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Conserved domains on  [gi|157427675|ref|NP_005090|]
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A disintegrin and metalloproteinase with thrombospondin motifs 4 isoform 1 preproprotein [Homo sapiens]

Protein Classification

Graphical summary

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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) ...
 218-425 3.82e-106

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: 324.96  E-value: 3.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157427675 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273  161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 687-802 1.78e-34

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: 127.31  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  687 KQSGSFRKFR-YGYNNVVTIPAGATHILVRQQGNPGHrsiYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVsLRYSGAT 765
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSFT---HLAVKNVQGKYILNGKGSISLNPTYPSLLGTV-LEYRRSL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 157427675  766 AASETLSGHGPLAQPLTLQVL-VAGNPQDTRLRYSFFV 802
Cdd:pfam05986  77 PALEELHAPGPTQEDLEIQVLrQYGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 439-507 3.23e-23

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: 93.56  E-value: 3.23e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 531-575 1.09e-11

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: 60.29  E-value: 1.09e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157427675   531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209   9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-181 4.04e-10

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 58.48  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562   1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157427675  132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562  81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 578-685 1.04e-08

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: 53.94  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236   1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157427675  648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236  76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 218-425 3.82e-106

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: 324.96  E-value: 3.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157427675 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273  161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 687-802 1.78e-34

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: 127.31  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  687 KQSGSFRKFR-YGYNNVVTIPAGATHILVRQQGNPGHrsiYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVsLRYSGAT 765
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSFT---HLAVKNVQGKYILNGKGSISLNPTYPSLLGTV-LEYRRSL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 157427675  766 AASETLSGHGPLAQPLTLQVL-VAGNPQDTRLRYSFFV 802
Cdd:pfam05986  77 PALEELHAPGPTQEDLEIQVLrQYGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 439-507 3.23e-23

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: 93.56  E-value: 3.23e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-428 1.40e-17

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: 81.96  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpvslvvtrlVILGSGE---EGPQ--VGPSAAQTL 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNIR----------VVLVGLEiwtDEDKidVSGDANDTL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  290 RSFCAW-QRGLNTPEDsdpdhFDTAILFTRQDLCGVSTcdtlGMADVGTVCDPARSCAIVED---DGLQSAFTAAHELGH 365
Cdd:pfam01421  71 RNFLKWrQEYLKKRKP-----HDVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGH 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427675  366 VFNMLHDNSKP---CISLNGPlstsrhVMAPVMAHVDPEEpWSPCSARFITDFLDNGYGHCLLDKP 428
Cdd:pfam01421 142 NLGMQHDDFNGgckCPPGGGC------IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 531-575 1.09e-11

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: 60.29  E-value: 1.09e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157427675   531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209   9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-181 4.04e-10

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: 58.48  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562   1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157427675  132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562  81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 578-685 1.04e-08

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: 53.94  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236   1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157427675  648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236  76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ACR smart00608
ADAM Cysteine-Rich Domain;
438-509 8.36e-08

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 51.98  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   438 FPGKDYDADRQCQLTFGPDSR----HCPQL-----------------PPPCAA-------LWCSG--------------- 474
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKvapdSCYEElntkgdrfgncgrengtYIPCAPedvkcgkLQCTNvselpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 157427675   475 -HLNGHaMCQTKHSP---------WADGTPCGPAQACMGGRCLHM 509
Cdd:smart00608  94 sNIGGL-VCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 531-574 2.67e-05

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: 42.27  E-value: 2.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157427675  531 DCSRTCGGGVQFSSRDCTRPvPRNGGKYCeGRRTRFRSCNTEDC 574
Cdd:pfam19028  11 ECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
490-659 3.13e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 44.66  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   490 ADGTPCGPAQA-CMGGRCLHMDQlQdfnipqaggwgpwgpwgdCSRTCGGGVQFSSRDCTRPVPRNGGK--YCEGRRTRF 566
Cdd:smart00608   1 QDGTPCDNGQGyCYNGRCPTRDN-Q------------------CQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   567 RSCNTED-------CPTGSALT-FREEQCAAYNHRTDlfksfpgpmdwvprytgvapqdqckLTCqaQALGYYYVLEP-- 636
Cdd:smart00608  62 IPCAPEDvkcgklqCTNVSELPlLGEHATVIYSNIGG-------------------------LVC--WSLDYHLGTDPdi 114

