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Conserved domains on  [gi|1039743768|ref|XP_017171012|]
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A disintegrin and metalloproteinase with thrombospondin motifs 16 isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 2-119 1.02e-58

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.


The actual alignment was detected with superfamily member cd04273:

Pssm-ID: 469599  Cd Length: 207  Bit Score: 199.00  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   2 GKDGTRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGEGNMCKKS 81
Cdd:cd04273    88 DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPE 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039743768  82 --EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 119
Cdd:cd04273   167 gkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 375-486 8.11e-38

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: 136.94  E-value: 8.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 375 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 453
Cdd:pfam05986   1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039743768 454 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 486
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 ...
 136-203 8.09e-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: 75.46  E-value: 8.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768 136 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 203
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 217-269 8.42e-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: 69.15  E-value: 8.42e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039743768  217 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 269
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 559-614 2.20e-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: 2.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743768 559 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 614
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-808 7.69e-11

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.85  E-value: 7.69e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039743768 758 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 808
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 618-675 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: 57.08  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039743768 618 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 675
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 818-848 8.94e-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: 54.46  E-value: 8.94e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743768 818 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 848
Cdd:pfam08686   1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 273-373 8.57e-07

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: 48.55  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 273 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 338
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039743768 339 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 373
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 683-742 6.69e-06

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: 43.98  E-value: 6.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 683 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 742
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQK---GGGSIVPDSECSAQKKP--PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 2-119 1.02e-58

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: 199.00  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   2 GKDGTRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGEGNMCKKS 81
Cdd:cd04273    88 DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPE 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039743768  82 --EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 119
Cdd:cd04273   167 gkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 375-486 8.11e-38

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: 136.94  E-value: 8.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 375 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 453
Cdd:pfam05986   1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039743768 454 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 486
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 7-123 2.93e-22

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


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 95.45  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   7 RHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDGEGNMCK--KS 81
Cdd:pfam01421  86 PHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDDFNGGCKcpPG 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039743768  82 EGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 123
Cdd:pfam01421 160 GGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 136-203 8.09e-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: 75.46  E-value: 8.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768 136 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 203
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 217-269 8.42e-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: 69.15  E-value: 8.42e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039743768  217 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 269
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 559-614 2.20e-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: 2.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743768 559 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 614
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-808 7.69e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.85  E-value: 7.69e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039743768 758 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 808
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 618-675 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: 57.08  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039743768 618 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 675
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 818-848 8.94e-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: 54.46  E-value: 8.94e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743768 818 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 848
Cdd:pfam08686   1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
218-268 9.41e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 9.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039743768 218 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 268
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 273-373 8.57e-07

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: 48.55  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 273 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 338
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039743768 339 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 373
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 683-742 6.69e-06

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: 43.98  E-value: 6.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 683 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 742
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQK---GGGSIVPDSECSAQKKP--PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 756-809 2.56e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 2.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039743768  756 GSWfaSPWSQCTASCGGGVQRRTVQCLLRGQPASDCFLHEKPETSSACNTHFCP 809
Cdd:smart00209   2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 557-615 2.31e-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: 2.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768  557 SSWSvgNWSVCSRTCGGGTQSRPVRCTRRAhyrdESIPASLCPqPEPPIHQACNSQSCP 615
Cdd:smart00209   2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPP----PQNGGGPCT-GEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 618-647 2.34e-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: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039743768  618 WSTGPWAECSRTCGKGWRKRTVACKSTNPS 647
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ 31
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 2-119 1.02e-58

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: 199.00  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   2 GKDGTRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGEGNMCKKS 81
Cdd:cd04273    88 DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPE 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039743768  82 --EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 119
Cdd:cd04273   167 gkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 375-486 8.11e-38

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: 136.94  E-value: 8.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 375 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 453
Cdd:pfam05986   1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039743768 454 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 486
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 2-112 2.26e-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: 101.34  E-value: 2.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   2 GKDGTRHDHAILLTGLDICSwknepCDTLGFAPISGMCSKYRSCTVNEDSGLGL--AFTIAHESGHNFGMVHDGEG---N 76
Cdd:cd04267    83 AEGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGDelaF 157

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039743768  77 MCKKSEGNIMSPTLAGRNGVFsWSSCSRQYLHKFLS 112
Cdd:cd04267   158 ECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 7-119 6.26e-23

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: 97.30  E-value: 6.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   7 RHDHAILLTGLDICSwknepcDTLGFAPISGMCSKYRSCTVNEDSG---LGLAFTIAHESGHNFGMVHDGEGnmCKKSEG 83
Cdd:cd04269    86 PHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDGG--CTCGRS 157

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039743768  84 N-IMSPTLAgrNGVFSWSSCSRQYLHKFLSTAQAICL 119
Cdd:cd04269   158 TcIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 7-123 2.93e-22

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


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 95.45  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   7 RHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDGEGNMCK--KS 81
Cdd:pfam01421  86 PHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDDFNGGCKcpPG 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039743768  82 EGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 123
Cdd:pfam01421 160 GGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 136-203 8.09e-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: 75.46  E-value: 8.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768 136 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 203
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 217-269 8.42e-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: 69.15  E-value: 8.42e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039743768  217 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 269
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 2-111 6.26e-13

