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Conserved domains on  [gi|16306598|gb|AAL17652|]
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von Willebrand factor-cleaving protease precursor [Homo sapiens]

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) ...
 80-283 9.47e-88

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: 283.75  E-value: 9.47e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598   80 LHLELLVAVGPDVFQ-AHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWS 158
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  159 QTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAp 238
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16306598  239 GSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 283
Cdd:cd04273  160 GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 441-555 2.13e-74

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: 242.31  E-value: 2.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    441 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 520
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 16306598    521 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 555
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 557-680 1.05e-50

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: 174.30  E-value: 1.05e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    557 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 635
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 16306598    636 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 680
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 301-371 1.00e-17

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: 78.54  E-value: 1.00e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16306598    301 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 371
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 387-439 1.75e-14

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: 69.15  E-value: 1.75e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 16306598     387 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 439
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1076-1130 1.47e-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: 1.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16306598   1076 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1130
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1012 4.97e-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: 50.53  E-value: 4.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    955 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 1012
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 746-804 4.64e-07

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: 47.83  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    746 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 804
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1016-1072 5.59e-07

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: 47.83  E-value: 5.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16306598   1016 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 1072
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 902-951 9.04e-04

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: 38.59  E-value: 9.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 16306598    902 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 951
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 80-283 9.47e-88

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: 283.75  E-value: 9.47e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598   80 LHLELLVAVGPDVFQ-AHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWS 158
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  159 QTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAp 238
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16306598  239 GSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 283
Cdd:cd04273  160 GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 441-555 2.13e-74

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: 242.31  E-value: 2.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    441 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 520
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 16306598    521 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 555
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 557-680 1.05e-50

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: 174.30  E-value: 1.05e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    557 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 635
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 16306598    636 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 680
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 301-371 1.00e-17

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: 78.54  E-value: 1.00e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16306598    301 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 371
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 387-439 1.75e-14

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: 69.15  E-value: 1.75e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 16306598     387 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 439
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 124-286 6.19e-12

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: 66.17  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    124 FRVHLVKMVILTEpEGAPNITANLTSSLLSVCGWSQT-INPEDDTDpgHADLVLYITrfdlelPDGNRQvrGVTQLGGAC 202
Cdd:pfam01421   44 IRVVLVGLEIWTD-EDKIDVSGDANDTLRNFLKWRQEyLKKRKPHD--VAQLLSGVE------FGGTTV--GAAYVGGMC 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    203 SPTWSCLITEDTGFD---LGVTIAHEIGHSFGLEHD-GAPGSGCGPSGH-VM-ASDGAAPraGLAWSPCSRRQLLSLLSA 276
Cdd:pfam01421  113 SLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHDdFNGGCKCPPGGGcIMnPSAGSSF--PRKFSNCSQEDFEQFLTK 190

                          170
                   ....*....|
gi 16306598    277 GRARCVWDPP 286
Cdd:pfam01421  191 QKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1076-1130 1.47e-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: 1.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16306598   1076 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1130
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
388-438 2.12e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 2.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 16306598    388 SSWGPRSPCSRSCGGGVVTRRRQCNNPRPafGGRACVGADLQAEMCNTQAC 438
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1012 4.97e-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: 50.53  E-value: 4.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    955 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 1012
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 746-804 4.64e-07

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: 47.83  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    746 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 804
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1016-1072 5.59e-07

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: 47.83  E-value: 5.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16306598   1016 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 1072
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 902-951 9.04e-04

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.59  E-value: 9.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 16306598    902 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 951
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 80-283 9.47e-88

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: 283.75  E-value: 9.47e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598   80 LHLELLVAVGPDVFQ-AHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWS 158
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  159 QTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAp 238
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16306598  239 GSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 283
Cdd:cd04273  160 GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 441-555 2.13e-74

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: 242.31  E-value: 2.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    441 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 520
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 16306598    521 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 555
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 557-680 1.05e-50

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: 174.30  E-value: 1.05e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    557 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 635
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 16306598    636 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 680
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 93-269 4.65e-24

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: 100.96  E-value: 4.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598   93 FQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTinpeddtDPGHA 172
Cdd:cd04267   17 FNSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWRAE-------GPIRH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  173 DLVLYITRFDLELPDGNrqvrGVTQLGGACSPTWSCLITEDTGFDL--GVTIAHEIGHSFGLEHDGAP---GSGCGPSGH 247
Cdd:cd04267   90 DNAVLLTAQDFIEGDIL----GLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGDelaFECDGGGNY 165

