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Conserved domains on  [gi|294345398|ref|NP_808540|]
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A disintegrin and metalloproteinase with thrombospondin motifs 3 isoform 1 precursor [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 5.99e-96

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: 304.93  E-value: 5.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 294345398  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 7.79e-40

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: 143.61  E-value: 7.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398    43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562    1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   123 prnshlhgSASEGSWRSEPLQT-SCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLErgKQMDEENGRIHVVY 201
Cdd:pfam01562   59 --------LDGGTGVESPPVQTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_spacer1 super family cl20316
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 714-828 3.71e-26

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.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 104.20  E-value: 3.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   714 TVKGTFTRtprklGKTRGA--FV-LPKGARNISLAETRETKNVLAIKNqATGHYILNGKGE-EAKSRTFIDLGVEWDYNI 789
Cdd:pfam05986    1 TVSGSFTE-----GRAKGYvtFVtIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRR 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 294345398   790 -EDDIETLHTDGPLHDPVIVLIIPQ-ENDTRSSLTYKYIIH 828
Cdd:pfam05986   75 sLPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-540 3.69e-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: 93.95  E-value: 3.69e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   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 1.63e-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: 74.55  E-value: 1.63e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 294345398    554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 971-1016 6.12e-11

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: 58.62  E-value: 6.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 294345398   971 WKTGSWNECSVTCGEGTEVRQVLCRT-------GDH-CDG-EKPESVRPCQLPPC 1016
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsivPDSeCSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 850-905 1.12e-10

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: 57.85  E-value: 1.12e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 294345398   850 WALKSWSQCSEPCGGGFQYTKYGCRRKSDSKMVHRSFCEVNKKPkPIRRMCNIQEC 905
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 4.29e-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: 58.18  E-value: 4.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSKETGDVAYMKQLVHDGTRCSYKDP-----YSI 678
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 294345398   679 CVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 910-967 8.56e-08

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 49.76  E-value: 8.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   910 WAADEWEHCSRSCGsSGNQLRTVRCLQPlqdGTNRSVHSKYCLGD-RPESRRPCNRVPC 967
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQK---GGGSIVPDSECSAQkKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1024-1052 8.24e-03

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 35.20  E-value: 8.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 294345398  1024 DKSIFCQMEVLARYCSIPGYNKLCCESCS 1052
Cdd:pfam08686    3 DKFANCSLVVQARLCSHKYYRQFCCRSCS 31
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 256-457 5.99e-96

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: 304.93  E-value: 5.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 294345398  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 7.79e-40

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: 143.61  E-value: 7.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398    43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562    1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   123 prnshlhgSASEGSWRSEPLQT-SCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLErgKQMDEENGRIHVVY 201
Cdd:pfam01562   59 --------LDGGTGVESPPVQTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 714-828 3.71e-26

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: 104.20  E-value: 3.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   714 TVKGTFTRtprklGKTRGA--FV-LPKGARNISLAETRETKNVLAIKNqATGHYILNGKGE-EAKSRTFIDLGVEWDYNI 789
Cdd:pfam05986    1 TVSGSFTE-----GRAKGYvtFVtIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRR 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 294345398   790 -EDDIETLHTDGPLHDPVIVLIIPQ-ENDTRSSLTYKYIIH 828
Cdd:pfam05986   75 sLPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-540 3.69e-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: 93.95  E-value: 3.69e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   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 3.09e-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: 95.83  E-value: 3.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   258 IEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHdeslGVHINVVLVRMIMLGYAKSISLIerGNPSRSLENVCRW 335
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDKIDVS--GDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   336 acQQQKTDPNHAehHDHAIFLTRQDFGpAGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHDGQG 412
Cdd:pfam01421   77 --RQEYLKKRKP--HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 294345398   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 1.63e-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: 74.55  E-value: 1.63e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 294345398    554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 971-1016 6.12e-11

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: 58.62  E-value: 6.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 294345398   971 WKTGSWNECSVTCGEGTEVRQVLCRT-------GDH-CDG-EKPESVRPCQLPPC 1016
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsivPDSeCSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 850-905 1.12e-10

