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Conserved domains on  [gi|45553379|ref|NP_996218|]
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ADAM metallopeptidase with thrombospondin type 1 motif A, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1493-1687 1.88e-73

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


:

Pssm-ID: 462559  Cd Length: 200  Bit Score: 243.29  E-value: 1.88e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1493 PRSCADLKEMHGYNKDGNYQLEVRSRMVHIYCHGMNSRTPQEYVNVD--PQENYSIYYEYRTKQTNSCPPESRGHEYY-- 1568
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPsgPQENYSEVYGYRLKNPNECPFNGSRRDDCac 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1569 ---NDQNSGRTHFRKLRLNITDLRIMDNDFKFADS-RGLAQKLGSAGDCYNRIgQCPQGDFSINMKDTDFSIRPGTVWRM 1644
Cdd:pfam08685   81 rqdYPANAGTTTFSKVRLDLTSLRIITNDFTFARTiRGKPVPFGTAGDCYSAA-KCPQGRFSINLTGTGLRVSPDTKWVS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 45553379   1645 HGQYSVMKriSEFDTTTQMRRGFCGGYCGGCYIAPDSGLYLDV 1687
Cdd:pfam08685  160 QGNYAVSK--IHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 455-655 2.37e-73

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: 243.30  E-value: 2.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  455 YTLEVLIAVDNSMKQF-HGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPNINDQ---THSSNEMLKHFCQFI 530
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGlliSGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  531 NQSGYER-------DTAMLITREPICGsvPGKICHMLGLAELGTV-CSSSSCSIVQDTGLPTAFTMAHELGHILNMNHDD 602
Cdd:cd04273   81 KKLNPPNdsdpehhDHAILLTRQDICR--SNGNCDTLGLAPVGGMcSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553379  603 D-DKCMPYVTRQnnnkvlHIMSSVMGIHMHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:cd04273  159 DgNSCGPEGKDG------HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 671-740 2.23e-21

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: 89.33  E-value: 2.23e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553379    671 PGEIYSLDAQCQLSFGNDFGYCP--TDEECKRLWCNRTSGNsneQCASSNLPWADGTPCGsSGHWCQRGKCV 740
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPngDEDVCSKLWCSNPGGS---TCTTKNLPAADGTPCG-NKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 295-394 3.21e-17

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 79.67  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    295 QYNLNVFGRQLHLVLRQDASFVHNHSMTHIRiLKEGEEHpgpeTEAEAEQRHlgCFYSGYVEDDPHSMVSVSLCGGMTGY 374
Cdd:pfam01562   28 SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY-LDGGTGV----ESPPVQTDH--CYYQGHVEGHPDSSVALSTCSGLRGF 100

                           90       100
                   ....*....|....*....|
gi 45553379    375 IKTSFGALLIQPVNRTSSDE 394
Cdd:pfam01562  101 IRTENEEYLIEPLEKYSREE 120
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-806 2.67e-14

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: 68.77  E-value: 2.67e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 45553379     754 WGPWTPFTPCSLTCGGGVQESRRECNQPVPENGGKYCTGSRKKYRSCNTHQCP 806
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1172-1229 1.40e-07

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: 49.51  E-value: 1.40e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553379    1172 CWVLSEWSTCSKSCGTGSQQREAHCYLHNSRVSDDLCnprtkPHLNTLIGICNTESCP 1229
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC-----TGEDVETRACNEQPCP 53
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1355-1405 2.85e-07

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 48.60  E-value: 2.85e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 45553379   1355 WNASDWRRCPADCSEEYQTRDVRC-ESFQGDGVEDKHCDAKKRPSKRRICNN 1405
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvQKGGGSIVPDSECSAQKKPPETQSCNL 52
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 815-911 2.64e-06

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: 48.17  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    815 QQCYAMNGRNM-NIPGVNPDTKW---VPKYEKDA-CKLFCRMDMKVTYFMLKSMVTDGTSCAVD------SFDKCVNGIC 883
Cdd:pfam19236    8 QQCARTDGQPLrSSPGGASFYHWgaaVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSC 87