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: 67.55  E-value: 6.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   2 GKDGTRHDHAILLTGLDIcswknePCDTLGFAPISGMCSKYRSCTVNEDSGLG---LAFTIAHESGHNFGMVHDGEGNMC 78
Cdd:cd00203    46 GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039743768  79 KK-------------SEGNIMSPTLAGRNGVFS--WSSCSRQYLHKFL 111
Cdd:cd00203   120 DDyptiddtlnaeddDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 7-119 4.78e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.22  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   7 RHDHAILLTGLDICSWKNEPCDT--LGFAPISGMCSKYRSCTVnEDSG--LGLAFTIAHESGHNFGMVHDGEG------- 75
Cdd:cd04272    94 NPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHLLGAPHDGSPppswvkg 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039743768  76 ----NMCKKSEGNIMSPTLAGRNGvFSWSSCSRQYLHKFLSTAQAICL 119
Cdd:cd04272   173 hpgsLDCPWDDGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 559-614 2.20e-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: 2.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743768 559 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 614
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 758-808 7.69e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.85  E-value: 7.69e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039743768 758 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 808
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 618-675 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: 57.08  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039743768 618 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 675
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 818-848 8.94e-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: 54.46  E-value: 8.94e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743768 818 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 848
Cdd:pfam08686   1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
218-268 9.41e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 9.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039743768 218 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 268
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 218-268 2.54e-08

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: 50.74  E-value: 2.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039743768 218 SDWSPWSPCSRTCGGGISHRDRLCTNPrPSHGGKFCQGSTRTLKlCNSQRC 268
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLERRP-CNLPPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 273-373 8.57e-07

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: 48.55  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 273 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 338
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039743768 339 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 373
Cdd:pfam19236  81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 29-104 5.14e-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: 372637  Cd Length: 193  Bit Score: 48.01  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768  29 TLGFAPISGMCSKYRSCtVNEDSGLGLAFT-------------IAHESGHNFGMVHD--GEGNMCKKSEGN--------- 84
Cdd:pfam13574  86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdGSQYASSGCERNaatsvcsan 164

                          90       100
                  ....*....|....*....|...
gi 1039743768  85 ---IMSPTlaGRNGVFSWSSCSR 104
Cdd:pfam13574 165 gsfIMNPA--SKSNNDLFSPCSI 185
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 683-742 6.69e-06

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: 43.98  E-value: 6.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768 683 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 742
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQK---GGGSIVPDSECSAQKKP--PETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 23-72 2.07e-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: 2.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039743768  23 KNEPCDTLGFAPISGMCSKYRSCTVNEDS---GLGLAFTIAHESGHNFGMVHD 72
Cdd:pfam13582  70 GRDGGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 756-809 2.56e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 2.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039743768  756 GSWfaSPWSQCTASCGGGVQRRTVQCLLRGQPASDCFLHEKPETSSACNTHFCP 809
Cdd:smart00209   2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
7-98 4.40e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.10  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743768   7 RHDHAILLTgldicswkNEPCDTLGFAPISGMCSKYRSCTVNEDSG--------LGLAFTIAHESGHNFGMVHDGEGNM- 77
Cdd:pfam13688  89 NDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGAVHDCDSSTs 160

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039743768  78 ----------CKKSEGNIMSPTLAGRNGVFS 98
Cdd:pfam13688 161 sqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 222-268 1.63e-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: 40.13  E-value: 1.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039743768 222 PWSPCSRTCGGGISHRDRLCTNPRP--SHGGKFCQGSTR--TLKLCNSQRC 268
Cdd:pfam19030   5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKppETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 58-118 2.03e-04

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: 43.90  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768  58 TIAHESGHNFGMVHDGEGNMCKKSE---GN-IMSP-TLAG---RNGVFswSSCSRQYLHKFLSTAQAIC 118
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYArATSGdkeNNKKF--SPCSKKSISKVLEVKSNSC 236
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 557-615 2.31e-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: 2.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743768  557 SSWSvgNWSVCSRTCGGGTQSRPVRCTRRAhyrdESIPASLCPqPEPPIHQACNSQSCP 615
Cdd:smart00209   2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPP----PQNGGGPCT-GEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 618-647 2.34e-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: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039743768  618 WSTGPWAECSRTCGKGWRKRTVACKSTNPS 647
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ 31
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 58-88 2.53e-03

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: 39.91  E-value: 2.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1039743768  58 TIAHESGHNFGMVHD----GEGNMCKKSEGN---IMSP 88
Cdd:pfam13583 138 IFAHEIGHTFGAVHDcssqGEGLSSSTEDGSgqtIMSY 175
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 550-614 3.54e-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: 36.10  E-value: 3.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743768 550 CKVSPcpssWSvgNWSVCSRTCGGGTQSRpvrcTRR--AHYRDESIPaslCPQPEppIHQACNSQSC 614
Cdd:pfam19028   1 CVVSE----WS--EWSECSVTCGGGVQTR----TRTviVEPQNGGRP---CPELL--ERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
620-646 6.91e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 6.91e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039743768 620 TGPWAECSRTCGKGWRKRTVACKSTNP 646
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP 29
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 221-237 9.45e-03

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 35.00  E-value: 9.45e-03
                          10
                  ....*....|....*..
gi 1039743768 221 SPWSPCSRTCGGGISHR 237
Cdd:pfam19035   6 TEWSPCSKTCGMGVSTR 22
 
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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