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Conserved domains on  [gi|1958757316|ref|XP_038954692|]
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A disintegrin and metalloproteinase with thrombospondin motifs 14 isoform X1 [Rattus norvegicus]

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) ...
 243-441 6.87e-92

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: 284.90  E-value: 6.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 243 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 322
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 395
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958757316 396 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--NCLL 441
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-191 3.63e-33

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: 123.96  E-value: 3.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316  68 HLRVARSPlslerETPRPRHHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQRE-CVYTGGVTGM 145
Cdd:pfam01562  10 PSRRRRSL-----ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGH 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958757316 146 PGAAVAISNCDGLAGLIRTDNSDFFIEPLErgQQEKEAGGRTHVVY 191
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 456-525 9.75e-23

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


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.02  E-value: 9.75e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 456 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCV 525
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 539-591 1.17e-17

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: 77.24  E-value: 1.17e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958757316  539 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRLCSGPMFEYQICNSEDCP 591
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 596-697 7.89e-10

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: 57.03  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 596 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSEAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 665
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958757316 666 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 697
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 243-441 6.87e-92

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: 284.90  E-value: 6.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 243 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 322
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 395
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958757316 396 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--NCLL 441
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-191 3.63e-33

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: 123.96  E-value: 3.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316  68 HLRVARSPlslerETPRPRHHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQRE-CVYTGGVTGM 145
Cdd:pfam01562  10 PSRRRRSL-----ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGH 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958757316 146 PGAAVAISNCDGLAGLIRTDNSDFFIEPLErgQQEKEAGGRTHVVY 191
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 456-525 9.75e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.02  E-value: 9.75e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 456 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCV 525
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 245-444 3.00e-22

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: 95.06  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYhdESLGAHVNIALVRLIMVGYRQSLSlierGNPARSLEQVCRW 322
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIY--KELNIRVVLVGLEIWTDEDKIDVS----GDANDTLRNFLKW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 AHSQQRqdpsHTEHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALN---HEDGFSSAFVVAHETGHVLGMEHDGQGN 397
Cdd:pfam01421  77 RQEYLK----KRKPHDVAQLLSGVEFGGTtvGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFNG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958757316 398 GCDDETSLGSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYN--CLLDDP 444
Cdd:pfam01421 153 GCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 539-591 1.17e-17

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: 77.24  E-value: 1.17e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958757316  539 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRLCSGPMFEYQICNSEDCP 591
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 596-697 7.89e-10

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: 57.03  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 596 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSEAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 665
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958757316 666 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 697
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
537-590 5.55e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 5.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958757316 537 GGWSSWTnfgSCSRSCGGGVRSRSRSCDNPPPayGGRLCSGPMFEYQICNSEDC 590
Cdd:pfam00090   1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ACR smart00608
ADAM Cysteine-Rich Domain;
489-525 4.60e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757316  489 LWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCV 525
Cdd:smart00608  99 LVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 243-441 6.87e-92

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: 284.90  E-value: 6.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 243 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 322
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 395
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958757316 396 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--NCLL 441
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-191 3.63e-33

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: 123.96  E-value: 3.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316  68 HLRVARSPlslerETPRPRHHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQRE-CVYTGGVTGM 145
Cdd:pfam01562  10 PSRRRRSL-----ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGH 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958757316 146 PGAAVAISNCDGLAGLIRTDNSDFFIEPLErgQQEKEAGGRTHVVY 191
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 245-442 4.59e-24

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: 100.00  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYHDeslgAHVNIALVRLIMVGYRQSLSLieRGNPARSLEQVCRW 322
Cdd:cd04269     3 VELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLDW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 ahsqQRQDPSHTEHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALNHEDG---FSSAFVVAHETGHVLGMEHDG--- 394
Cdd:cd04269    77 ----KRSNLLPRKPHDNAQLLTGRDFDGNtvGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDggc 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958757316 395 --QGNGCddetslgsVMAPlvQAAFHRFHWSRCSKLELSRYLPSYN--CLLD 442
Cdd:cd04269   153 tcGRSTC--------IMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 245-427 1.02e-23

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: 99.03  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMvgyRQSLSLIERGNP--ARSLEQVC 320
Cdd:cd04267     3 IELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQI---LKGEQFAPPIDSdaSNTLNSFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 321 RWahsqQRQDPSHtehHDHVIFLTRQNFGPS---GYAPVTGMCHPLRSCAL--NHEDGFSSAFVVAHETGHVLGMEHDGQ 395
Cdd:cd04267    80 FW----RAEGPIR---HDNAVLLTAQDFIEGdilGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGG 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958757316 396 GNGCDDETSLGS-VMAPLVQAAFHRfHWSRCSK 427
Cdd:cd04267   153 DELAFECDGGGNyIMAPVDSGLNSY-RFSQCSI 184
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 456-525 9.75e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.02  E-value: 9.75e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 456 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCV 525
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 245-444 3.00e-22