                           90       100
                   ....*....|....*....|....*...
gi 45553379    884 RPAGCDNELNSIAKLDKCGVCEGRNDTC 911
Cdd:pfam19236   88 RTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1243-1282 3.01e-03

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.43  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 45553379   1243 WVIGEWGECNEWC---EKTRSVSCSHPYGIG------CGSR-KPKDVRKC 1282
Cdd:pfam19030    1 WVAGPWGECSVTCgggVQTRLVQCVQKGGGSivpdseCSAQkKPPETQSC 50
 
Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1493-1687 1.88e-73

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


Pssm-ID: 462559  Cd Length: 200  Bit Score: 243.29  E-value: 1.88e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1493 PRSCADLKEMHGYNKDGNYQLEVRSRMVHIYCHGMNSRTPQEYVNVD--PQENYSIYYEYRTKQTNSCPPESRGHEYY-- 1568
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPsgPQENYSEVYGYRLKNPNECPFNGSRRDDCac 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1569 ---NDQNSGRTHFRKLRLNITDLRIMDNDFKFADS-RGLAQKLGSAGDCYNRIgQCPQGDFSINMKDTDFSIRPGTVWRM 1644
Cdd:pfam08685   81 rqdYPANAGTTTFSKVRLDLTSLRIITNDFTFARTiRGKPVPFGTAGDCYSAA-KCPQGRFSINLTGTGLRVSPDTKWVS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 45553379   1645 HGQYSVMKriSEFDTTTQMRRGFCGGYCGGCYIAPDSGLYLDV 1687
Cdd:pfam08685  160 QGNYAVSK--IHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 455-655 2.37e-73

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: 243.30  E-value: 2.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  455 YTLEVLIAVDNSMKQF-HGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPNINDQ---THSSNEMLKHFCQFI 530
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGlliSGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  531 NQSGYER-------DTAMLITREPICGsvPGKICHMLGLAELGTV-CSSSSCSIVQDTGLPTAFTMAHELGHILNMNHDD 602
Cdd:cd04273   81 KKLNPPNdsdpehhDHAILLTRQDICR--SNGNCDTLGLAPVGGMcSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553379  603 D-DKCMPYVTRQnnnkvlHIMSSVMGIHMHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:cd04273  159 DgNSCGPEGKDG------HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 671-740 2.23e-21

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: 89.33  E-value: 2.23e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553379    671 PGEIYSLDAQCQLSFGNDFGYCP--TDEECKRLWCNRTSGNsneQCASSNLPWADGTPCGsSGHWCQRGKCV 740
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPngDEDVCSKLWCSNPGGS---TCTTKNLPAADGTPCG-NKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 295-394 3.21e-17

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 79.67  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    295 QYNLNVFGRQLHLVLRQDASFVHNHSMTHIRiLKEGEEHpgpeTEAEAEQRHlgCFYSGYVEDDPHSMVSVSLCGGMTGY 374
Cdd:pfam01562   28 SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY-LDGGTGV----ESPPVQTDH--CYYQGHVEGHPDSSVALSTCSGLRGF 100

                           90       100
                   ....*....|....*....|
gi 45553379    375 IKTSFGALLIQPVNRTSSDE 394
Cdd:pfam01562  101 IRTENEEYLIEPLEKYSREE 120
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-806 2.67e-14

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: 68.77  E-value: 2.67e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 45553379     754 WGPWTPFTPCSLTCGGGVQESRRECNQPVPENGGKYCTGSRKKYRSCNTHQCP 806
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 457-655 2.26e-08

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: 56.15  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    457 LEVLIAVDNSMKQFHGEDL---QPYILILMSIVSSIFADASIgnsiRILLVrliSLPNINDQ-----THSSNEMLKHFCQ 528
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNI----RVVLV---GLEIWTDEdkidvSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    529 FINQSGYER---DTAMLITREpicgsvpGKICHMLGLAELGTVCSSSSCSIVQDTGLPT----AFTMAHELGHILNMNHD 601
Cdd:pfam01421   76 WRQEYLKKRkphDVAQLLSGV-------EFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesfAVTMAHELGHNLGMQHD 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553379    602 DDD---KCMPyvtrqnnnKVLHIMSSVMGiHMHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:pfam01421  149 DFNggcKCPP--------GGGCIMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACL 196
TSP_1 pfam00090
Thrombospondin type 1 domain;
755-805 3.60e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 3.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 45553379    755 GPWTPFTPCSLTCGGGVQESRRECNQPVPenGGKYCTGSRKKYRSCNTHQC 805
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1172-1229 1.40e-07

