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Conserved domains on  [gi|1907075041|ref|XP_036011668|]
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A disintegrin and metalloproteinase with thrombospondin motifs 14 isoform X1 [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) ...
 246-444 2.03e-90

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: 287.60  E-value: 2.03e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  246 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 325
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907075041  399 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 444
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 73-194 1.81e-34

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: 128.20  E-value: 1.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041   73 RSPLSLERETPRPGGPRQHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQQE-CVYTGGVTGMPG 150
Cdd:pfam01562    7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGHPD 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907075041  151 AAVAISNCDGLAGLIRTDNSDYFIEPLErgQQEKEAGGRTHVVY 194
Cdd:pfam01562   87 SSVALSTCSGLRGFIRTENEEYLIEPLE--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 ...
 702-816 3.06e-24

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: 98.42  E-value: 3.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  702 TVKGTLGKGsKQAAALKQVQIPAGARHIQIELLEKAPHRIAVKNqVTGSFIFNPKGK-EASSRTFTALGLEWEHE-AEDT 779
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRrSLPA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907075041  780 KDSLRTNGPLPEAIAILVLPPAEGKPRGSLAYKYVIH 816
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 459-528 5.33e-22

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: 90.48  E-value: 5.33e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  459 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 528
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 542-594 2.89e-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: 2.89e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1907075041   542 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRPCSGSMFEYQICNSEDCP 594
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 838-893 9.55e-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: 57.85  E-value: 9.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075041  838 WALKSWSPCSKACGGGIQFTKYGCRRRRDHHMVHRHLCDHKKRPkPIRRRCNQHSC 893
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1008 2.02e-09

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: 54.38  E-value: 2.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907075041  959 WRTGAWSQCSATCGEGIQQRQVVCRNTSSALGP----CEGV-KPDMVQICSLPAC 1008
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpdseCSAQkKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 599-700 2.57e-09

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 55.87  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  599 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSDAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 668
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907075041  669 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 700
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 898-955 2.27e-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: 51.30  E-value: 2.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075041  898 WVTEEWGACSRSCGKlGLQTRGVQCLLPLSNGTHkamPAKACLGN-RPEAKKPCLRVPC 955
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIV---PDSECSAQkKPPETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 246-444 2.03e-90

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: 287.60  E-value: 2.03e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  246 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 325
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907075041  399 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 444
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 73-194 1.81e-34

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: 128.20  E-value: 1.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041   73 RSPLSLERETPRPGGPRQHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQQE-CVYTGGVTGMPG 150
Cdd:pfam01562    7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGHPD 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907075041  151 AAVAISNCDGLAGLIRTDNSDYFIEPLErgQQEKEAGGRTHVVY 194
Cdd:pfam01562   87 SSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 702-816 3.06e-24

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: 98.42  E-value: 3.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  702 TVKGTLGKGsKQAAALKQVQIPAGARHIQIELLEKAPHRIAVKNqVTGSFIFNPKGK-EASSRTFTALGLEWEHE-AEDT 779
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRrSLPA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907075041  780 KDSLRTNGPLPEAIAILVLPPAEGKPRGSLAYKYVIH 816
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 248-447 6.05e-23

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 97.76  E-value: 6.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYhdESLGAHVNIALVRLIMVGYRQSLSlierGNPARSLEQVCRW 325
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIY--KELNIRVVLVGLEIWTDEDKIDVS----GDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 AHSQ--QRQDpshtehHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALN---HEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:pfam01421   77 RQEYlkKRKP------HDVAQLLSGVEFGGTtvGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDF 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907075041  399 GNGCDDETSLGSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYD--CLLDDP 447
Cdd:pfam01421  151 NGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 459-528 5.33e-22

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: 90.48  E-value: 5.33e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  459 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 528
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 542-594 2.89e-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: 2.89e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1907075041   542 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRPCSGSMFEYQICNSEDCP 594
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 838-893 9.55e-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: 57.85  E-value: 9.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075041  838 WALKSWSPCSKACGGGIQFTKYGCRRRRDHHMVHRHLCDHKKRPkPIRRRCNQHSC 893
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1008 2.02e-09

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: 54.38  E-value: 2.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907075041  959 WRTGAWSQCSATCGEGIQQRQVVCRNTSSALGP----CEGV-KPDMVQICSLPAC 1008
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpdseCSAQkKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 599-700 2.57e-09

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 55.87  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  599 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSDAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 668
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907075041  669 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 700
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
540-593 1.76e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.76e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907075041  540 GGWSSWTnfgSCSRSCGGGVRSRSRSCDNPPPayGGRPCSGSMFEYQICNSEDC 593
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 898-955 2.27e-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: 51.30  E-value: 2.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075041  898 WVTEEWGACSRSCGKlGLQTRGVQCLLPLSNGTHkamPAKACLGN-RPEAKKPCLRVPC 955
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIV---PDSECSAQkKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 959-1008 2.46e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.35  E-value: 2.46e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1907075041   959 WRTGAWSQCSATCGEGIQQRQVVCRNTSSALG--PCEGVKPDmVQICSLPAC 1008
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVE-TRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 898-956 8.82e-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: 41.03  E-value: 8.82e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075041   898 WVTEEWGACSRSCGKlGLQTRGVQCLLPLSNGthkamPAKACLGNRPEaKKPCLRVPCP 956
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQN-----GGGPCTGEDVE-TRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 842-894 4.27e-03

