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Conserved domains on  [gi|313104077|sp|Q9UP79|]
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RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 8; Short=ADAM-TS 8; Short=ADAM-TS8; Short=ADAMTS-8; AltName: Full=METH-2; AltName: Full=METH-8; Flags: Precursor

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) ...
 219-426 7.58e-97

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: 301.85  E-value: 7.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273    1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 313104077 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHGDCLL 426
Cdd:cd04273  161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 691-809 1.38e-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: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  691 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 769
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 313104077  770 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 809
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 ...
 440-513 1.09e-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: 1.09e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313104077  440 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 513
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 2.66e-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: 84.67  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077   39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 313104077  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.
 529-581 6.76e-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: 6.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 313104077   529 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 581
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 836-887 1.13e-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: 1.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 313104077  836 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 887
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 ...
 587-689 3.26e-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: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  587 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 655
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 313104077  656 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 689
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) ...
 219-426 7.58e-97

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: 301.85  E-value: 7.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273    1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 313104077 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHGDCLL 426
Cdd:cd04273  161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 691-809 1.38e-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: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  691 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 769
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 313104077  770 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 809
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 219-429 2.63e-23

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: 98.53  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYK------ELNIRVVLVGL---EIWTDEdkidVSGDANDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGQeglcdTLGVADIGTICDPNKSCSVIED-----EGLqaAHTLAHELG 366
Cdd:pfam01421  72 NFLKWRQEYLKKRKPH----DVAQLLSGVEFGGT-----TVGAAYVGGMCSLEYSGGVNEDhsknlESF--AVTMAHELG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313104077  367 HVLSMPHDDS-KPCTrlfGPMGKHHVMAPLFVHlnqTLP--WSPCSAMYLTELLDGGHGDCLLDAP 429
Cdd:pfam01421 141 HNLGMQHDDFnGGCK---CPPGGGCIMNPSAGS---SFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 440-513 1.09e-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: 1.09e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313104077  440 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 513
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 2.66e-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: 84.67  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077   39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 313104077  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.
 529-581 6.76e-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: 6.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 313104077   529 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 581
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 836-887 1.13e-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: 1.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 313104077  836 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 887
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 ...
 587-689 3.26e-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: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  587 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 655
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 313104077  656 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 689
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 531-580 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 313104077  531 PWGPWGECSRTCGGGVQFSHRECKDPePQNGGRYC---LGRRAkyqsCHTEEC 580
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCpelLERRP----CNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 836-888 1.46e-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: 1.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 313104077   836 WVLGDWSECSSTCGAGWQRRTVECRDPSGQAS-ATCNKALKpeDAKPCESQLCP 888
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDV--ETRACNEQPCP 53
ACR smart00608
ADAM Cysteine-Rich Domain;
448-514 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 313104077   448 LDQQCRQIFGPDFR----HCP---NT------------------SAQDV-CAQLWCHTDGAEPL---------------- 485
Cdd:smart00608  21 RDNQCQALFGPGAKvapdSCYeelNTkgdrfgncgrengtyipcAPEDVkCGKLQCTNVSELPLlgehatviysnigglv 100

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 313104077   486 ---CHTKNGSLP----WADGTPCGPGHLCSEGSCLP 514
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) ...
 219-426 7.58e-97

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: 301.85  E-value: 7.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 219 RFVETLLVADASMAAFY-GADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQ 297
Cdd:cd04273    1 RYVETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 298 RRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDS- 376
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 313104077 377 KPCTRLFGPMgkhHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHGDCLL 426
Cdd:cd04273  161 NSCGPEGKDG---HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 691-809 1.38e-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: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  691 KVSGSLTPTN-YGYNDIVTIPAGATNIDVKQRSHPGvqndgNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGS 769
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 313104077  770 IATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVP 809
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 219-418 1.98e-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: 1.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 219 RFVETLLVADASMAAFYGAD---LQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCN 295
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 296 WQRRfnqpsdrHPEHYDTAILLTRQNFcgqeGLCDTLGVADIGTICDPNKSCSVIEDEG--LQAAHTLAHELGHVLSMPH 373
Cdd:cd04267   81 WRAE-------GPIRHDNAVLLTAQDF----IEGDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEH 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 313104077 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 ...
 219-427 2.87e-26