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: 49.51  E-value: 1.40e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553379    1172 CWVLSEWSTCSKSCGTGSQQREAHCYLHNSRVSDDLCnprtkPHLNTLIGICNTESCP 1229
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC-----TGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1355-1405 2.85e-07

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: 48.60  E-value: 2.85e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 45553379   1355 WNASDWRRCPADCSEEYQTRDVRC-ESFQGDGVEDKHCDAKKRPSKRRICNN 1405
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvQKGGGSIVPDSECSAQKKPPETQSCNL 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1173-1215 9.81e-07

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: 47.45  E-value: 9.81e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45553379   1173 WVLSEWSTCSKSCGTGSQQREAHC--YLHNSRVSDDLCNPRTKPH 1215
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqKGGGSIVPDSECSAQKKPP 45
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 815-911 2.64e-06

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: 48.17  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    815 QQCYAMNGRNM-NIPGVNPDTKW---VPKYEKDA-CKLFCRMDMKVTYFMLKSMVTDGTSCAVD------SFDKCVNGIC 883
Cdd:pfam19236    8 QQCARTDGQPLrSSPGGASFYHWgaaVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSC 87

                           90       100
                   ....*....|....*....|....*...
gi 45553379    884 RPAGCDNELNSIAKLDKCGVCEGRNDTC 911
Cdd:pfam19236   88 RTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1243-1282 3.01e-03

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: 37.43  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 45553379   1243 WVIGEWGECNEWC---EKTRSVSCSHPYGIG------CGSR-KPKDVRKC 1282
Cdd:pfam19030    1 WVAGPWGECSVTCgggVQTRLVQCVQKGGGSivpdseCSAQkKPPETQSC 50
 
Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1493-1687 1.88e-73

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


Pssm-ID: 462559  Cd Length: 200  Bit Score: 243.29  E-value: 1.88e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1493 PRSCADLKEMHGYNKDGNYQLEVRSRMVHIYCHGMNSRTPQEYVNVD--PQENYSIYYEYRTKQTNSCPPESRGHEYY-- 1568
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPsgPQENYSEVYGYRLKNPNECPFNGSRRDDCac 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379   1569 ---NDQNSGRTHFRKLRLNITDLRIMDNDFKFADS-RGLAQKLGSAGDCYNRIgQCPQGDFSINMKDTDFSIRPGTVWRM 1644
Cdd:pfam08685   81 rqdYPANAGTTTFSKVRLDLTSLRIITNDFTFARTiRGKPVPFGTAGDCYSAA-KCPQGRFSINLTGTGLRVSPDTKWVS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 45553379   1645 HGQYSVMKriSEFDTTTQMRRGFCGGYCGGCYIAPDSGLYLDV 1687
Cdd:pfam08685  160 QGNYAVSK--IHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 455-655 2.37e-73

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: 243.30  E-value: 2.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  455 YTLEVLIAVDNSMKQF-HGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPNINDQ---THSSNEMLKHFCQFI 530
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGlliSGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  531 NQSGYER-------DTAMLITREPICGsvPGKICHMLGLAELGTV-CSSSSCSIVQDTGLPTAFTMAHELGHILNMNHDD 602
Cdd:cd04273   81 KKLNPPNdsdpehhDHAILLTRQDICR--SNGNCDTLGLAPVGGMcSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553379  603 D-DKCMPYVTRQnnnkvlHIMSSVMGIHMHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:cd04273  159 DgNSCGPEGKDG------HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 456-648 1.33e-25

