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Conserved domains on  [gi|1028224123|ref|NP_001313287|]
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A disintegrin and metalloproteinase with thrombospondin motifs 18 isoform 3 [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) ...
 121-322 9.91e-113

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: 346.92  E-value: 9.91e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  121 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 200
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  201 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 277
Cdd:cd04273     81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1028224123  278 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 322
Cdd:cd04273    160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 578-689 1.14e-39

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: 142.72  E-value: 1.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  578 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 656
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1028224123  657 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 689
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 339-406 1.82e-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: 77.39  E-value: 1.82e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028224123  339 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 406
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 420-471 3.87e-15

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: 70.31  E-value: 3.87e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1028224123   420 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 471
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 476-576 1.05e-12

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: 65.50  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  476 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 543
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1028224123  544 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 576
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-819 1.52e-12

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: 63.24  E-value: 1.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028224123  763 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 819
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1001 7.55e-12

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: 61.31  E-value: 7.55e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  955 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1001
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 823-876 3.50e-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: 59.39  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123  823 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 876
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1016-1046 1.66e-10

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


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.66e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1028224123 1016 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1046
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 884-943 1.14e-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: 49.37  E-value: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  884 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 943
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 711-759 1.23e-03

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: 37.82  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1028224123  711 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 759
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) ...
 121-322 9.91e-113

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: 346.92  E-value: 9.91e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  121 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 200
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  201 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 277
Cdd:cd04273     81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1028224123  278 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 322
Cdd:cd04273    160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 578-689 1.14e-39

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: 142.72  E-value: 1.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  578 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 656
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1028224123  657 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 689
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 123-326 2.93e-33

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: 127.42  E-value: 2.93e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  123 VETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKdgtiGSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQW 199
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeIWTDEDK--IDVSGDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  200 QSALIGKNgKRHDHAILLTGfdicswKNEPCDTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHDG 276
Cdd:pfam01421   77 RQEYLKKR-KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1028224123  277 EGNPCR--KAEGNIMSPTlTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEP 326
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 339-406 1.82e-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: 77.39  E-value: 1.82e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028224123  339 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 406
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 420-471 3.87e-15

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: 70.31  E-value: 3.87e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1028224123   420 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 471
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 476-576 1.05e-12

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: 65.50  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  476 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 543
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1028224123  544 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 576
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-819 1.52e-12

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: 63.24  E-value: 1.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028224123  763 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 819
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1001 7.55e-12

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: 61.31  E-value: 7.55e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  955 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1001
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 823-876 3.50e-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: 59.39  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123  823 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 876
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1016-1046 1.66e-10

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


Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.66e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1028224123 1016 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1046
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
421-471 5.14e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  421 SAWSKWSECSRTCGGGVKFQERHCNNPKPqyGGLFCPGSSRIYQLCNINPC 471
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 884-943 1.14e-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: 49.37  E-value: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  884 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 943
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 823-877 8.13e-06

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: 44.11  E-value: 8.13e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123   823 WSLGPWSQCSKTCGRGVRKRELLCKgSAAETLPESQCTSlPRPELQEgCVLGRCP 877
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG-EDVETRA-CNEQPCP 53
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 819-877 7.62e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 7.62e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  819 CPPqWSlgPWSQCSKTCGRGV--RKRELLCKGsaaetlpesqCTSlprpELQEGCVLGRCP 877
Cdd:PTZ00441   240 CGP-WD--EWTPCSVTCGKGThsRSRPILHEG----------CTT----HMVEECEEEECP 283
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 887-944 2.25e-04

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: 39.88  E-value: 2.25e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028224123   887 SSWSECSATCGLGVRKREMKCsekgfqgklITFPERRCRNIKKPNLDLEETCNRRACP 944
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC---------CSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 766-820 3.58e-04

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: 39.49  E-value: 3.58e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123   766 GEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlhsLCPVSTPtQVQACNSHACP 820
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-----PCTGEDV-ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 959-1006 3.84e-04

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: 39.49  E-value: 3.84e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1028224123   959 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSCLLHQKPPVLRACNTNFCP 1006
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 711-759 1.23e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.82  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1028224123  711 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 759
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) ...
 121-322 9.91e-113

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: 346.92  E-value: 9.91e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  121 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 200
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  201 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 277
Cdd:cd04273     81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1028224123  278 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 322
Cdd:cd04273    160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 578-689 1.14e-39

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: 142.72  E-value: 1.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  578 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 656
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1028224123  657 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 689
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 123-315 1.97e-38

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: 141.79  E-value: 1.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  123 VETLVVADKKMVEK-HGKGNVTT-YILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 200
Cdd:cd04267      3 IELVVVADHRMVSYfNSDENILQaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  201 SaligKNGKRHDHAILLTGFDICSwknepCDTLGFAPISGMCSKYRSCTINEDTGLGL--AFTIAHESGHNFGMIHDGEG 278
Cdd:cd04267     83 A----EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGD 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1028224123  279 ---NPCRKAEGNIMSPTLTGNNGVFsWSSCSRQYLKKFLS 315
Cdd:cd04267    154 elaFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 122-322 3.57e-35