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: 36.41  E-value: 4.27e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1907075041   842 SWSPCSKACGGGIQftkygcRRRRDHHMVHRHLCDHK-KRPKPIRRRCNQHSCP 894
Cdd:smart00209    6 EWSPCSVTCGGGVQ------TRTRSCCSPPPQNGGGPcTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 246-444 2.03e-90

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: 287.60  E-value: 2.03e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  246 YSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIeRGNPARSLEQVCRW 325
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 AHSQQRQDPSHTEHHDHVIFLTRQNF-------GPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907075041  399 GNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 444
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 73-194 1.81e-34

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: 128.20  E-value: 1.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041   73 RSPLSLERETPRPGGPRQHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEW-QEDFRELFRQPLQQE-CVYTGGVTGMPG 150
Cdd:pfam01562    7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYYQGHVEGHPD 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907075041  151 AAVAISNCDGLAGLIRTDNSDYFIEPLErgQQEKEAGGRTHVVY 194
Cdd:pfam01562   87 SSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 248-445 2.58e-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: 101.54  E-value: 2.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYHDeslgAHVNIALVRLIMVGYRQSLSLieRGNPARSLEQVCRW 325
Cdd:cd04269      3 VELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLDW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 ahsqQRQDPSHTEHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALNHEDG---FSSAFVVAHETGHVLGMEHDG--- 397
Cdd:cd04269     77 ----KRSNLLPRKPHDNAQLLTGRDFDGNtvGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDggc 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907075041  398 --QGNGCddetslgsVMAPlvQAAFHRFHWSRCSKLELSRYLPSYD--CLLD 445
Cdd:cd04269    153 tcGRSTC--------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 ...
 702-816 3.06e-24

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: 98.42  E-value: 3.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  702 TVKGTLGKGsKQAAALKQVQIPAGARHIQIELLEKAPHRIAVKNqVTGSFIFNPKGK-EASSRTFTALGLEWEHE-AEDT 779
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRrSLPA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907075041  780 KDSLRTNGPLPEAIAILVLPPAEGKPRGSLAYKYVIH 816
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQYGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 248-430 1.23e-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: 99.42  E-value: 1.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMvgyRQSLSLIERGNP--ARSLEQVC 323
Cdd:cd04267      3 IELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQI---LKGEQFAPPIDSdaSNTLNSFS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  324 RWahsqQRQDPSHtehHDHVIFLTRQNFGPS---GYAPVTGMCHPLRSCAL--NHEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:cd04267     80 FW----RAEGPIR---HDNAVLLTAQDFIEGdilGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGG 152

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907075041  399 GNGCDDETSLGS-VMAPLVQAAFHRfHWSRCSK 430
Cdd:cd04267    153 DELAFECDGGGNyIMAPVDSGLNSY-RFSQCSI 184
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 248-447 6.05e-23

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 97.76  E-value: 6.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDDSVVRFHGR--EHTQNYVLTLMNIVDEIYhdESLGAHVNIALVRLIMVGYRQSLSlierGNPARSLEQVCRW 325
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIY--KELNIRVVLVGLEIWTDEDKIDVS----GDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  326 AHSQ--QRQDpshtehHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCALN---HEDGFSSAFVVAHETGHVLGMEHDGQ 398
Cdd:pfam01421   77 RQEYlkKRKP------HDVAQLLSGVEFGGTtvGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDF 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907075041  399 GNGCDDETSLGSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYD--CLLDDP 447
Cdd:pfam01421  151 NGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 459-528 5.33e-22

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: 90.48  E-value: 5.33e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  459 PGIDYSMDEQCRFDFGTGYHTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 528
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 542-594 2.89e-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: 2.89e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1907075041   542 WSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRPCSGSMFEYQICNSEDCP 594
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
250-414 2.79e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 66.67  E-value: 2.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  250 VLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESlgaHVNIALVRLIMVGYRQSlsliERGNPARSLEQVCRWAHSQ 329
Cdd:pfam13688    7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCP----YTPPACSTGDSSDRLSEFQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  330 QRQDPSHTEHHDHVIFLTRQNFGPSGYAPVTGMCHPLRSCALNHEDGF--------SSAFVVAHETGHVLGMEHDGQGNG 401
Cdd:pfam13688   80 DFSAWRGTQNDDLAYLFLMTNCSGGGLAWLGQLCNSGSAGSVSTRVSGnnvvvstaTEWQVFAHEIGHNFGAVHDCDSST 159

