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Conserved domains on  [gi|1034571798|ref|XP_016872634|]
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A disintegrin and metalloproteinase with thrombospondin motifs 8 isoform X1 [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) ...
 219-422 1.86e-93

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: 292.61  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273     1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034571798 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHG 422
Cdd:cd04273   161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDG 203
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 675-793 1.34e-39

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: 141.95  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 675 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 753
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034571798 754 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 793
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 424-497 1.10e-20

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: 86.63  E-value: 1.10e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571798 424 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 497
Cdd:pfam17771   1 PGQL--YSADEQCRLIFGPGSTFCPNGD-EDVCSKLWC-SNPGGSTCTTKNL--PAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-148 3.08e-19

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: 84.29  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798  39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034571798 106 VNGEPESLAAVSLCRGLSGSFLLDGEEFTIQP--QGAGGSLAQPH 148
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPleKYSREEGGHPH 125
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 513-565 7.39e-16

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: 72.23  E-value: 7.39e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034571798  513 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 565
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 820-871 1.17e-12

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: 63.24  E-value: 1.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034571798 820 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 871
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 571-673 3.19e-09

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: 55.49  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 571 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 639
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034571798 640 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 673
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 219-422 1.86e-93

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: 292.61  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273     1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034571798 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHG 422
Cdd:cd04273   161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDG 203
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 675-793 1.34e-39

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: 141.95  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 675 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 753
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034571798 754 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 793
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 424-497 1.10e-20

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: 86.63  E-value: 1.10e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571798 424 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 497
Cdd:pfam17771   1 PGQL--YSADEQCRLIFGPGSTFCPNGD-EDVCSKLWC-SNPGGSTCTTKNL--PAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 219-380 5.69e-20

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: 88.90  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYK------ELNIRVVLVGL---EIWTDEdkidVSGDANDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGQeglcdTLGVADIGTICDPNKSCSVIED-----EGLqaAHTLAHELG 366
Cdd:pfam01421  72 NFLKWRQEYLKKRKPH----DVAQLLSGVEFGGT-----TVGAAYVGGMCSLEYSGGVNEDhsknlESF--AVTMAHELG 140

                         170
                  ....*....|....*
gi 1034571798 367 HVLSMPHDDS-KPCT 380
Cdd:pfam01421 141 HNLGMQHDDFnGGCK 155
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-148 3.08e-19

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: 84.29  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798  39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034571798 106 VNGEPESLAAVSLCRGLSGSFLLDGEEFTIQP--QGAGGSLAQPH 148
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPleKYSREEGGHPH 125
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 513-565 7.39e-16

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: 72.23  E-value: 7.39e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034571798  513 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 565
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 820-871 1.17e-12

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: 63.24  E-value: 1.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034571798 820 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 871
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 571-673 3.19e-09

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: 55.49  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 571 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 639
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034571798 640 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 673
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 515-564 4.59e-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: 49.97  E-value: 4.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034571798 515 PWGPWGECSRTCGGGVQFSHRECKDPePQNGGRYC---LGRRAkyqsCHTEEC 564
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCpelLERRP----CNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 820-872 1.59e-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: 48.74  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034571798  820 WVLGDWSECSSTCGAGWQRRTVECRDPSGQAS-ATCNKALKpeDAKPCESQLCP 872
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDV--ETRACNEQPCP 53
ACR smart00608
ADAM Cysteine-Rich Domain;
432-498 1.39e-06

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 48.51  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798  432 LDQQCRQIFGPDFR----HCP---NT------------------SAQDV-CAQLWCHTDGAEPL---------------- 469
Cdd:smart00608  21 RDNQCQALFGPGAKvapdSCYeelNTkgdrfgncgrengtyipcAPEDVkCGKLQCTNVSELPLlgehatviysnigglv 100

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034571798  470 ---CHTKNGSLP----WADGTPCGPGHLCSEGSCLP 498
Cdd:smart00608 101 cwsLDYHLGTDPdigmVKDGTKCGPGKVCINGQCVD 136
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 219-422 1.86e-93

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: 292.61  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273     1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034571798 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHG 422
Cdd:cd04273   161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDG 203
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 675-793 1.34e-39

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: 141.95  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 675 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 753
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034571798 754 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 793
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 219-418 1.93e-34