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: 132.74  E-value: 3.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  122 NVETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKDgtigSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQ 198
Cdd:cd04269      2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLeIWTDKDK--ISVSGDAGETLNRFLD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  199 WQSALIGKnGKRHDHAILLTGFDICSwknepcDTLGFAPISGMCSKYRSCTINEDTG---LGLAFTIAHESGHNFGMIHD 275
Cdd:cd04269     76 WKRSNLLP-RKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHD 148

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1028224123  276 GEGNPCRkAEGNIMSPTLTgnNGVFSWSSCSRQYLKKFLSTPQAGCL 322
Cdd:cd04269    149 DGGCTCG-RSTCIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 123-326 2.93e-33

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: 127.42  E-value: 2.93e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  123 VETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKdgtiGSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQW 199
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeIWTDEDK--IDVSGDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  200 QSALIGKNgKRHDHAILLTGfdicswKNEPCDTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHDG 276
Cdd:pfam01421   77 RQEYLKKR-KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1028224123  277 EGNPCR--KAEGNIMSPTlTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEP 326
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 339-406 1.82e-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: 77.39  E-value: 1.82e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028224123  339 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 406
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 121-322 3.73e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.85  E-value: 3.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  121 LNVETLVVADKKmVEKHGKGN--VTTYILTVMNMVSGLFKDgTIGSDINVVVVSLILLEQEPGGLLINHHAD------QS 192
Cdd:cd04272      1 VYPELFVVVDYD-HQSEFFSNeqLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYgyidaaET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  193 LNSFCQWqsaligKNGKRH----DHAILLTGFDICSWKNEPCDT--LGFAPISGMCSKYRsCTINEDTG--LGLAFTIAH 264
Cdd:cd04272     79 LENFNEY------VKKKRDyfnpDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENR-VAMGEDTPgsYYGVYTMTH 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  265 ESGHNFGMIHDGEGNP-----------CRKAEGNIMSptlTGNNGV--FSWSSCSRQYLKKFLSTPQAGCL 322
Cdd:cd04272    152 ELAHLLGAPHDGSPPPswvkghpgsldCPWDDGYIMS---YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 420-471 3.87e-15

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: 70.31  E-value: 3.87e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1028224123   420 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 471
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 189-314 6.72e-15

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: 73.71  E-value: 6.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  189 ADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDIcswknePCDTLGFAPISGMCSKYRSCTINEDTGLG---LAFTIAHE 265
Cdd:cd00203     30 AMQIWRDYLNIRFVLVGVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHE 103

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028224123  266 SGHNFGMIHDG-------------EGNPCRKAEGNIMSPTLTGNNGVFS--WSSCSRQYLKKFL 314
Cdd:cd00203    104 LGHALGFYHDHdrkdrddyptiddTLNAEDDDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 476-576 1.05e-12

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: 65.50  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  476 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 543
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1028224123  544 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 576
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-819 1.52e-12

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: 63.24  E-value: 1.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028224123  763 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 819
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1001 7.55e-12

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: 61.31  E-value: 7.55e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  955 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1001
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
126-301 1.26e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 64.75  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  126 LVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGtigSDINVVVVSLILLEQE-----PGGLLINhhADQSLNSFcQWQ 200
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERD---FNISLGLVNLTISDSTcpytpPACSTGD--SSDRLSEF-QDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  201 SALIGKngKRHDHAILLTGFDicswknepCDTLGFAPISGMCSKYRSCTINEDTG--------LGLAFTIAHESGHNFGM 272
Cdd:pfam13688   82 SAWRGT--QNDDLAYLFLMTN--------CSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGA 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1028224123  273 IHDGE----------GNPCRKAEGN-IMSPTLTGNNGVFS 301
Cdd:pfam13688  152 VHDCDsstssqccppSNSTCPAGGRyIMNPSSSPNSTDFS 191
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 823-876 3.50e-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: 59.39  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123  823 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 876
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 140-307 6.33e-11

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: 62.65  E-value: 6.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  140 GNVTTYILTVMNMVSGLFKDGTIGSDINVVvvslilleqEPGGLLINHHADQSLNSFCQ---WQ-------SALIGKNGK 209
Cdd:pfam13574    1 GNVTENLVNVVNRVNQIYEPDDININGGLV---------NPGEIPATTSASDSGNNYCNsptTIvrrlnflSQWRGEQDY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  210 RHDHAILLTGFdicswkNEPcdTLGFAPISGMCSKYRSCtINEDTGLGLAFT-------------IAHESGHNFGMIHD- 275
Cdd:pfam13574   72 CLAHLVTMGTF------SGG--ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDc 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1028224123  276 -GEGNPCRKAEGN------------IMSPTLTGNNGVFswSSCSR 307
Cdd:pfam13574  143 dGSQYASSGCERNaatsvcsangsfIMNPASKSNNDLF--SPCSI 185
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1016-1046 1.66e-10