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: 95.06  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYhdESLGAHVNIALVRLIMVGYRQSLSlierGNPARSLEQVCRW 322
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIY--KELNIRVVLVGLEIWTDEDKIDVS----GDANDTLRNFLKW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 323 AHSQQRqdpsHTEHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALN---HEDGFSSAFVVAHETGHVLGMEHDGQGN 397
Cdd:pfam01421  77 RQEYLK----KRKPHDVAQLLSGVEFGGTtvGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFNG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958757316 398 GCDDETSLGSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYN--CLLDDP 444
Cdd:pfam01421 153 GCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 539-591 1.17e-17

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: 77.24  E-value: 1.17e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958757316  539 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRLCSGPMFEYQICNSEDCP 591
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
247-411 3.41e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 65.90  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 247 VLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESlgaHVNIALVRLIMVGYRQSlsliERGNPARSLEQVCRWAHSQ 326
Cdd:pfam13688   7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCP----YTPPACSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 327 QRQDPSHTEHHDHVIFLTRQNFGPSGYAPVTGMCHPLRSCALNHEDGF--------SSAFVVAHETGHVLGMEHDGQGNG 398
Cdd:pfam13688  80 DFSAWRGTQNDDLAYLFLMTNCSGGGLAWLGQLCNSGSAGSVSTRVSGnnvvvstaTEWQVFAHEIGHNFGAVHDCDSST 159

                         170
                  ....*....|...
gi 1958757316 399 CDDETSLGSVMAP 411
Cdd:pfam13688 160 SSQCCPPSNSTCP 172
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 245-434 2.31e-10

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: 59.84  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDDsvvRFHGREHTQNYVLTLMNIVDEIYHDEsLGAHVNIALVRLImvgyrqslsliergnparsleqvcrwah 324
Cdd:cd00203     3 IPYVVVADD---RDVEEENLSAQIQSLILIAMQIWRDY-LNIRFVLVGVEID---------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 325 sqqrqdpshteHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCAL---NHEDGFSSAFVVAHETGHVLGMEHDGQGNGC 399
Cdd:cd00203    51 -----------KADIAILVTRQDFDGGtgGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDRKDR 119

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958757316 400 DDE-----------TSLGSVMAPLVQAAFH--RFHWSRCSKLELSRYL 434
Cdd:cd00203   120 DDYptiddtlnaedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 596-697 7.89e-10

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: 57.03  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 596 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSEAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 665
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958757316 666 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 697
Cdd:pfam19236  84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
537-590 5.55e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 5.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958757316 537 GGWSSWTnfgSCSRSCGGGVRSRSRSCDNPPPayGGRLCSGPMFEYQICNSEDC 590
Cdd:pfam00090   1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 245-440 5.58e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 56.98  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 245 IEVLLAVDdsvvRFHGREHTQN-----YVLTLMNIVDEIYHDESlGAHVNIALVRLIMVGYRQSLSLIERGNP-----AR 314
Cdd:cd04272     3 PELFVVVD----YDHQSEFFSNeqlirYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYgyidaAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757316 315 SLEQVCrwAHSQQRqdpSHTEHHDHVIFLTRQ----------NFGPSGYAPVTGMCHPLRsCALNHEDG--FSSAFVVAH 382
Cdd:cd04272    78 TLENFN--EYVKKK---RDYFNPDVVFLVTGLdmstysggslQTGTGGYAYVGGACTENR-VAMGEDTPgsYYGVYTMTH 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958757316 383 ETGHVLGMEHDGQG-----------NGCDDEtsLGSVMAPLVQAAFHrFHWSRCSKLELSRYL--PSYNCL 440
Cdd:cd04272   152 ELAHLLGAPHDGSPppswvkghpgsLDCPWD--DGYIMSYVVNGERQ-YRFSQCSQRQIRNVFrrLGASCL 219
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 540-590 1.76e-06

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.35  E-value: 1.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958757316 540 SSWTNFGSCSRSCGGGVRSRSRSCDNpPPAYGGRLCsGPMFEYQICNSEDC 590
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPC-PELLERRPCNLPPC 52
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 348-409 1.19e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 40.17  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958757316 348 FGPSGYAPVTGMCHPLRSCALNHEDGFSSAF---VVAHETGHVLGMEHDGQGNGCDDETSL-------GSVM 409
Cdd:cd04268    63 YGPSQVDPLTGEILLARVYLYSSFVEYSGARlrnTAEHELGHALGLRHNFAASDRDDNVDLlaekgdtSSVM 134
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 344-411 2.47e-03

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 39.91  E-value: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958757316 344 TRQNFGPSGYAPVTgmchplrscalnheDGFSsafVVAHETGHVLGMEHDGQGNGCD-----DETSLGSVMAP 411
Cdd:pfam13583 120 ARQNAKASGVARSR--------------DEWD---IFAHEIGHTFGAVHDCSSQGEGlssstEDGSGQTIMSY 175
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 543-590 3.01e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 36.28  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958757316 543 TNFGSCSRSCGGGVRSRSRSCDNP--PPAYGGRLCSG---PMfEYQICNSEDC 590
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQKggGSIVPDSECSAqkkPP-ETQSCNLKPC 55
ACR smart00608
ADAM Cysteine-Rich Domain;
489-525 4.60e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958757316  489 LWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCV 525
Cdd:smart00608  99 LVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
 
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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