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: 105.97  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  456 TLEVLIAVDNSMKQF---HGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPN---INDQTHSSNEMLKHFCQF 529
Cdd:cd04267    2 EIELVVVADHRMVSYfnsDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGeqfAPPIDSDASNTLNSFSFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  530 INQSGYERDTAMLITREPICGsvpgkiCHMLGLAELGTVCSSSSCS-IVQDTGLP--TAFTMAHELGHILNMNHDDDDKC 606
Cdd:cd04267   82 RAEGPIRHDNAVLLTAQDFIE------GDILGLAYVGSMCNPYSSVgVVEDTGFTllTALTMAHELGHNLGAEHDGGDEL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 45553379  607 mPYVTRQNNNkvlHIMSSVMGiHMHPWSWSKCSRHFVSEFLE 648
Cdd:cd04267  156 -AFECDGGGN---YIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 671-740 2.23e-21

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: 89.33  E-value: 2.23e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553379    671 PGEIYSLDAQCQLSFGNDFGYCP--TDEECKRLWCNRTSGNsneQCASSNLPWADGTPCGsSGHWCQRGKCV 740
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPngDEDVCSKLWCSNPGGS---TCTTKNLPAADGTPCG-NKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 295-394 3.21e-17

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 79.67  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    295 QYNLNVFGRQLHLVLRQDASFVHNHSMTHIRiLKEGEEHpgpeTEAEAEQRHlgCFYSGYVEDDPHSMVSVSLCGGMTGY 374
Cdd:pfam01562   28 SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY-LDGGTGV----ESPPVQTDH--CYYQGHVEGHPDSSVALSTCSGLRGF 100

                           90       100
                   ....*....|....*....|
gi 45553379    375 IKTSFGALLIQPVNRTSSDE 394
Cdd:pfam01562  101 IRTENEEYLIEPLEKYSREE 120
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 457-655 1.04e-14

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: 74.19  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  457 LEVLIAVDNSMKQFHGEDLQP---YILILMSIVSSIFADASIgnsiRILLVRL--------ISLpnindqTHSSNEMLKH 525
Cdd:cd04269    3 VELVVVVDNSLYKKYGSNLSKvrqRVIEIVNIVDSIYRPLNI----RVVLVGLeiwtdkdkISV------SGDAGETLNR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  526 FCQFINQSGYER---DTAMLITREPICGsvpgkicHMLGLAELGTV-CSSSSCSIVQDTG---LPTAFTMAHELGHILNM 598
Cdd:cd04269   73 FLDWKRSNLLPRkphDNAQLLTGRDFDG-------NTVGLAYVGGMcSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGM 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553379  599 NHDDDD------KCmpyvtrqnnnkvlhIMSSVMGIhmHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:cd04269  146 EHDDGGctcgrsTC--------------IMAPSPSS--LTDAFSNCSYEDYQKFLSRGGGQCL 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-806 2.67e-14

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: 68.77  E-value: 2.67e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 45553379     754 WGPWTPFTPCSLTCGGGVQESRRECNQPVPENGGKYCTGSRKKYRSCNTHQCP 806
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 458-656 3.54e-11

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 64.68  E-value: 3.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  458 EVLIAVDNSMKQ--FHGEDLQPYILILMSIVSSIFADASiGNSIRILLVRLI---------SLPNINDQTHSSNEMLKHF 526
Cdd:cd04272    4 ELFVVVDYDHQSefFSNEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITiskdpdfepYIHPINYGYIDAAETLENF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  527 CQFINQSGYER--DTAMLITREPICGSVPGKICH-MLGLAELGTVCSSSSCSIVQDTglPTAF----TMAHELGHILNMN 599
Cdd:cd04272   83 NEYVKKKRDYFnpDVVFLVTGLDMSTYSGGSLQTgTGGYAYVGGACTENRVAMGEDT--PGSYygvyTMTHELAHLLGAP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553379  600 HDDDDKCmPYVTRQNNNKVL-----HIMSSVM-GIHMHpwSWSKCSRHFVSEFLEKTDKSCLE 656
Cdd:cd04272  161 HDGSPPP-SWVKGHPGSLDCpwddgYIMSYVVnGERQY--RFSQCSQRQIRNVFRRLGASCLH 220
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 456-647 2.12e-08