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


Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.66e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1028224123 1016 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1046
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
421-471 5.14e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  421 SAWSKWSECSRTCGGGVKFQERHCNNPKPqyGGLFCPGSSRIYQLCNINPC 471
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 884-943 1.14e-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: 49.37  E-value: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  884 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 943
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 261-329 2.14e-06

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: 50.06  E-value: 2.14e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028224123  261 TIAHESGHNFGMIHDGEGNPCRKAE---GN-IMSPTLTG----NNGVFswSSCSRQYLKKFLSTPQAGCLVdEPKQA 329
Cdd:cd04270    170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYARATSgdkeNNKKF--SPCSKKSISKVLEVKSNSCFV-ERSQS 243
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 421-471 2.56e-06

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.35  E-value: 2.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  421 SAWSKWSECSRTCGGGVKFQERHCNNPkPQYGGLFCPGSSRIyQLCNINPC 471
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 144-275 7.64e-06

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: 46.21  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  144 TYILTVMNMVSGLFKdgtIGSDINVVVVSLILLE-QEPGGLLINhhADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDI 222
Cdd:pfam13582    1 ARIVSLVNRANTIYE---RDLGIRLQLAAIIITTsADTPYTSSD--ALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGG 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1028224123  223 cswknepcdTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHD 275
Cdd:pfam13582   76 ---------GGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 823-877 8.13e-06

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: 44.11  E-value: 8.13e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123   823 WSLGPWSQCSKTCGRGVRKRELLCKgSAAETLPESQCTSlPRPELQEgCVLGRCP 877
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG-EDVETRA-CNEQPCP 53
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 819-877 7.62e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 7.62e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  819 CPPqWSlgPWSQCSKTCGRGV--RKRELLCKGsaaetlpesqCTSlprpELQEGCVLGRCP 877
Cdd:PTZ00441   240 CGP-WD--EWTPCSVTCGKGThsRSRPILHEG----------CTT----HMVEECEEEECP 283
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 425-471 1.08e-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: 40.90  E-value: 1.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1028224123  425 KWSECSRTCGGGVKFQERHCNNPKPQ--YGGLFCPGSSR--IYQLCNINPC 471
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 887-944 2.25e-04

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: 39.88  E-value: 2.25e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028224123   887 SSWSECSATCGLGVRKREMKCsekgfqgklITFPERRCRNIKKPNLDLEETCNRRACP 944
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC---------CSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 766-820 3.58e-04

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: 39.49  E-value: 3.58e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1028224123   766 GEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlhsLCPVSTPtQVQACNSHACP 820
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-----PCTGEDV-ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 959-1006 3.84e-04

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: 39.49  E-value: 3.84e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1028224123   959 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSCLLHQKPPVLRACNTNFCP 1006
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 711-759 1.23e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.82  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1028224123  711 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 759
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 887-943 1.70e-03

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: 37.26  E-value: 1.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  887 SSWSECSATCGLGVRKREMkcsekgfqgKLITFPE---RRCrnikkPNLDLEETCNRRAC 943
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRTR---------TVIVEPQnggRPC-----PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
826-848 2.56e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.01  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|...
gi 1028224123  826 GPWSQCSKTCGRGVRKRELLCKG 848
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKS 26
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 823-842 3.45e-03

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: 36.49  E-value: 3.45e-03
                           10        20
                   ....*....|....*....|
gi 1028224123  823 WSlgPWSQCSKTCGRGVRKR 842
Cdd:pfam19028    6 WS--EWSECSVTCGGGVQTR 23
TSP_1 pfam00090
Thrombospondin type 1 domain;
959-988 4.03e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 4.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1028224123  959 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSC 988
Cdd:pfam00090    5 PWSPCSVTCGKGIQVRQRTCKSPFPGGEPC 34
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 146-275 9.48e-03

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 38.94  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028224123  146 ILTVMNMVSGLFKDGTigsDINVVVVSLILLEQE---------PGGLLINHHAD--QSLNSFCQWQSaligknGKRHDHA 214
Cdd:cd04271     27 ILNNVNSASQLYESSF---NISLGLRNLTISDAScpstavdsaPWNLPCNSRIDidDRLSIFSQWRG------QQPDDGN 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028224123  215 ILLTGFDICswKNEPcdTLGFAPISGMCSKYRSCTINEDTG--LGLAFT------IAHESGHNFGMIHD 275
Cdd:cd04271     98 AFWTLMTAC--PSGS--EVGVAWLGQLCRTGASDQGNETVAgtNVVVRTsnewqvFAHEIGHTFGAVHD 162
 
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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