                          170
                   ....*....|...
gi 1907075041  402 CDDETSLGSVMAP 414
Cdd:pfam13688  160 SSQCCPPSNSTCP 172
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 248-437 6.74e-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: 62.15  E-value: 6.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDDsvvRFHGREHTQNYVLTLMNIVDEIYHDEsLGAHVNIALVRLImvgyrqslsliergnparsleqvcrwah 327
Cdd:cd00203      3 IPYVVVADD---RDVEEENLSAQIQSLILIAMQIWRDY-LNIRFVLVGVEID---------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  328 sqqrqdpshteHHDHVIFLTRQNFGPS--GYAPVTGMCHPLRSCAL---NHEDGFSSAFVVAHETGHVLGMEHDGQGNGC 402
Cdd:cd00203     51 -----------KADIAILVTRQDFDGGtgGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDRKDR 119

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907075041  403 DDE-----------TSLGSVMAPLVQAAFH--RFHWSRCSKLELSRYL 437
Cdd:cd00203    120 DDYptiddtlnaedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 838-893 9.55e-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: 57.85  E-value: 9.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907075041  838 WALKSWSPCSKACGGGIQFTKYGCRRRRDHHMVHRHLCDHKKRPkPIRRRCNQHSC 893
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1008 2.02e-09

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: 54.38  E-value: 2.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907075041  959 WRTGAWSQCSATCGEGIQQRQVVCRNTSSALGP----CEGV-KPDMVQICSLPAC 1008
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpdseCSAQkKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 599-700 2.57e-09

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 55.87  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  599 DFRAQQCAKRNSYYTHQD----AKHSWLPYEPDSDAQK-CELICQSADTGDVVFMNQVVHDGTRCSYRDP-----YSVCA 668
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907075041  669 RGECVPFGCDKEVGSMKTDDKCGVCGGDNSHC 700
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 248-443 2.87e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 58.52  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  248 IEVLLAVDdsvvRFHGREHTQN-----YVLTLMNIVDEIYHDESlGAHVNIALVRLIMVGYRQSLSLIERGNP-----AR 317
Cdd:cd04272      3 PELFVVVD----YDHQSEFFSNeqlirYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYgyidaAE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075041  318 SLEQVCrwAHSQQRqdpSHTEHHDHVIFLTRQ----------NFGPSGYAPVTGMCHPLRsCALNHEDG--FSSAFVVAH 385
Cdd:cd04272     78 TLENFN--EYVKKK---RDYFNPDVVFLVTGLdmstysggslQTGTGGYAYVGGACTENR-VAMGEDTPgsYYGVYTMTH 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075041  386 ETGHVLGMEHDGQG-----------NGCDDEtsLGSVMAPLVQAAFHrFHWSRCSKLELSRYL--PSYDCL 443
Cdd:cd04272    152 ELAHLLGAPHDGSPppswvkghpgsLDCPWD--DGYIMSYVVNGERQ-YRFSQCSQRQIRNVFrrLGASCL 219
TSP_1 pfam00090
Thrombospondin type 1 domain;
540-593 1.76e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.76e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907075041  540 GGWSSWTnfgSCSRSCGGGVRSRSRSCDNPPPayGGRPCSGSMFEYQICNSEDC 593
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 898-955 2.27e-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: 51.30  E-value: 2.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075041  898 WVTEEWGACSRSCGKlGLQTRGVQCLLPLSNGTHkamPAKACLGN-RPEAKKPCLRVPC 955
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIV---PDSECSAQkKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
961-1008 1.68e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.57  E-value: 1.68e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907075041  961 TGAWSQCSATCGEGIQQRQVVCRNTSSALGPCEGvKPDMVQICSLPAC 1008
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTG-DDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 959-1008 2.46e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.35  E-value: 2.46e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1907075041   959 WRTGAWSQCSATCGEGIQQRQVVCRNTSSALG--PCEGVKPDmVQICSLPAC 1008
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVE-TRACNEQPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 543-593 5.85e-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: 47.27  E-value: 5.85e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907075041  543 SSWTNFGSCSRSCGGGVRSRSRSCDNpPPAYGGRPCsGSMFEYQICNSEDC 593
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPC-PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 898-956 8.82e-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: 41.03  E-value: 8.82e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907075041   898 WVTEEWGACSRSCGKlGLQTRGVQCLLPLSNGthkamPAKACLGNRPEaKKPCLRVPCP 956
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQN-----GGGPCTGEDVE-TRACNEQPCP 53
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 351-412 1.80e-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: 1.80e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907075041  351 FGPSGYAPVTGMCHPLRSCALNHEDGFSSAF---VVAHETGHVLGMEHDGQGNGCDDETSL-------GSVM 412
Cdd:cd04268     63 YGPSQVDPLTGEILLARVYLYSSFVEYSGARlrnTAEHELGHALGLRHNFAASDRDDNVDLlaekgdtSSVM 134
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 842-894 4.27e-03

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: 36.41  E-value: 4.27e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1907075041   842 SWSPCSKACGGGIQftkygcRRRRDHHMVHRHLCDHK-KRPKPIRRRCNQHSCP 894
Cdd:smart00209    6 EWSPCSVTCGGGVQ------TRTRSCCSPPPQNGGGPcTGEDVETRACNEQPCP 53
 
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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