240
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHD--- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568913826 241 GSGSTCKAS---GHVMAADGaTPTGGTLEWSACSQRQLQHLLSTGQMHC 286
Cdd:cd04273  158 GDGNSCGPEgkdGHIMSPTL-GANTGPFTWSKCSRRYLTSFLDTGDGNC 205
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 446-560 1.86e-60

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 201.09  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  446 TQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLS 525
Cdd:pfam19236   1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568913826  526 LCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTC 560
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 563-684 3.87e-51

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 175.07  E-value: 3.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  563 RNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVR-IQGHYIVAGKTSISPNTTYPSLLEDYrVEYRVtltedQ 641
Cdd:pfam05986   2 VSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR-----S 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568913826  642 LPHLEEIHIRGPVRDDIEIQVYRRyggeYGDLTHPDITFSYFQ 684
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQ----YGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 306-376 5.69e-17

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 75.84  E-value: 5.69e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568913826  306 PGLYYSADDQCRVAFGSGAVACtfSREGLDVCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKARC 376
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC--PNGDEDVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 392-444 2.99e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.99e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568913826   392 WSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACE 444
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 751-809 2.02e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568913826  751 WVAGDFSPCSVSCGGGLRERSLRCVETQDGflKTLPPARCRAVAQQPaaEVENCNSQPC 809
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKPP--ETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 82-286 6.71e-75

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 244.07  E-value: 6.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  82 LHLELLVAVGPDVSR-AHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWS 160
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 161 QTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDgap 240
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHD--- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568913826 241 GSGSTCKAS---GHVMAADGaTPTGGTLEWSACSQRQLQHLLSTGQMHC 286
Cdd:cd04273  158 GDGNSCGPEgkdGHIMSPTL-GANTGPFTWSKCSRRYLTSFLDTGDGNC 205
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 446-560 1.86e-60

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 201.09  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  446 TQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLS 525
Cdd:pfam19236   1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568913826  526 LCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTC 560
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 563-684 3.87e-51

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 175.07  E-value: 3.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  563 RNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVR-IQGHYIVAGKTSISPNTTYPSLLEDYrVEYRVtltedQ 641
Cdd:pfam05986   2 VSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR-----S 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568913826  642 LPHLEEIHIRGPVRDDIEIQVYRRyggeYGDLTHPDITFSYFQ 684
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQ----YGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 306-376 5.69e-17

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 75.84  E-value: 5.69e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568913826  306 PGLYYSADDQCRVAFGSGAVACtfSREGLDVCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKARC 376
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC--PNGDEDVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 392-444 2.99e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.99e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568913826   392 WSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACE 444
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 126-291 1.21e-11

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 64.63  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  126 FQVHLVKLITLSDsESTPNITANITSSLMSVCEWSQTI----NPHDdrdpsHADLILYITRfdlelpdgNQQVRGVTQLG 201
Cdd:pfam01421  44 IRVVLVGLEIWTD-EDKIDVSGDANDTLRNFLKWRQEYlkkrKPHD-----VAQLLSGVEF--------GGTTVGAAYVG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  202 GACSLSWSCLITEDTGFD---LGVTIAHEIGHSFGLDHDgAPGSGSTCKASGH-VMAAdgATPTGGTLEWSACSQRQLQH 277
Cdd:pfam01421 110 GMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHD-DFNGGCKCPPGGGcIMNP--SAGSSFPRKFSNCSQEDFEQ 186

                         170
                  ....*....|....
gi 568913826  278 LLSTGQMHCFQDPP 291
Cdd:pfam01421 187 FLTKQKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 751-809 2.02e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568913826  751 WVAGDFSPCSVSCGGGLRERSLRCVETQDGflKTLPPARCRAVAQQPaaEVENCNSQPC 809
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
393-443 1.49e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 54.35  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568913826  393 SSWGPHSPCSRSCGGGVITRRRWCNNPRPafGGRACVGEDLQAKMCNTQAC 443
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-810 3.53e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 3.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568913826   754 GDFSPCSVSCGGGLRERSLRCVetqdGFLKTLPPARCravaQQPAAEVENCNSQPCP 810
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCC----SPPPQNGGGPC----TGEDVETRACNEQPCP 53
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
167-236 3.69e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 167 DDRDPSHADLILYITRFDLELPDGNQqVRGVTQLGG-ACSLSWSCLITEDTGFDLG---------VTIAHEIGHSFGLDH 236
Cdd:COG1913   61 SRLKEEDGDKVLGVTDVDLYAPGLNF-VFGLAYLGGrVAVVSTARLRPEFYGLPPDeelflervlKEAVHELGHLFGLGH 139
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 82-286 6.71e-75

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 244.07  E-value: 6.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  82 LHLELLVAVGPDVSR-AHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWS 160
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 161 QTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDgap 240
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHD--- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568913826 241 GSGSTCKAS---GHVMAADGaTPTGGTLEWSACSQRQLQHLLSTGQMHC 286
Cdd:cd04273  158 GDGNSCGPEgkdGHIMSPTL-GANTGPFTWSKCSRRYLTSFLDTGDGNC 205
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 446-560 1.86e-60