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: 55.22  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  456 TLEVLIAVDNSMkqFHGEDLQPYILILMSIVSSIFADAsigNSIRILLVrlislpNINDQTHssnemlkhfcqfinqsgy 535
Cdd:cd00203    2 VIPYVVVADDRD--VEEENLSAQIQSLILIAMQIWRDY---LNIRFVLV------GVEIDKA------------------ 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379  536 erDTAMLITREPICGSVpgkichmLGLAELGTVCSSSSCSIV-QDTGLPT---AFTMAHELGHILNMNHDDDDKC---MP 608
Cdd:cd00203   53 --DIAILVTRQDFDGGT-------GGWAYLGRVCDSLRGVGVlQDNQSGTkegAQTIAHELGHALGFYHDHDRKDrddYP 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45553379  609 YVTRQNNNKV---LHIMS--SVMGIHMHPWSWSKCSRHFVSEFL 647
Cdd:cd00203  124 TIDDTLNAEDddyYSVMSytKGSFSDGQRKDFSQCDIDQINKLY 167
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 457-655 2.26e-08

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: 56.15  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    457 LEVLIAVDNSMKQFHGEDL---QPYILILMSIVSSIFADASIgnsiRILLVrliSLPNINDQ-----THSSNEMLKHFCQ 528
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNI----RVVLV---GLEIWTDEdkidvSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    529 FINQSGYER---DTAMLITREpicgsvpGKICHMLGLAELGTVCSSSSCSIVQDTGLPT----AFTMAHELGHILNMNHD 601
Cdd:pfam01421   76 WRQEYLKKRkphDVAQLLSGV-------EFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesfAVTMAHELGHNLGMQHD 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553379    602 DDD---KCMPyvtrqnnnKVLHIMSSVMGiHMHPWSWSKCSRHFVSEFLEKTDKSCL 655
Cdd:pfam01421  149 DFNggcKCPP--------GGGCIMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACL 196
TSP_1 pfam00090
Thrombospondin type 1 domain;
755-805 3.60e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 3.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 45553379    755 GPWTPFTPCSLTCGGGVQESRRECNQPVPenGGKYCTGSRKKYRSCNTHQC 805
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 755-805 8.16e-08

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: 50.36  E-value: 8.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 45553379    755 GPWTPFTPCSLTCGGGVQESRRECNQPvPENGGKYCTGSRKKyRSCNTHQC 805
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1172-1229 1.40e-07

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: 49.51  E-value: 1.40e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553379    1172 CWVLSEWSTCSKSCGTGSQQREAHCYLHNSRVSDDLCnprtkPHLNTLIGICNTESCP 1229
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC-----TGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1355-1405 2.85e-07

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: 48.60  E-value: 2.85e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 45553379   1355 WNASDWRRCPADCSEEYQTRDVRC-ESFQGDGVEDKHCDAKKRPSKRRICNN 1405
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvQKGGGSIVPDSECSAQKKPPETQSCNL 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1173-1215 9.81e-07

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: 47.45  E-value: 9.81e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45553379   1173 WVLSEWSTCSKSCGTGSQQREAHC--YLHNSRVSDDLCNPRTKPH 1215
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqKGGGSIVPDSECSAQKKPP 45
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 815-911 2.64e-06

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: 48.17  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    815 QQCYAMNGRNM-NIPGVNPDTKW---VPKYEKDA-CKLFCRMDMKVTYFMLKSMVTDGTSCAVD------SFDKCVNGIC 883
Cdd:pfam19236    8 QQCARTDGQPLrSSPGGASFYHWgaaVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSC 87

                           90       100
                   ....*....|....*....|....*...
gi 45553379    884 RPAGCDNELNSIAKLDKCGVCEGRNDTC 911
Cdd:pfam19236   88 RTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
459-616 7.70e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 48.57  E-value: 7.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    459 VLIAVDNS-MKQFHGEDLQPYILILMSIVSSIFADASignSIRILLVRLISLPN------INDQTHSSNEMLKHFCQFIN 531
Cdd:pfam13688    7 LLVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDStcpytpPACSTGDSSDRLSEFQDFSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    532 QSGYERDTAMLITREPICGSVpgkichmlGLAELGT----------VCSSSSCSIVQDTGLpTAFTMAHELGHILNMNHD 601
Cdd:pfam13688   84 WRGTQNDDLAYLFLMTNCSGG--------GLAWLGQlcnsgsagsvSTRVSGNNVVVSTAT-EWQVFAHEIGHNFGAVHD 154