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: 130.23  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFYGAD---LQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCN 295
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 296 WQRRfnqpsdrHPEHYDTAILLTRQNFcgqeGLCDTLGVADIGTICDPNKSCSVIEDEG--LQAAHTLAHELGHVLSMPH 373
Cdd:cd04267    81 WRAE-------GPIRHDNAVLLTAQDF----IEGDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEH 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034571798 374 DDSkPCTRLFGPMGKHHVMAPLFVHLNQTLpWSPCSAMYLTELLD 418
Cdd:cd04267   150 DGG-DELAFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 219-422 1.58e-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: 98.84  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYR------PLNIRVVLVGL---EIWTDKdkisVSGDAGETLN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGqeglcDTLGVADIGTICDPNKSCSVIEDEG---LQAAHTLAHELGHV 368
Cdd:cd04269    72 RFLDWKRSNLLPRKPH----DNAQLLTGRDFDG-----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHN 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 369 LSMPHDDS------KPCtrlfgpmgkhhVMAPLFVHLNQTlpWSPCSAMYLTELLDGGHG 422
Cdd:cd04269   143 LGMEHDDGgctcgrSTC-----------IMAPSPSSLTDA--FSNCSYEDYQKFLSRGGG 189
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 424-497 1.10e-20

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: 86.63  E-value: 1.10e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571798 424 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 497
Cdd:pfam17771   1 PGQL--YSADEQCRLIFGPGSTFCPNGD-EDVCSKLWC-SNPGGSTCTTKNL--PAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 219-380 5.69e-20

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: 88.90  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYK------ELNIRVVLVGL---EIWTDEdkidVSGDANDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGQeglcdTLGVADIGTICDPNKSCSVIED-----EGLqaAHTLAHELG 366
Cdd:pfam01421  72 NFLKWRQEYLKKRKPH----DVAQLLSGVEFGGT-----TVGAAYVGGMCSLEYSGGVNEDhsknlESF--AVTMAHELG 140

                         170
                  ....*....|....*
gi 1034571798 367 HVLSMPHDDS-KPCT 380
Cdd:pfam01421 141 HNLGMQHDDFnGGCK 155
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-148 3.08e-19

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: 84.29  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798  39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034571798 106 VNGEPESLAAVSLCRGLSGSFLLDGEEFTIQP--QGAGGSLAQPH 148
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPleKYSREEGGHPH 125
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 513-565 7.39e-16

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: 72.23  E-value: 7.39e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034571798  513 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 565
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 820-871 1.17e-12

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: 63.24  E-value: 1.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034571798 820 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 871
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 302-417 1.71e-12

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: 66.39  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 302 QPSDRHPEHYDTAILLTRQNFCGqeglcDTLGVADIGTICDPNKSCSVIEDEGL---QAAHTLAHELGHVLSMPHDDS-- 376
Cdd:cd00203    43 VLVGVEIDKADIAILVTRQDFDG-----GTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDHDrk 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034571798 377 -------KPCTRLFGPMGKHHVMAP--LFVHLNQTLPWSPCSAMYLTELL 417
Cdd:cd00203   118 drddyptIDDTLNAEDDDYYSVMSYtkGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 220-409 9.44e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.45  E-value: 9.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 220 FVETLLVADASMAAfYGADLQNHIL---TLMSVAARIYKhpSIKN-SINLMVVKVLIVEDEKWGPEV------SDNGGLT 289
Cdd:cd04272     2 YPELFVVVDYDHQS-EFFSNEQLIRylaVMVNAANLRYR--DLKSpRIRLLLVGITISKDPDFEPYIhpinygYIDAAET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 290 LRNFcnwqrRFNQPSDRHPEHYDTAILLTRQN-FCGQEGLCDT--LGVADIGTICDPNkSCSVIEDEG--LQAAHTLAHE 364
Cdd:cd04272    79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDmSTYSGGSLQTgtGGYAYVGGACTEN-RVAMGEDTPgsYYGVYTMTHE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034571798 365 LGHVLSMPHDDSKPCTRLFGPMGKH-------HVMAPLFVHLNQtLPWSPCS 409
Cdd:cd04272   153 LAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgYIMSYVVNGERQ-YRFSQCS 203
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
224-394 6.53e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.44  E-value: 6.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 224 LLVADAS-MAAFYGADLQNHILTLMSVAARIYKHPSiknSINLMVVKVLIVEDEK---WGPEVSDNGGLTLRNFcnwqRR 299
Cdd:pfam13688   8 LVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCpytPPACSTGDSSDRLSEF----QD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 300 FNqpSDRHPEHYDTAILLTRQNfcgqeglCDTLGVADIGTICDPNKSCSVIEDEG--------LQAAHTLAHELGHVLSM 371
Cdd:pfam13688  81 FS--AWRGTQNDDLAYLFLMTN-------CSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGA 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034571798 372 PHD-------DSKPCTRLFGPMGKHHVMAP 394
Cdd:pfam13688 152 VHDcdsstssQCCPPSNSTCPAGGRYIMNP 181
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 571-673 3.19e-09