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: 57.85  E-value: 1.12e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 294345398   850 WALKSWSQCSEPCGGGFQYTKYGCRRKSDSKMVHRSFCEVNKKPkPIRRMCNIQEC 905
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 4.29e-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: 58.18  E-value: 4.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSKETGDVAYMKQLVHDGTRCSYKDP-----YSI 678
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 294345398   679 CVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 971-1016 5.53e-08

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: 50.28  E-value: 5.53e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 294345398    971 WKTGSWNECSVTCGEGTEVRQVLCRT------GDHCDGEKPESvRPCQLPPC 1016
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVET-RACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 910-967 8.56e-08

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: 49.76  E-value: 8.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   910 WAADEWEHCSRSCGsSGNQLRTVRCLQPlqdGTNRSVHSKYCLGD-RPESRRPCNRVPC 967
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQK---GGGSIVPDSECSAQkKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-605 2.17e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.57  E-value: 2.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 294345398   552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPTPinGGQDCPGVNFEYQLCNTEEC 605
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 914-968 2.17e-05

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: 42.96  E-value: 2.17e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 294345398    914 EWEHCSRSCGsSGNQLRTVRCLQPlqdgtNRSVHSKYCLGDRPESrRPCNRVPCP 968
Cdd:smart00209    6 EWSPCSVTCG-GGVQTRTRSCCSP-----PPQNGGGPCTGEDVET-RACNEQPCP 53
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 969-1028 2.88e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 41.47  E-value: 2.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294345398  969 AQWktGSWNECSVTCG--EGTEVRQVLC--RTGDHCDGEKPESvRPCQ--LPPCNDEPCLGDKSIF 1028
Cdd:PTZ00087  234 TEW--GEWSNCSMECDhpDNVQIRERKCahPSGDCFKGDLKET-RPCQvpLPPCNSLFEHKESSTF 296
M6dom_TIGR03296 TIGR03296
M6 family metalloprotease domain; This model describes a metalloproteinase domain, with a ...
 383-423 4.87e-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: 4.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 294345398   383 TLNHEDGfsSAFVVAHETGHVLGM------EHDGQGNRCGDETAMGS 423
Cdd:TIGR03296  158 TIQPEDG--GIGVFAHELGHDLGLpdlydtQYDGGGEPVGYWSLMSS 202
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1024-1052 8.24e-03

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 35.20  E-value: 8.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 294345398  1024 DKSIFCQMEVLARYCSIPGYNKLCCESCS 1052
Cdd:pfam08686    3 DKFANCSLVVQARLCSHKYYRQFCCRSCS 31
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 256-457 5.99e-96

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: 304.93  E-value: 5.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  256 YNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIeRGNPSRSLENVCRW 335
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  336 ACQQQKTDPNHAEHHDHAIFLTRQDF----GPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 294345398  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 7.79e-40

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: 143.61  E-value: 7.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398    43 ELVTPVSTNlkghylshilsANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHetaprpgnttd 122
Cdd:pfam01562    1 EVVIPVRLD-----------PSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYY----------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   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 4.38e-28

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: 112.32  E-value: 4.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  257 NIEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHDeslgVHINVVLVRMIMLGYAKSISLieRGNPSRSLENVCR 334
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  335 WacqqQKTDPNHAEHHDHAIFLTRQDFGPaGMQGYAPVTGMCHPVRSCTLNHEDG---FSSAFVVAHETGHVLGMEHDGQ 411
Cdd:cd04269    76 W----KRSNLLPRKPHDNAQLLTGRDFDG-NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 294345398  412 GNRCGDETAmgsVMAPlvQAAFHRYHWSRCSGQELKRYIHSYD--CLLD 458
Cdd:cd04269   151 GCTCGRSTC---IMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 714-828 3.71e-26