                          170       180
                   ....*....|....*....|
gi 45553379    602 DDDK-----CMPYVTRQNNN 616
Cdd:pfam13688  155 CDSStssqcCPPSNSTCPAG 174
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-805 3.29e-04

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: 40.13  E-value: 3.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 45553379    758 TPFTPCSLTCGGGVQESRRECNQPVP--ENGGKYCTGSRK--KYRSCNTHQC 805
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 479-648 5.07e-04

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: 372637  Cd Length: 193  Bit Score: 43.00  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    479 ILILMSIVSSIFADASIGNSIRillvrLISLPNINDQTHSSN-------------EMLKHFCQFINQSGYerDTAMLITR 545
Cdd:pfam13574    7 LVNVVNRVNQIYEPDDININGG-----LVNPGEIPATTSASDsgnnycnspttivRRLNFLSQWRGEQDY--CLAHLVTM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    546 EPICGSVpgkichmLGLAELGTVCSSSSCSIVQDTGLPTAFT-------------MAHELGHILNMNHDDD--------- 603
Cdd:pfam13574   80 GTFSGGE-------LGLAYVGQICQKGASSPKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsqyassgc 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 45553379    604 DKCMPYVTRQNNNKVLHIMSSVMGIHMhpwsWSKCSRHFVSEFLE 648
Cdd:pfam13574  153 ERNAATSVCSANGSFIMNPASKSNNDL----FSPCSISLICDVLG 193
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1243-1282 3.01e-03

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: 37.43  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 45553379   1243 WVIGEWGECNEWC---EKTRSVSCSHPYGIG------CGSR-KPKDVRKC 1282
Cdd:pfam19030    1 WVAGPWGECSVTCgggVQTRLVQCVQKGGGSivpdseCSAQkKPPETQSC 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1176-1192 3.58e-03

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: 37.26  E-value: 3.58e-03
                           10
                   ....*....|....*..
gi 45553379   1176 SEWSTCSKSCGTGSQQR 1192
Cdd:pfam19028    7 SEWSECSVTCGGGVQTR 23
Salp15 pfam12115
Salivary protein of 15kDa inhibits CD4+ T cell activation; This is a family of 15kDa salivary ...
 696-745 3.74e-03

Salivary protein of 15kDa inhibits CD4+ T cell activation; This is a family of 15kDa salivary proteins from Acari Arachnids that is induced on feeding and assists the parasite to remain attached to its arthropod host. By repressing calcium fluxes triggered by TCR engagement, Salp15 inhibits CD4+ T cell activation. Salp15 shows weak similarity to Inhibin A, a member of the TGF-beta superfamily that inhibits the production of cytokines and the proliferation of T cells.


Pssm-ID: 314916  Cd Length: 112  Bit Score: 38.91  E-value: 3.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 45553379    696 EECKRLwCNRTSgNSNEQCASSNLPwaDGTPCGSSGHWCQRGKCVSNKHG 745
Cdd:pfam12115   66 KNCTFT-CGKHN-NGGTNITLRQLP--DGTPCGPQGKTCKNGKCVGHVPS 111
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 478-601 3.89e-03

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: 38.89  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553379    478 YILILMSIVSSIFADASignSIRILLVRLISLPNINDQTHSSN--EMLKHFCQF----INQSGYerDTAMLITREPICGS 551
Cdd:pfam13582    2 RIVSLVNRANTIYERDL---GIRLQLAAIIITTSADTPYTSSDalEILDELQEVndtrIGQYGY--DLGHLFTGRDGGGG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 45553379    552 vpgkichmLGLAELGTVCSSSSCSIV----QDTGLPTAFTMAHELGHILNMNHD 601
Cdd:pfam13582   77 --------GGIAYVGGVCNSGSKFGVnsgsGPVGDTGADTFAHEIGHNFGLNHT 122
 
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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