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Conserved domains on  [gi|1039771792|ref|XP_017176420|]
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A disintegrin and metalloproteinase with thrombospondin motifs 3 isoform X2 [Mus musculus]

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) ...
 256-457 2.94e-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: 299.92  E-value: 2.94e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039771792 412 GNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSY--DCLL 457
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-201 1.29e-38

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: 139.37  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792  43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562   1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 123 prnshlhgSASEGSWRSEPLQT-SCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLErgKQMDEENGRIHVVY 201
Cdd:pfam01562  59 --------LDGGTGVESPPVQTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-540 3.65e-23

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


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 93.18  E-value: 3.65e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771792 472 PGINYSMDEQCRFDFGVGYKMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECAAGKWCYKGHC 540
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 554-605 2.35e-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: 76.47  E-value: 2.35e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771792  554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 1.13e-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: 59.34  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSkeTGDVAYMKQ--LVHDGTRCSYKDP-----Y 676
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRA--IGESFIMKRgdSFLDGTRCMPSGPredgtL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039771792 677 SICVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236  80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 256-457 2.94e-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: 299.92  E-value: 2.94e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039771792 412 GNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSY--DCLL 457
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-201 1.29e-38

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: 139.37  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792  43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562   1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 123 prnshlhgSASEGSWRSEPLQT-SCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLErgKQMDEENGRIHVVY 201
Cdd:pfam01562  59 --------LDGGTGVESPPVQTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-540 3.65e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 93.18  E-value: 3.65e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771792 472 PGINYSMDEQCRFDFGVGYKMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECAAGKWCYKGHC 540
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKC 67
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 258-460 1.07e-21

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: 93.52  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 258 IEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHdeslGVHINVVLVRMIMLGYAKSISLIerGNPSRSLENVCRW 335
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDKIDVS--GDANDTLRNFLKW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 acQQQKTDPNHAehHDHAIFLTRQDFGpAGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHDGQG 412
Cdd:pfam01421  77 --RQEYLKKRKP--HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039771792 413 NRCGDETAMGSVMAPLVQAAFHRyHWSRCSGQELKRYIHSYD--CLLDDP 460
Cdd:pfam01421 152 GGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 554-605 2.35e-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: 76.47  E-value: 2.35e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771792  554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 1.13e-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: 59.34  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSkeTGDVAYMKQ--LVHDGTRCSYKDP-----Y 676
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRA--IGESFIMKRgdSFLDGTRCMPSGPredgtL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039771792 677 SICVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236  80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-605 4.34e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 4.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039771792 552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPTPinGGQDCPGVNFEYQLCNTEEC 605
Cdd:pfam00090   1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
M6dom_TIGR03296 TIGR03296
M6 family metalloprotease domain; This model describes a metalloproteinase domain, with a ...
 383-423 2.94e-03

M6 family metalloprotease domain; This model describes a metalloproteinase domain, with a characteristic HExxH motif. Examples of this domain are found in proteins in the family of immune inhibitor A, which cleaves antibacterial peptides, and in other, only distantly related proteases. This model is built to be broader and more inclusive than pfam05547.


Pssm-ID: 274507 [Multi-domain]  Cd Length: 285  Bit Score: 40.47  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039771792 383 TLNHEDGfsSAFVVAHETGHVLGM------EHDGQGNRCGDETAMGS 423
Cdd:TIGR03296 158 TIQPEDG--GIGVFAHELGHDLGLpdlydtQYDGGGEPVGYWSLMSS 202
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 256-457 2.94e-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: 299.92  E-value: 2.94e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039771792 412 GNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSY--DCLL 457
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-201 1.29e-38

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: 139.37  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792  43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562   1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 123 prnshlhgSASEGSWRSEPLQT-SCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLErgKQMDEENGRIHVVY 201
Cdd:pfam01562  59 --------LDGGTGVESPPVQTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 257-458 3.63e-27

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: 109.24  E-value: 3.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 257 NIEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHDeslgVHINVVLVRMIMLGYAKSISLieRGNPSRSLENVCR 334
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 335 WacqqQKTDPNHAEHHDHAIFLTRQDFGPaGMQGYAPVTGMCHPVRSCTLNHEDG---FSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04269    76 W----KRSNLLPRKPHDNAQLLTGRDFDG-NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039771792 412 GNRCGDETAmgsVMAPlvQAAFHRYHWSRCSGQELKRYIHSYD--CLLD 458
Cdd:cd04269   151 GCTCGRSTC---IMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 258-442 1.68e-25

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 104.42  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 258 IEVLLGVDDSVVR-FHGKE-HVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIErGNPSRSLENVCRW 335
Cdd:cd04267     3 IELVVVADHRMVSyFNSDEnILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPID-SDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 acqQQKTDPnhaeHHDHAIFLTRQDFGPAGMQGYAPVTGMCHPVRSCTL--NHEDGFSSAFVVAHETGHVLGMEHDGQGN 413
Cdd:cd04267    82 ---RAEGPI----RHDNAVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGGDE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039771792 414 RCGDETAMGS-VMAPlVQAAFHRYHWSRCS 442
Cdd:cd04267   155 LAFECDGGGNyIMAP-VDSGLNSYRFSQCS 183
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-540 3.65e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 93.18  E-value: 3.65e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771792 472 PGINYSMDEQCRFDFGVGYKMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECAAGKWCYKGHC 540
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKC 67
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 258-460 1.07e-21