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: 104.20  E-value: 3.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   714 TVKGTFTRtprklGKTRGA--FV-LPKGARNISLAETRETKNVLAIKNqATGHYILNGKGE-EAKSRTFIDLGVEWDYNI 789
Cdd:pfam05986    1 TVSGSFTE-----GRAKGYvtFVtIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRR 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 294345398   790 -EDDIETLHTDGPLHDPVIVLIIPQ-ENDTRSSLTYKYIIH 828
Cdd:pfam05986   75 sLPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 258-442 9.91e-26

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: 105.58  E-value: 9.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  258 IEVLLGVDDSVVR-FHGKE-HVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIErGNPSRSLENVCRW 335
Cdd:cd04267     3 IELVVVADHRMVSyFNSDEnILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPID-SDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  336 acqQQKTDPnhaeHHDHAIFLTRQDFGPAGMQGYAPVTGMCHPVRSCTL--NHEDGFSSAFVVAHETGHVLGMEHDGQGN 413
Cdd:cd04267    82 ---RAEGPI----RHDNAVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGGDE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 294345398  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 3.69e-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: 93.95  E-value: 3.69e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   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 3.09e-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: 95.83  E-value: 3.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   258 IEVLLGVDDSVVRFHGK--EHVQNYLLTLMNIVNEIYHdeslGVHINVVLVRMIMLGYAKSISLIerGNPSRSLENVCRW 335
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDKIDVS--GDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   336 acQQQKTDPNHAehHDHAIFLTRQDFGpAGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHDGQG 412
Cdd:pfam01421   77 --RQEYLKKRKP--HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 294345398   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 1.63e-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: 74.55  E-value: 1.63e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 294345398    554 WGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEEC 605
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 258-450 6.39e-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: 65.24  E-value: 6.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  258 IEVLLGVDDsvvRFHGKEHVQNYLLTLMNIVNEIYHDEsLGVHInvvlvrmimlgyakSISLIERGnpsrslenvcrwac 337
Cdd:cd00203     3 IPYVVVADD---RDVEEENLSAQIQSLILIAMQIWRDY-LNIRF--------------VLVGVEID-------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  338 qqqktdpnhaeHHDHAIFLTRQDFgPAGMQGYAPVTGMCHPVRSCTL---NHEDGFSSAFVVAHETGHVLGMEHDGqGNR 414
Cdd:cd00203    51 -----------KADIAILVTRQDF-DGGTGGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDH-DRK 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 294345398  415 CGDE------------TAMGSVMAPLVQAAFH--RYHWSRCSGQELKRYI 450
Cdd:cd00203   118 DRDDyptiddtlnaedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 971-1016 6.12e-11

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: 58.62  E-value: 6.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 294345398   971 WKTGSWNECSVTCGEGTEVRQVLCRT-------GDH-CDG-EKPESVRPCQLPPC 1016
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsivPDSeCSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 850-905 1.12e-10

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: 57.85  E-value: 1.12e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 294345398   850 WALKSWSQCSEPCGGGFQYTKYGCRRKSDSKMVHRSFCEVNKKPkPIRRMCNIQEC 905
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 611-712 4.29e-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: 58.18  E-value: 4.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   611 DFRAQQCQQRNSHFDYQN----TKHHW---LPHEHPDSkkRCHLYCQSKETGDVAYMKQLVHDGTRCSYKDP-----YSI 678
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDA--LCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 294345398   679 CVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHC 712
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
260-427 8.34e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.66  E-value: 8.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   260 VLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESlgvHINVVLVRMIMLGYAKSISLIERGNPSRS--LENVcrwac 337
Cdd:pfam13688    7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDSSdrLSEF----- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398   338 qQQKTDPNHAEHHDHAIFLTRQDFGPAGMqGYAPVTGMCHPVRSCTLNHEDGF------SSAFVVAHETGHVLGMEHDGQ 411
Cdd:pfam13688   79 -QDFSAWRGTQNDDLAYLFLMTNCSGGGL-AWLGQLCNSGSAGSVSTRVSGNNvvvstaTEWQVFAHEIGHNFGAVHDCD 156