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 201.09  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  446 TQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLS 525
Cdd:pfam19236   1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568913826  526 LCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTC 560
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 563-684 3.87e-51

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 175.07  E-value: 3.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  563 RNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVR-IQGHYIVAGKTSISPNTTYPSLLEDYrVEYRVtltedQ 641
Cdd:pfam05986   2 VSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR-----S 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568913826  642 LPHLEEIHIRGPVRDDIEIQVYRRyggeYGDLTHPDITFSYFQ 684
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQ----YGKGTNPGITYEYFI 114
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 96-280 3.09e-24

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 100.96  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  96 RAHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWSQtinphddRDPSHAD 175
Cdd:cd04267   18 NSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWRA-------EGPIRHD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 176 LILYITRFDLelpdGNQQVRGVTQLGGACSLSWSCLITEDTGFDL--GVTIAHEIGHSFGLDHDGAPGSGSTC-KASGHV 252
Cdd:cd04267   91 NAVLLTAQDF----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGDELAFECdGGGNYI 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 568913826 253 MA--ADGATPTggtlEWSACSQRQLQHLLS 280
Cdd:cd04267  167 MApvDSGLNSY----RFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 144-289 6.74e-19

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 85.74  E-value: 6.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 144 NITANITSSLMSVCEWSQTI----NPHDdrdpsHADLILYITrfdlelPDGNqqVRGVTQLGGACSLSWSCLITEDTG-- 217
Cdd:cd04269   61 SVSGDAGETLNRFLDWKRSNllprKPHD-----NAQLLTGRD------FDGN--TVGLAYVGGMCSPKYSGGVVQDHSrn 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568913826 218 -FDLGVTIAHEIGHSFGLDHDgapGSGSTCKASGHVMAadgATPTGGTLEWSACSQRQLQHLLSTGQMHCFQD 289
Cdd:cd04269  128 lLLFAVTMAHELGHNLGMEHD---DGGCTCGRSTCIMA---PSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 306-376 5.69e-17

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 75.84  E-value: 5.69e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568913826  306 PGLYYSADDQCRVAFGSGAVACtfSREGLDVCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKARC 376
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC--PNGDEDVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 392-444 2.99e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.99e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568913826   392 WSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACE 444
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 82-279 3.70e-14

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 72.77  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  82 LHLELLVAVGPDVSRaHQEDTERY-----VLTN-LNIGSELLRNPslGVQFqvhLVKLITLSDSESTPNITANITSSLMS 155
Cdd:cd04272    1 VYPELFVVVDYDHQS-EFFSNEQLirylaVMVNaANLRYRDLKSP--RIRL---LLVGITISKDPDFEPYIHPINYGYID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 156 VCEWSQTINPH--DDRDPSHADLILYITRFDLELPDG---NQQVRGVTQLGGACSlSWSCLITEDT-GFDLGV-TIAHEI 228
Cdd:cd04272   75 AAETLENFNEYvkKKRDYFNPDVVFLVTGLDMSTYSGgslQTGTGGYAYVGGACT-ENRVAMGEDTpGSYYGVyTMTHEL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 229 GHSFGLDHDGAPGSGS--------TCKAS-GHVMAADGATPTGgtLEWSACSQRQLQHLL 279
Cdd:cd04272  154 AHLLGAPHDGSPPPSWvkghpgslDCPWDdGYIMSYVVNGERQ--YRFSQCSQRQIRNVF 211
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 126-291 1.21e-11

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 64.63  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  126 FQVHLVKLITLSDsESTPNITANITSSLMSVCEWSQTI----NPHDdrdpsHADLILYITRfdlelpdgNQQVRGVTQLG 201
Cdd:pfam01421  44 IRVVLVGLEIWTD-EDKIDVSGDANDTLRNFLKWRQEYlkkrKPHD-----VAQLLSGVEF--------GGTTVGAAYVG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  202 GACSLSWSCLITEDTGFD---LGVTIAHEIGHSFGLDHDgAPGSGSTCKASGH-VMAAdgATPTGGTLEWSACSQRQLQH 277
Cdd:pfam01421 110 GMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHD-DFNGGCKCPPGGGcIMNP--SAGSSFPRKFSNCSQEDFEQ 186

                         170
                  ....*....|....
gi 568913826  278 LLSTGQMHCFQDPP 291
Cdd:pfam01421 187 FLTKQKGACLFNKP 200
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 86-259 6.28e-11

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 62.64  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826   86 LLVAVGPDVSRAHQEDTE--RYVLTNLNIGSELLRNpSLGVQFQVHLVKLITLSDSESTPnitANITSSLMSVCEWSQtI 163
Cdd:pfam13583   7 VAVATDCTYSASFGSVDElrANINATVTTANEVYGR-DFNVSLALISDRDVIYTDSSTDS---FNADCSGGDLGNWRL-A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  164 NPHDDRDPSHADLILYITRFDlelpdGNQQVRGVTQLGGACSLSW-----SCLITEDTGFDlgvTIAHEIGHSFGLDHD- 237
Cdd:pfam13583  82 TLTSWRDSLNYDLAYLTLMTG-----PSGQNVGVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTFGAVHDc 153