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: 93.52  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 258 IEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHdeslGVHINVVLVRMIMLGYAKSISLIerGNPSRSLENVCRW 335
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDKIDVS--GDANDTLRNFLKW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 acQQQKTDPNHAehHDHAIFLTRQDFGpAGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHDGQG 412
Cdd:pfam01421  77 --RQEYLKKRKP--HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039771792 413 NRCGDETAMGSVMAPLVQAAFHRyHWSRCSGQELKRYIHSYD--CLLDDP 460
Cdd:pfam01421 152 GGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 554-605 2.35e-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: 76.47  E-value: 2.35e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771792  554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 258-450 3.27e-11

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: 62.54  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 258 IEVLLGVDDsvvRFHGKEHVQNYLLTLMNIVNEIYHDEsLGVHInvvlvrmimlgyakSISLIERGnpsrslenvcrwac 337
Cdd:cd00203     3 IPYVVVADD---RDVEEENLSAQIQSLILIAMQIWRDY-LNIRF--------------VLVGVEID-------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 338 qqqktdpnhaeHHDHAIFLTRQDFgPAGMQGYAPVTGMCHPVRSCTL---NHEDGFSSAFVVAHETGHVLGMEHDGqGNR 414
Cdd:cd00203    51 -----------KADIAILVTRQDF-DGGTGGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDH-DRK 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039771792 415 CGDE------------TAMGSVMAPLVQAAFH--RYHWSRCSGQELKRYI 450
Cdd:cd00203   118 DRDDyptiddtlnaedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 1.13e-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: 59.34  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSkeTGDVAYMKQ--LVHDGTRCSYKDP-----Y 676
Cdd:pfam19236   4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRA--IGESFIMKRgdSFLDGTRCMPSGPredgtL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039771792 677 SICVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236  80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
260-427 7.77e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.27  E-value: 7.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 260 VLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESlgvHINVVLVRMIMLGYAKSISLIERGNPSRS--LENVcrwac 337
Cdd:pfam13688   7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDSSdrLSEF----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 338 qQQKTDPNHAEHHDHAIFLTRQDFGPAGMqGYAPVTGMCHPVRSCTLNHEDGF------SSAFVVAHETGHVLGMEHDGQ 411
Cdd:pfam13688  79 -QDFSAWRGTQNDDLAYLFLMTNCSGGGL-AWLGQLCNSGSAGSVSTRVSGNNvvvstaTEWQVFAHEIGHNFGAVHDCD 156

                         170
                  ....*....|....*.
gi 1039771792 412 GNRCGDETAMGSVMAP 427
Cdd:pfam13688 157 SSTSSQCCPPSNSTCP 172
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-605 4.34e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 4.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039771792 552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPTPinGGQDCPGVNFEYQLCNTEEC 605
Cdd:pfam00090   1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 257-453 9.40e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 53.51  E-value: 9.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 257 NIEVLLGVDDSVVRFHGK-EHVQNYLLTLMNIVNEIYHDESlGVHINVVLVRMIMLGYAKSISLIERGNPSRSLENVCRW 335
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771792 336 ACQQQKTDPNHAEHHDHAIFLTRQDF-----GPA--GMQGYAPVTGMC--HPVRSCtlnhED---GFSSAFVVAHETGHV 403
Cdd:cd04272    81 NFNEYVKKKRDYFNPDVVFLVTGLDMstysgGSLqtGTGGYAYVGGACteNRVAMG----EDtpgSYYGVYTMTHELAHL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771792 404 LGMEHDGQ---GNRCGDETAM------GSVMAPLVQAAFHrYHWSRCSGQELKRYIHSY 453
Cdd:cd04272   157 LGAPHDGSpppSWVKGHPGSLdcpwddGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRL 214
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 552-605 1.32e-07

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: 48.81  E-value: 1.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039771792 552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPtPINGGQDCPGVNfEYQLCNTEEC 605
Cdd:pfam19028   4 SEWSEWS---ECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 558-605 1.53e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.43  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039771792 558 TKFGSCSRTCGTGVRFRTRQCNNPTP--INGGQDCPGVN--FEYQLCNTEEC 605
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKkpPETQSCNLKPC 55
M6dom_TIGR03296 TIGR03296
M6 family metalloprotease domain; This model describes a metalloproteinase domain, with a ...
 383-423 2.94e-03

M6 family metalloprotease domain; This model describes a metalloproteinase domain, with a characteristic HExxH motif. Examples of this domain are found in proteins in the family of immune inhibitor A, which cleaves antibacterial peptides, and in other, only distantly related proteases. This model is built to be broader and more inclusive than pfam05547.


Pssm-ID: 274507 [Multi-domain]  Cd Length: 285  Bit Score: 40.47  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039771792 383 TLNHEDGfsSAFVVAHETGHVLGM------EHDGQGNRCGDETAMGS 423
Cdd:TIGR03296 158 TIQPEDG--GIGVFAHELGHDLGLpdlydtQYDGGGEPVGYWSLMSS 202
 
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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