                          170       180
                   ....*....|....*....|....
gi 157427675   637 -RVVDGTPCSPDssSVCVQGRCIH 659
Cdd:smart00608 115 gMVKDGTKCGPG--KVCINGQCVD 136
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 218-425 3.82e-106

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: 324.96  E-value: 3.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157427675 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273  161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 218-417 5.78e-38

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: 140.25  E-value: 5.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 218 RFVETLVVADDKM---AAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCA 294
Cdd:cd04267    1 REIELVVVADHRMvsyFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 295 WQRGlntpedsDPDHFDTAILFTRQDLCGvstCDTLGMADVGTVCDPARSCAIVEDDG--LQSAFTAAHELGHVFNMLHD 372
Cdd:cd04267   81 WRAE-------GPIRHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157427675 373 nSKPCISLNGPlSTSRHVMAPVmahVDPEEP--WSPCSARFITDFLD 417
Cdd:cd04267  151 -GGDELAFECD-GGGNYIMAPV---DSGLNSyrFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 687-802 1.78e-34

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: 127.31  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  687 KQSGSFRKFR-YGYNNVVTIPAGATHILVRQQGNPGHrsiYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVsLRYSGAT 765
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSFT---HLAVKNVQGKYILNGKGSISLNPTYPSLLGTV-LEYRRSL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 157427675  766 AASETLSGHGPLAQPLTLQVL-VAGNPQDTRLRYSFFV 802
Cdd:pfam05986  77 PALEELHAPGPTQEDLEIQVLrQYGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 439-507 3.23e-23

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: 93.56  E-value: 3.23e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 218-426 4.21e-23

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: 97.69  E-value: 4.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpVSLVvtrLVILGSGEEGPQVGPSAAQTLRSFCA 294
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNIR--VVLV---GLEIWTDKDKISVSGDAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 295 WQRglntpEDSDPDHF-DTAILFTRQDLCGvstcDTLGMADVGTVCDPARSCAIVEDDG---LQSAFTAAHELGHVFNML 370
Cdd:cd04269   76 WKR-----SNLLPRKPhDNAQLLTGRDFDG----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427675 371 HDNS------KPCIslngplstsrhvMAPVMahVDPEEPWSPCSARFITDFLDNGYGHCLLD 426
Cdd:cd04269  147 HDDGgctcgrSTCI------------MAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-428 1.40e-17

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: 81.96  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpvslvvtrlVILGSGE---EGPQ--VGPSAAQTL 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNIR----------VVLVGLEiwtDEDKidVSGDANDTL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  290 RSFCAW-QRGLNTPEDsdpdhFDTAILFTRQDLCGVSTcdtlGMADVGTVCDPARSCAIVED---DGLQSAFTAAHELGH 365
Cdd:pfam01421  71 RNFLKWrQEYLKKRKP-----HDVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGH 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427675  366 VFNMLHDNSKP---CISLNGPlstsrhVMAPVMAHVDPEEpWSPCSARFITDFLDNGYGHCLLDKP 428
Cdd:pfam01421 142 NLGMQHDDFNGgckCPPGGGC------IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 301-416 1.00e-14

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: 72.55  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 301 TPEDSDPDHFDTAILFTRQDLcgvsTCDTLGMADVGTVCDPARSCAIVEDDGL---QSAFTAAHELGHVFNMLHD----- 372
Cdd:cd00203   43 VLVGVEIDKADIAILVTRQDF----DGGTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDhdrkd 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157427675 373 -NSKPCISLNGPLST--SRHVMAPVMAHVDPE--EPWSPCSARFITDFL 416
Cdd:cd00203  119 rDDYPTIDDTLNAEDddYYSVMSYTKGSFSDGqrKDFSQCDIDQINKLY 167
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 531-575 1.09e-11

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: 60.29  E-value: 1.09e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157427675   531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209   9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 219-416 5.17e-11