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: 55.49  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 571 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 639
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034571798 640 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 673
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 515-564 4.59e-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: 49.97  E-value: 4.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034571798 515 PWGPWGECSRTCGGGVQFSHRECKDPePQNGGRYC---LGRRAkyqsCHTEEC 564
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCpelLERRP----CNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
515-564 6.98e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.34  E-value: 6.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034571798 515 PWGPWGECSRTCGGGVQFSHRECKDPEPqnGGRYCLGRRAKYQSCHTEEC 564
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 820-872 1.59e-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: 48.74  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034571798  820 WVLGDWSECSSTCGAGWQRRTVECRDPSGQAS-ATCNKALKpeDAKPCESQLCP 872
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDV--ETRACNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-374 2.27e-07

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: 50.45  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 243 ILTLMSVAARIYKHPSiknSINLMVVKVLIVEDEKwGPEVSDNGGLTLRNFCNWQR-RFNQPSdrhpehYDTAILLTRQN 321
Cdd:pfam13582   3 IVSLVNRANTIYERDL---GIRLQLAAIIITTSAD-TPYTSSDALEILDELQEVNDtRIGQYG------YDLGHLFTGRD 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034571798 322 FCGqeglcdTLGVADIGTICDPNKSCSVIEDE---GLQAAHTLAHELGHVLSMPHD 374
Cdd:pfam13582  73 GGG------GGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ACR smart00608
ADAM Cysteine-Rich Domain;
432-498 1.39e-06

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 48.51  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798  432 LDQQCRQIFGPDFR----HCP---NT------------------SAQDV-CAQLWCHTDGAEPL---------------- 469
Cdd:smart00608  21 RDNQCQALFGPGAKvapdSCYeelNTkgdrfgncgrengtyipcAPEDVkCGKLQCTNVSELPLlgehatviysnigglv 100

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034571798  470 ---CHTKNGSLP----WADGTPCGPGHLCSEGSCLP 498
Cdd:smart00608 101 cwsLDYHLGTDPdigmVKDGTKCGPGKVCINGQCVD 136
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-417 2.01e-05

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: 46.47  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 243 ILTLMSVAARIYKHPSIknSINLMVVKVLIVEDEkwgPEVSDNGgltlRNFCN---WQRRFNQPSD--RHPEHYDTAILL 317
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDI--NINGGLVNPGEIPAT---TSASDSG----NNYCNsptTIVRRLNFLSqwRGEQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 318 TRQNFCGQEglcdtLGVADIGTICDpNKSCSVIEDEGL-------------QAAHTLAHELGHVLSMPHD---DSKPCTR 381
Cdd:pfam13574  78 TMGTFSGGE-----LGLAYVGQICQ-KGASSPKTNTGLstttnygsfnyptQEWDVVAHEVGHNFGATHDcdgSQYASSG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034571798 382 -------LFGPMGKHHVMAPLFVHlNQTLpWSPCSAMYLTELL 417
Cdd:pfam13574 152 cernaatSVCSANGSFIMNPASKS-NNDL-FSPCSISLICDVL 192
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 517-576 4.47e-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: 38.97  E-value: 4.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 517 GPWGECSRTCGGGVQFSHRECKDPepqnggrycLGRRAKyqscHTEECPPDGKSFREQQC 576
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQK---------GGGSIV----PDSECSAQKKPPETQSC 50
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 226-379 2.04e-03

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 40.48  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 226 VADASMAAFYG--ADLQNHILTLMSVAARIYKhpSIKNsINLMVVKVLI---------VEDEKWGPEVSDNGGLT--LRN 292
Cdd:cd04271     8 AADCSYTKSFGsvEEARRNILNNVNSASQLYE--SSFN-ISLGLRNLTIsdascpstaVDSAPWNLPCNSRIDIDdrLSI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571798 293 FCNWqrRFNQPSDRhpehydtAILLTRQNFCGQEglcDTLGVADIGTICDPNKScsviEDEGLQAAHT------------ 360
Cdd:cd04271    85 FSQW--RGQQPDDG-------NAFWTLMTACPSG---SEVGVAWLGQLCRTGAS----DQGNETVAGTnvvvrtsnewqv 148

                         170       180
                  ....*....|....*....|
gi 1034571798 361 LAHELGHVLSMPHD-DSKPC 379
Cdd:cd04271   149 FAHEIGHTFGAVHDcTSGTC 168
TSP_1 pfam00090
Thrombospondin type 1 domain;
823-871 6.29e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 6.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034571798 823 GDWSECSSTCGAGWQRRTVECRDPSGQASAtCnkALKPEDAKPCESQLC 871
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGEP-C--TGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 823-840 8.24e-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: 35.33  E-value: 8.24e-03
                          10
                  ....*....|....*...
gi 1034571798 823 GDWSECSSTCGAGWQRRT 840
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRT 24
 
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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