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: 106.93  E-value: 2.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYR------PLNIRVVLVGL---EIWTDKdkisVSGDAGETLN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGqeglcDTLGVADIGTICDPNKSCSVIEDEG---LQAAHTLAHELGHV 368
Cdd:cd04269   72 RFLDWKRSNLLPRKPH----DNAQLLTGRDFDG-----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHN 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313104077 369 LSMPHDDS------KPCtrlfgpmgkhhVMAPLFVHLNQTlpWSPCSAMYLTELLDGGHGDCLLD 427
Cdd:cd04269  143 LGMEHDDGgctcgrSTC-----------IMAPSPSSLTDA--FSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 219-429 2.63e-23

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: 98.53  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  219 RFVETLLVADASMAAFYGADL---QNHILTLMSVAARIYKhpsiknSINLMVVKVLIvedEKWGPE----VSDNGGLTLR 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYK------ELNIRVVLVGL---EIWTDEdkidVSGDANDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  292 NFCNWQRRFNQPSDRHpehyDTAILLTRQNFCGQeglcdTLGVADIGTICDPNKSCSVIED-----EGLqaAHTLAHELG 366
Cdd:pfam01421  72 NFLKWRQEYLKKRKPH----DVAQLLSGVEFGGT-----TVGAAYVGGMCSLEYSGGVNEDhsknlESF--AVTMAHELG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313104077  367 HVLSMPHDDS-KPCTrlfGPMGKHHVMAPLFVHlnqTLP--WSPCSAMYLTELLDGGHGDCLLDAP 429
Cdd:pfam01421 141 HNLGMQHDDFnGGCK---CPPGGGCIMNPSAGS---SFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 440-513 1.09e-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: 1.09e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313104077  440 PGRMalYQLDQQCRQIFGPDFRHCPNTSaQDVCAQLWChTDGAEPLCHTKNGslPWADGTPCGPGHLCSEGSCL 513
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 2.66e-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: 84.67  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077   39 ELVVPTRLPGS------------AGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRG-CFFSGT 105
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDhCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 313104077  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.
 529-581 6.76e-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: 6.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 313104077   529 WAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECP 581
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 836-887 1.13e-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: 1.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 313104077  836 WVLGDWSECSSTCGAGWQRRTVECRDPSG---QASATCNKALKPEDAKPCESQLC 887
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 302-417 1.75e-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: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 302 QPSDRHPEHYDTAILLTRQNFCGqeglcDTLGVADIGTICDPNKSCSVIEDEGL---QAAHTLAHELGHVLSMPHDDS-- 376
Cdd:cd00203   43 VLVGVEIDKADIAILVTRQDFDG-----GTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDHDrk 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 313104077 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 9.64e-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: 9.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 220 FVETLLVADASMAAfYGADLQNHIL---TLMSVAARIYKhpSIKN-SINLMVVKVLIVEDEKWGPEV------SDNGGLT 289
Cdd:cd04272    2 YPELFVVVDYDHQS-EFFSNEQLIRylaVMVNAANLRYR--DLKSpRIRLLLVGITISKDPDFEPYIhpinygYIDAAET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 290 LRNFcnwqrRFNQPSDRHPEHYDTAILLTRQN-FCGQEGLCDT--LGVADIGTICDPNkSCSVIEDEG--LQAAHTLAHE 364
Cdd:cd04272   79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDmSTYSGGSLQTgtGGYAYVGGACTEN-RVAMGEDTPgsYYGVYTMTHE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313104077 365 LGHVLSMPHDDSKPCTRLFGPMGKH-------HVMAPLFVHLNQtLPWSPCS 409
Cdd:cd04272  153 LAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgYIMSYVVNGERQ-YRFSQCS 203
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
224-394 6.67e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.44  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  224 LLVADAS-MAAFYGADLQNHILTLMSVAARIYKHPSiknSINLMVVKVLIVEDEK---WGPEVSDNGGLTLRNFcnwqRR 299
Cdd:pfam13688   8 LVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCpytPPACSTGDSSDRLSEF----QD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  300 FNqpSDRHPEHYDTAILLTRQNfcgqeglCDTLGVADIGTICDPNKSCSVIEDEG--------LQAAHTLAHELGHVLSM 371
Cdd:pfam13688  81 FS--AWRGTQNDDLAYLFLMTN-------CSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGA 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 313104077  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 ...
 587-689 3.26e-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: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  587 FREQQCEKYNAYNYTDMDG--NLLQW---VPKYAGVSprdRCKLFCRARGRSEFKVFEAKVIDGTLCGPE------TLAI 655
Cdd:pfam19236   5 FMSQQCARTDGQPLRSSPGgaSFYHWgaaVPHSQGDA---LCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 313104077  656 CVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSC 689
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 531-580 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 313104077  531 PWGPWGECSRTCGGGVQFSHRECKDPePQNGGRYC---LGRRAkyqsCHTEEC 580
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCpelLERRP----CNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
531-580 6.70e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.72  E-value: 6.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 313104077  531 PWGPWGECSRTCGGGVQFSHRECKDPEPqnGGRYCLGRRAKYQSCHTEEC 580
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 836-888 1.46e-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: 1.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 313104077   836 WVLGDWSECSSTCGAGWQRRTVECRDPSGQAS-ATCNKALKpeDAKPCESQLCP 888
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDV--ETRACNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-374 2.32e-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: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  243 ILTLMSVAARIYKHPSiknSINLMVVKVLIVEDEKwGPEVSDNGGLTLRNFCNWQR-RFNQPSdrhpehYDTAILLTRQN 321
Cdd:pfam13582   3 IVSLVNRANTIYERDL---GIRLQLAAIIITTSAD-TPYTSSDALEILDELQEVNDtRIGQYG------YDLGHLFTGRD 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 313104077  322 FCGqeglcdTLGVADIGTICDPNKSCSVIEDE---GLQAAHTLAHELGHVLSMPHD 374
Cdd:pfam13582  73 GGG------GGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ACR smart00608
ADAM Cysteine-Rich Domain;
448-514 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 313104077   448 LDQQCRQIFGPDFR----HCP---NT------------------SAQDV-CAQLWCHTDGAEPL---------------- 485
Cdd:smart00608  21 RDNQCQALFGPGAKvapdSCYeelNTkgdrfgncgrengtyipcAPEDVkCGKLQCTNVSELPLlgehatviysnigglv 100