                          170
                   ....*....|....*.
gi 294345398   412 GNRCGDETAMGSVMAP 427
Cdd:pfam13688  157 SSTSSQCCPPSNSTCP 172
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 257-456 4.65e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 55.05  E-value: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  257 NIEVLLGVDDSVVRFHGK-EHVQNYLLTLMNIVNEIYHDESlGVHINVVLVRMIMLGYAKSISLIERGNPSRSLENVCRW 335
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294345398  336 ACQQQKTDPNHAEHHDHAIFLTRQDF-----GPA--GMQGYAPVTGMC--HPVRSCtlnhED---GFSSAFVVAHETGHV 403
Cdd:cd04272    81 NFNEYVKKKRDYFNPDVVFLVTGLDMstysgGSLqtGTGGYAYVGGACteNRVAMG----EDtpgSYYGVYTMTHELAHL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294345398  404 LGMEHDGQ---GNRCGDETAM------GSVMAPLVQAAFHrYHWSRCSGQELKRYIHSYD--CL 456
Cdd:cd04272   157 LGAPHDGSpppSWVKGHPGSLdcpwddGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGasCL 219
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 971-1016 5.53e-08

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: 50.28  E-value: 5.53e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 294345398    971 WKTGSWNECSVTCGEGTEVRQVLCRT------GDHCDGEKPESvRPCQLPPC 1016
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVET-RACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 910-967 8.56e-08

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: 49.76  E-value: 8.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 294345398   910 WAADEWEHCSRSCGsSGNQLRTVRCLQPlqdGTNRSVHSKYCLGD-RPESRRPCNRVPC 967
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQK---GGGSIVPDSECSAQkKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-605 2.17e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.57  E-value: 2.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 294345398   552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPTPinGGQDCPGVNFEYQLCNTEEC 605
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 552-605 5.33e-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: 47.66  E-value: 5.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 294345398   552 GNWGSWTkfgSCSRTCGTGVRFRTRQCNNPtPINGGQDCPGVNfEYQLCNTEEC 605
Cdd:pfam19028    4 SEWSEWS---ECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 914-968 2.17e-05

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: 42.96  E-value: 2.17e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 294345398    914 EWEHCSRSCGsSGNQLRTVRCLQPlqdgtNRSVHSKYCLGDRPESrRPCNRVPCP 968
Cdd:smart00209    6 EWSPCSVTCG-GGVQTRTRSCCSP-----PPQNGGGPCTGEDVET-RACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
973-1016 3.06e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.41  E-value: 3.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 294345398   973 TGSWNECSVTCGEGTEVRQVLC----RTGDHCDGEKPEsVRPCQLPPC 1016
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIE-TQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 974-1016 9.60e-04

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: 38.41  E-value: 9.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 294345398   974 GSWNECSVTCGEGTEVRQvlcRT--------GDHCdgekPES--VRPCQLPPC 1016
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRT---RTvivepqngGRPC----PELleRRPCNLPPC 52
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 969-1028 2.88e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 41.47  E-value: 2.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294345398  969 AQWktGSWNECSVTCG--EGTEVRQVLC--RTGDHCDGEKPESvRPCQ--LPPCNDEPCLGDKSIF 1028
Cdd:PTZ00087  234 TEW--GEWSNCSMECDhpDNVQIRERKCahPSGDCFKGDLKET-RPCQvpLPPCNSLFEHKESSTF 296
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 558-605 4.35e-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: 36.66  E-value: 4.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 294345398   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 4.87e-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: 4.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 294345398   383 TLNHEDGfsSAFVVAHETGHVLGM------EHDGQGNRCGDETAMGS 423
Cdd:TIGR03296  158 TIQPEDG--GIGVFAHELGHDLGLpdlydtQYDGGGEPVGYWSLMSS 202
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1024-1052 8.24e-03

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 35.20  E-value: 8.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 294345398  1024 DKSIFCQMEVLARYCSIPGYNKLCCESCS 1052
Cdd:pfam08686    3 DKFANCSLVVQARLCSHKYYRQFCCRSCS 31
 
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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