                        170       180
                 ....*....|....*....|....
gi 16306598  248 VMA--SDGAAPRaglAWSPCSRRQ 269
Cdd:cd04267  166 IMApvDSGLNSY---RFSQCSIGS 186
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 301-371 1.00e-17

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: 78.54  E-value: 1.00e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16306598    301 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 371
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 80-281 1.01e-14

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 74.70  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598   80 LHLELLVAVGPDvFQAHQEDTERY-----VLTN-LNIGAELLRDPslGAQFRvhLVKMVILTEPEGAPNITANLTSSLLS 153
Cdd:cd04272    1 VYPELFVVVDYD-HQSEFFSNEQLirylaVMVNaANLRYRDLKSP--RIRLL--LVGITISKDPDFEPYIHPINYGYIDA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  154 vcgwSQTINPEDD-----TDPGHADLVLYITRFDLELPDG---NRQVRGVTQLGGACSpTWSCLITEDT-GFDLGV-TIA 223
Cdd:cd04272   76 ----AETLENFNEyvkkkRDYFNPDVVFLVTGLDMSTYSGgslQTGTGGYAYVGGACT-ENRVAMGEDTpGSYYGVyTMT 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598  224 HEIGHSFGLEHDGAPGSG-CGPS----------GHVMASDGAAPRaGLAWSPCSRRQLLSLLSAGRARC 281
Cdd:cd04272  151 HELAHLLGAPHDGSPPPSwVKGHpgsldcpwddGYIMSYVVNGER-QYRFSQCSQRQIRNVFRRLGASC 218
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 387-439 1.75e-14

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: 69.15  E-value: 1.75e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 16306598     387 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 439
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 194-284 1.20e-13

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: 71.11  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  194 GVTQLGGACSPTWSCLITEDTG---FDLGVTIAHEIGHSFGLEHDGaPGSGCGPSGHVMASDGAAPRagLAWSPCSRRQL 270
Cdd:cd04269  104 GLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDD-GGCTCGRSTCIMAPSPSSLT--DAFSNCSYEDY 180

                         90
                 ....*....|....
gi 16306598  271 LSLLSAGRARCVWD 284
Cdd:cd04269  181 QKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 124-286 6.19e-12

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: 66.17  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    124 FRVHLVKMVILTEpEGAPNITANLTSSLLSVCGWSQT-INPEDDTDpgHADLVLYITrfdlelPDGNRQvrGVTQLGGAC 202
Cdd:pfam01421   44 IRVVLVGLEIWTD-EDKIDVSGDANDTLRNFLKWRQEyLKKRKPHD--VAQLLSGVE------FGGTTV--GAAYVGGMC 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    203 SPTWSCLITEDTGFD---LGVTIAHEIGHSFGLEHD-GAPGSGCGPSGH-VM-ASDGAAPraGLAWSPCSRRQLLSLLSA 276
Cdd:pfam01421  113 SLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHDdFNGGCKCPPGGGcIMnPSAGSSF--PRKFSNCSQEDFEQFLTK 190

                          170
                   ....*....|
gi 16306598    277 GRARCVWDPP 286
Cdd:pfam01421  191 QKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1076-1130 1.47e-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: 1.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16306598   1076 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1130
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
388-438 2.12e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 2.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 16306598    388 SSWGPRSPCSRSCGGGVVTRRRQCNNPRPafGGRACVGADLQAEMCNTQAC 438
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1012 4.97e-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: 50.53  E-value: 4.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    955 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 1012
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 120-268 4.40e-07

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 52.24  E-value: 4.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    120 LGAQFRVHLVKMVILTEPEGAPnitANLTSSLLSVCGWSQ-TINPEDDTDpgHADLVLYITRFDlelpdGNRQVRGVTQL 198
Cdd:pfam13583   44 FNVSLALISDRDVIYTDSSTDS---FNADCSGGDLGNWRLaTLTSWRDSL--NYDLAYLTLMTG-----PSGQNVGVAWV 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    199 GGACSPTW-----SCLITEDTGFDlgvTIAHEIGHSFGLEHDGApGSGCGPSGHVMASDG------AAPRAGLAWSPCSR 267
Cdd:pfam13583  114 GALCSSARqnakaSGVARSRDEWD---IFAHEIGHTFGAVHDCS-SQGEGLSSSTEDGSGqtimsyASTASQTAFSPCTI 189