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 63.14  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 219 FVETLVVADdkmAAFHGAG-----LKRYLLTVMAAAAkaFKHPSIRNP-VSLVVTRLVILGSGEEGPQVGPS------AA 286
Cdd:cd04272    2 YPELFVVVD---YDHQSEFfsneqLIRYLAVMVNAAN--LRYRDLKSPrIRLLLVGITISKDPDFEPYIHPInygyidAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675 287 QTLRSFCAWQRGLNTPEDSDpdhfdTAILFTRQDLC----GVSTCDTLGMADVGTVCDpARSCAIVEDDG--LQSAFTAA 360
Cdd:cd04272   77 ETLENFNEYVKKKRDYFNPD-----VVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDTPgsYYGVYTMT 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427675 361 HELGHVFNMLHDNSKPCISLNGPLSTSR------HVMAPVMAHVDpEEPWSPCSARFITDFL 416
Cdd:cd04272  151 HELAHLLGAPHDGSPPPSWVKGHPGSLDcpwddgYIMSYVVNGER-QYRFSQCSQRQIRNVF 211
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-181 4.04e-10

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: 58.48  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562   1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157427675  132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562  81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
223-393 8.96e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.97  E-value: 8.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  223 LVVADDK-MAAFHGAGLKRYLLTVMAAAAKAFKHPSirnPVSLVVTRLVILGSGEE---GPQVGPSAAQTLRSF--CAWQ 296
Cdd:pfam13688   8 LVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPytpPACSTGDSSDRLSEFqdFSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  297 RGlntpEDSDpdhfDTAILFTrqdlcgVSTCDTLGMADVGTVCDPARSCAIVEDDG--------LQSAFTAAHELGHVFN 368
Cdd:pfam13688  85 RG----TQND----DLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFG 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157427675  369 MLHDnskPCISLNG---PLSTS------RHVMAP 393
Cdd:pfam13688 151 AVHD---CDSSTSSqccPPSNStcpaggRYIMNP 181
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 578-685 1.04e-08

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: 53.94  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236   1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157427675  648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236  76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 240-372 1.43e-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: 53.53  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675  240 RYLLTVMAAAAKAFKHPSirnPVSLVVTRLVILgSGEEGPQVGPSAAQTLRSFCAWQRglntpEDSDPDHFDTAILFTRQ 319
Cdd:pfam13582   1 ARIVSLVNRANTIYERDL---GIRLQLAAIIIT-TSADTPYTSSDALEILDELQEVND-----TRIGQYGYDLGHLFTGR 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157427675  320 DLCGVstcdtLGMADVGTVCDPARSCAIVEDD---GLQSAFTAAHELGHVFNMLHD 372
Cdd:pfam13582  72 DGGGG-----GGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ACR smart00608
ADAM Cysteine-Rich Domain;
438-509 8.36e-08

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 51.98  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   438 FPGKDYDADRQCQLTFGPDSR----HCPQL-----------------PPPCAA-------LWCSG--------------- 474
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKvapdSCYEElntkgdrfgncgrengtYIPCAPedvkcgkLQCTNvselpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 157427675   475 -HLNGHaMCQTKHSP---------WADGTPCGPAQACMGGRCLHM 509
Cdd:smart00608  94 sNIGGL-VCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 531-574 2.67e-05

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: 42.27  E-value: 2.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157427675  531 DCSRTCGGGVQFSSRDCTRPvPRNGGKYCeGRRTRFRSCNTEDC 574
Cdd:pfam19028  11 ECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
490-659 3.13e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 44.66  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   490 ADGTPCGPAQA-CMGGRCLHMDQlQdfnipqaggwgpwgpwgdCSRTCGGGVQFSSRDCTRPVPRNGGK--YCEGRRTRF 566
Cdd:smart00608   1 QDGTPCDNGQGyCYNGRCPTRDN-Q------------------CQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427675   567 RSCNTED-------CPTGSALT-FREEQCAAYNHRTDlfksfpgpmdwvprytgvapqdqckLTCqaQALGYYYVLEP-- 636
Cdd:smart00608  62 IPCAPEDvkcgklqCTNVSELPlLGEHATVIYSNIGG-------------------------LVC--WSLDYHLGTDPdi 114

                          170       180
                   ....*....|....*....|....
gi 157427675   637 -RVVDGTPCSPDssSVCVQGRCIH 659
Cdd:smart00608 115 gMVKDGTKCGPG--KVCINGQCVD 136
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 531-574 1.08e-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: 37.82  E-value: 1.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 157427675  531 DCSRTCGGGVQFSSRDCTRPVPR--NGGKYCEG--RRTRFRSCNTEDC 574
Cdd:pfam19030   8 ECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAqkKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
531-574 1.74e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.01  E-value: 1.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157427675  531 DCSRTCGGGVQFSSRDCTRPVPrnGGKYCEGRRTRFRSCNTEDC 574
Cdd:pfam00090   8 PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
 
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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