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 313104077   486 ---CHTKNGSLP----WADGTPCGPGHLCSEGSCLP 514
Cdd:smart00608 101 cwsLDYHLGTDPdigmVKDGTKCGPGKVCINGQCVD 136
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-417 2.05e-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: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  243 ILTLMSVAARIYKHPSIknSINLMVVKVLIVEDEkwgPEVSDNGgltlRNFCN---WQRRFNQPSD--RHPEHYDTAILL 317
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDI--NINGGLVNPGEIPAT---TSASDSG----NNYCNsptTIVRRLNFLSqwRGEQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  318 TRQNFCGQEglcdtLGVADIGTICDpNKSCSVIEDEGL-------------QAAHTLAHELGHVLSMPHD---DSKPCTR 381
Cdd:pfam13574  78 TMGTFSGGE-----LGLAYVGQICQ-KGASSPKTNTGLstttnygsfnyptQEWDVVAHEVGHNFGATHDcdgSQYASSG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 313104077  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 ...
 533-592 4.42e-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: 4.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077  533 GPWGECSRTCGGGVQFSHRECKDPepqnggrycLGRRAKyqscHTEECPPDGKSFREQQC 592
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 1.99e-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: 40.87  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 226 VADASMAAFYG--ADLQNHILTLMSVAARIYKhpSIKNsINLMVVKVLI---------VEDEKWGPEVSDNGGLT--LRN 292
Cdd:cd04271    8 AADCSYTKSFGsvEEARRNILNNVNSASQLYE--SSFN-ISLGLRNLTIsdascpstaVDSAPWNLPCNSRIDIDdrLSI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313104077 293 FCNWqrRFNQPSDRhpehydtAILLTRQNFCGQEglcDTLGVADIGTICDPNKScsviEDEGLQAAHT------------ 360
Cdd:cd04271   85 FSQW--RGQQPDDG-------NAFWTLMTACPSG---SEVGVAWLGQLCRTGAS----DQGNETVAGTnvvvrtsnewqv 148

                        170       180
                 ....*....|....*....|
gi 313104077 361 LAHELGHVLSMPHD-DSKPC 379
Cdd:cd04271  149 FAHEIGHTFGAVHDcTSGTC 168
TSP_1 pfam00090
Thrombospondin type 1 domain;
839-887 6.04e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 6.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 313104077  839 GDWSECSSTCGAGWQRRTVECRDPSGQASAtCnkALKPEDAKPCESQLC 887
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 ...
 839-856 8.23e-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: 8.23e-03
                          10
                  ....*....|....*...
gi 313104077  839 GDWSECSSTCGAGWQRRT 856
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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