                   .
gi 16306598    268 R 268
Cdd:pfam13583  190 R 190
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 746-804 4.64e-07

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: 47.83  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16306598    746 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 804
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1016-1072 5.59e-07

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: 47.83  E-value: 5.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16306598   1016 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 1072
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 166-243 8.39e-07

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: 50.60  E-value: 8.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  166 DTDPGHADLVLYITRFDLELPDGnrqvrGVTQLGGACSPTWSCLITEDTGFD---LGVTIAHEIGHSFGLEHDGAPGSGC 242
Cdd:cd00203   46 GVEIDKADIAILVTRQDFDGGTG-----GWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRD 120


                 .
gi 16306598  243 G 243
Cdd:cd00203  121 D 121
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 388-438 4.72e-06

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 44.96  E-value: 4.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 16306598    388 SSWGPRSPCSRSCGGGVVTRRRQCNNPrPAFGGRACvGADLQAEMCNTQAC 438
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 220-281 1.16e-05

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 48.52  E-value: 1.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598  220 VTIAHEIGHSFGLEHDgAPGSGCGPSG-----HVM---ASDGAAPRAGLaWSPCSRRQLLSLLSAGRARC 281
Cdd:cd04270  169 LVTAHELGHNFGSPHD-PDIAECAPGEsqggnYIMyarATSGDKENNKK-FSPCSKKSISKVLEVKSNSC 236
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 125-235 3.61e-05

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 44.67  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    125 RVHLVKMVILTEPEgapniTANLTSSLLSVCGWSQTINpedDTDPGH--ADLVLYITRFDlelpdgNRQVRGVTQLGGAC 202
Cdd:pfam13582   21 RLQLAAIIITTSAD-----TPYTSSDALEILDELQEVN---DTRIGQygYDLGHLFTGRD------GGGGGGIAYVGGVC 86

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 16306598    203 SPTWSCLITEDTG--FDLGV-TIAHEIGHSFGLEHD 235
Cdd:pfam13582   87 NSGSKFGVNSGSGpvGDTGAdTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 194-275 9.57e-05

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 44.93  E-value: 9.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    194 GVTQLGGACSPTWSCLITED---TGFDLGVT---------IAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAG-- 259
Cdd:pfam13574   88 GLAYVGQICQKGASSPKTNTglsTTTNYGSFnyptqewdvVAHEVGHNFGATHDCDGSQYASSGCERNAATSVCSANGsf 167

                           90       100
                   ....*....|....*....|....*.
gi 16306598    260 LAW----------SPCSRRQLLSLLS 275
Cdd:pfam13574  168 IMNpasksnndlfSPCSISLICDVLG 193
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
160-254 2.03e-04

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 43.95  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16306598    160 TINPEDDTDPGHA----DLVLYITRFDLELPDGNRQV--------------RGVTQLGGACSPTWSCLITEDTGFDLGV- 220
Cdd:pfam13688   53 TISDSTCPYTPPAcstgDSSDRLSEFQDFSAWRGTQNddlaylflmtncsgGGLAWLGQLCNSGSAGSVSTRVSGNNVVv 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 16306598    221 -------TIAHEIGHSFGLEHD--GAPGSGCGPSGHVMASDGA 254
Cdd:pfam13688  133 statewqVFAHEIGHNFGAVHDcdSSTSSQCCPPSNSTCPAGG 175
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 211-240 5.87e-04

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 41.81  E-value: 5.87e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 16306598  211 TEDTGFDLGVTIAHEIGHSFGLEHDGAPGS 240
Cdd:cd04278  100 SDSGGTDLFSVAAHEIGHALGLGHSSDPDS 129
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 902-951 9.04e-04

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.59  E-value: 9.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 16306598    902 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 951
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 216-243 5.01e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 40.02  E-value: 5.01e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 16306598  216 FDLGVTIAHEIGHSFGLEH---DGAPGSGCG 243
Cdd:cd04275  135 YNLGDTATHEVGHWLGLYHtfqGGSPCCTTG 165
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 205-240 5.46e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 39.14  E-value: 5.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 16306598    205 TWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGS 240
Cdd:pfam00413   95 TWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGA 130
 
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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