                         170       180
                  ....*....|....*....|....*
gi 568913826  238 ---GAPGSGSTCKASGHVMAADGAT 259
Cdd:pfam13583 154 ssqGEGLSSSTEDGSGQTIMSYAST 178
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 751-809 2.02e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568913826  751 WVAGDFSPCSVSCGGGLRERSLRCVETQDGflKTLPPARCRAVAQQPaaEVENCNSQPC 809
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
393-443 1.49e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 54.35  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568913826  393 SSWGPHSPCSRSCGGGVITRRRWCNNPRPafGGRACVGEDLQAKMCNTQAC 443
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 170-279 2.99e-09

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: 57.15  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 170 DPSHADLILYITRFDLELPDGnqqvrGVTQLGGACSLSWSCLITEDTGFD---LGVTIAHEIGHSFGLDHDGAPGSG--- 243
Cdd:cd00203   48 EIDKADIAILVTRQDFDGGTG-----GWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRddy 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568913826 244 --------STCKASGHVMAA-DGATPTGGTLEWSACSQRQLQHLL 279
Cdd:cd00203  123 ptiddtlnAEDDDYYSVMSYtKGSFSDGQRKDFSQCDIDQINKLY 167
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 122-237 9.40e-08

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 51.60  E-value: 9.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  122 LGVQFQVhlVKLITLSDSeSTPNITANITSSLMSVCEWSQTINPHDDRDPSHAdlilyitrFDLELPDGNQqvrGVTQLG 201
Cdd:pfam13582  18 LGIRLQL--AAIIITTSA-DTPYTSSDALEILDELQEVNDTRIGQYGYDLGHL--------FTGRDGGGGG---GIAYVG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913826  202 GAC------SLSWSCLITEDTGFDlgvTIAHEIGHSFGLDHD 237
Cdd:pfam13582  84 GVCnsgskfGVNSGSGPVGDTGAD---TFAHEIGHNFGLNHT 122
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 393-443 4.63e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 44.58  E-value: 4.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568913826  393 SSWGPHSPCSRSCGGGVITRRRWCNNPrPAFGGRACvGEDLQAKMCNTQAC 443
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
195-257 2.87e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.87  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826  195 RGVTQLGGACSLSWSCLITEDTGFDLGV--------TIAHEIGHSFGLDHD--------GAPGSGSTCKASGH-VMAADG 257
Cdd:pfam13688 104 GGLAWLGQLCNSGSAGSVSTRVSGNNVVvstatewqVFAHEIGHNFGAVHDcdsstssqCCPPSNSTCPAGGRyIMNPSS 183
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-810 3.53e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 3.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568913826   754 GDFSPCSVSCGGGLRERSLRCVetqdGFLKTLPPARCravaQQPAAEVENCNSQPCP 810
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCC----SPPPQNGGGPC----TGEDVETRACNEQPCP 53
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
167-236 3.69e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913826 167 DDRDPSHADLILYITRFDLELPDGNQqVRGVTQLGG-ACSLSWSCLITEDTGFDLG---------VTIAHEIGHSFGLDH 236
Cdd:COG1913   61 SRLKEEDGDKVLGVTDVDLYAPGLNF-VFGLAYLGGrVAVVSTARLRPEFYGLPPDeelflervlKEAVHELGHLFGLGH 139
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 213-242 4.17e-04

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: 41.81  E-value: 4.17e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 568913826 213 TEDTGFDLGVTIAHEIGHSFGLDHDGAPGS 242
Cdd:cd04278  100 SDSGGTDLFSVAAHEIGHALGLGHSSDPDS 129
TSP_1 pfam00090
Thrombospondin type 1 domain;
754-809 1.95e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.01  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568913826  754 GDFSPCSVSCGGGLRERSLRCVETQDGflktlpPARCRAvaqqPAAEVENCNSQPC 809
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPG------GEPCTG----DDIETQACKMDKC 49
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 218-245 2.43e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 40.40  E-value: 2.43e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568913826 218 FDLGVTIAHEIGHSFGLDH---DGAPGSGST 245
Cdd:cd04275  135 YNLGDTATHEVGHWLGLYHtfqGGSPCCTTG 165
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 217-242 2.69e-03

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: 39.52  E-value: 2.69e-03
                          10        20
                  ....*....|....*....|....*.
gi 568913826  217 GFDLGVTIAHEIGHSFGLDHDGAPGS 242
Cdd:pfam00413 105 GINLFLVAAHEIGHALGLGHSSDPGA 130
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 171-236 3.94e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.20  E-value: 3.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913826 171 PSHADLILYITRFDLeLPDGNQQVRGVTQLG-GACSLSWSCLITEDTGFDLGV---------TIAHEIGHSFGLDH 236
Cdd:cd11375   65 PPDADCVLGVTDVDL-YEPGLNFVFGLADGGsGVAVVSTARLRPEFYGLPPDEglflerllkEAVHELGHLFGLDH 139
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH