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Conserved domains on  [gi|1958795063|ref|XP_038936949|]
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A disintegrin and metalloproteinase with thrombospondin motifs 15 isoform X1 [Rattus norvegicus]

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 ...
 1-93 1.61e-42

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: 152.01  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV-KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAI 79
Cdd:cd04273   117 LAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRY 193

                          90
                  ....*....|....
gi 1958795063  80 ITDFLDSGHGDCLL 93
Cdd:cd04273   194 LTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 353-470 7.60e-40

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: 141.56  E-value: 7.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 353 RVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGT 431
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958795063 432 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 470
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 107-174 3.16e-21

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: 87.40  E-value: 3.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 107 PGTSYSLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 174
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 566-619 1.42e-13

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: 65.55  E-value: 1.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 566 WELGNWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCDLRRKPQELDFCVLRPC 619
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 188-240 2.72e-13

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: 64.53  E-value: 2.72e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958795063  188 WAKWEPYGPCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCP 240
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 512-563 2.39e-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: 62.09  E-value: 2.39e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 512 WVAGNWGPCSVSCGSGLQKRAVDCRDSPGQ--QGISACDVDHRPVEKRACGE-PC 563
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKPPETQSCNLkPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 285-351 1.94e-11

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: 61.26  E-value: 1.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795063 285 CKLICRANGTGYFYVLAPKVVDGTLCTPD------STSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSC 351
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-93 1.61e-42

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: 152.01  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV-KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAI 79
Cdd:cd04273   117 LAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRY 193

                          90
                  ....*....|....
gi 1958795063  80 ITDFLDSGHGDCLL 93
Cdd:cd04273   194 LTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 353-470 7.60e-40

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: 141.56  E-value: 7.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 353 RVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGT 431
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958795063 432 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 470
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 107-174 3.16e-21

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: 87.40  E-value: 3.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 107 PGTSYSLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 174
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 566-619 1.42e-13

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: 65.55  E-value: 1.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 566 WELGNWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCDLRRKPQELDFCVLRPC 619
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 188-240 2.72e-13

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: 64.53  E-value: 2.72e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958795063  188 WAKWEPYGPCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCP 240
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 512-563 2.39e-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: 62.09  E-value: 2.39e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 512 WVAGNWGPCSVSCGSGLQKRAVDCRDSPGQ--QGISACDVDHRPVEKRACGE-PC 563
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKPPETQSCNLkPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 285-351 1.94e-11

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: 61.26  E-value: 1.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795063 285 CKLICRANGTGYFYVLAPKVVDGTLCTPD------STSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSC 351
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-96 6.55e-11

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: 61.93  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDdGLPS----AFTTAHELGHVFNMPHDNVKV---CEEVFGKLranhmMSPTLIQIDrANPWS 73
Cdd:pfam01421 105 AAYVGGMCSLEYSGGVNED-HSKNlesfAVTMAHELGHNLGMQHDDFNGgckCPPGGGCI-----MNPSAGSSF-PRKFS 177

                          90       100
                  ....*....|....*....|...
gi 1958795063  74 ACSAAIITDFLDSGHGDCLLDQP 96
Cdd:pfam01421 178 NCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 515-564 6.63e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.43  E-value: 6.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958795063  515 GNWGPCSVSCGSGLQKRAVDCRDSPGQQGISACDVDHRpvEKRAC-GEPCP 564
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACnEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
191-239 6.04e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.56  E-value: 6.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958795063 191 WEPYGPCSRTCGGGVQLARRQCSNPTPanGGKYCEGVRVKYRSCNLEPC 239
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ACR smart00608
ADAM Cysteine-Rich Domain;
106-175 1.47e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 41.96  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063  106 LPGTSYSLSQQCELAFGVGSKPCPYMQY-----------------------------CTKLWCTGKAK------------ 144
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKVAPDSCYeelntkgdrfgncgrengtyipcapedvkCGKLQCTNVSElpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958795063  145 ---GQMVCQTRHFP---------WADGTSCGEGKFCLKGACVE 175
Cdd:smart00608  94 sniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 566-619 7.04e-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: 37.95  E-value: 7.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958795063  566 WELGNWSPCSKSCGRGFKRRPLKCVGHGGRLLARdQCDLRRKpqELDFCVLRPC 619
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-PCTGEDV--ETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-93 1.61e-42

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: 152.01  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV-KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAI 79
Cdd:cd04273   117 LAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRY 193

                          90
                  ....*....|....
gi 1958795063  80 ITDFLDSGHGDCLL 93
Cdd:cd04273   194 LTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 353-470 7.60e-40

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: 141.56  E-value: 7.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 353 RVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGT 431
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958795063 432 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 470
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 107-174 3.16e-21

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: 87.40  E-value: 3.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063 107 PGTSYSLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 174
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 1-85 4.75e-17

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: 79.77  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDDGLP--SAFTTAHELGHVFNMPHDNVKVCEEVFGKlRANHMMSPTLiqiDRANP--WSACS 76
Cdd:cd04267   108 LAYVGSMCNPYSSVGVVEDTGFTllTALTMAHELGHNLGAEHDGGDELAFECDG-GGNYIMAPVD---SGLNSyrFSQCS 183


                  ....*....
gi 1958795063  77 AAIITDFLD 85
Cdd:cd04267   184 IGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 1-94 8.59e-14

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: 70.34  E-value: 8.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDDG---LPSAFTTAHELGHVFNMPHDNVK-VCEevfgklRANHMMSPTLIQIDRAnpWSACS 76
Cdd:cd04269   105 LAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDGGcTCG------RSTCIMAPSPSSLTDA--FSNCS 176

                          90
                  ....*....|....*...
gi 1958795063  77 AAIITDFLDSGHGDCLLD 94
Cdd:cd04269   177 YEDYQKFLSRGGGQCLLN 194
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 566-619 1.42e-13

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: 65.55  E-value: 1.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 566 WELGNWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCDLRRKPQELDFCVLRPC 619
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 188-240 2.72e-13

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: 64.53  E-value: 2.72e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958795063  188 WAKWEPYGPCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCP 240
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 512-563 2.39e-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: 62.09  E-value: 2.39e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958795063 512 WVAGNWGPCSVSCGSGLQKRAVDCRDSPGQ--QGISACDVDHRPVEKRACGE-PC 563
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKPPETQSCNLkPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 285-351 1.94e-11

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: 61.26  E-value: 1.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795063 285 CKLICRANGTGYFYVLAPKVVDGTLCTPD------STSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSC 351
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-96 6.55e-11

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: 61.93  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   1 MADVGTMCDPKRSCSVIEDdGLPS----AFTTAHELGHVFNMPHDNVKV---CEEVFGKLranhmMSPTLIQIDrANPWS 73
Cdd:pfam01421 105 AAYVGGMCSLEYSGGVNED-HSKNlesfAVTMAHELGHNLGMQHDDFNGgckCPPGGGCI-----MNPSAGSSF-PRKFS 177

                          90       100
                  ....*....|....*....|...
gi 1958795063  74 ACSAAIITDFLDSGHGDCLLDQP 96
Cdd:pfam01421 178 NCSQEDFEQFLTKQKGACLFNKP 200
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 2-84 1.05e-10

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: 60.61  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   2 ADVGTMCDPKRSCSVIEDDGLPS---AFTTAHELGHVFNMPHDNVKVCEEVFGKL---------RANHMMSPTLIQIDRA 69
Cdd:cd00203    71 AYLGRVCDSLRGVGVLQDNQSGTkegAQTIAHELGHALGFYHDHDRKDRDDYPTIddtlnaeddDYYSVMSYTKGSFSDG 150

                          90
                  ....*....|....*..
gi 1958795063  70 N--PWSACSAAIITDFL 84
Cdd:cd00203   151 QrkDFSQCDIDQINKLY 167
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 515-564 6.63e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.43  E-value: 6.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958795063  515 GNWGPCSVSCGSGLQKRAVDCRDSPGQQGISACDVDHRpvEKRAC-GEPCP 564
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACnEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
191-239 6.04e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.56  E-value: 6.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958795063 191 WEPYGPCSRTCGGGVQLARRQCSNPTPanGGKYCEGVRVKYRSCNLEPC 239
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 2-92 1.12e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 46.96  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063   2 ADVGTMCDpKRSCSVIEDdgLPSAF----TTAHELGHVFNMPHDNVKVCEEVFGKLRAN-------HMMSpTLIQIDRAN 70
Cdd:cd04272   122 AYVGGACT-ENRVAMGED--TPGSYygvyTMTHELAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgYIMS-YVVNGERQY 197

                          90       100
                  ....*....|....*....|..
gi 1958795063  71 PWSACSAAIITDFLDSGHGDCL 92
Cdd:cd04272   198 RFSQCSQRQIRNVFRRLGASCL 219
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 191-239 8.93e-05

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: 40.34  E-value: 8.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958795063 191 WEPYGPCSRTCGGGVQLARRQCSNPtPANGGKYCeGVRVKYRSCNLEPC 239
Cdd:pfam19028   6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
106-175 1.47e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 41.96  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795063  106 LPGTSYSLSQQCELAFGVGSKPCPYMQY-----------------------------CTKLWCTGKAK------------ 144
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKVAPDSCYeelntkgdrfgncgrengtyipcapedvkCGKLQCTNVSElpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958795063  145 ---GQMVCQTRHFP---------WADGTSCGEGKFCLKGACVE 175
Cdd:smart00608  94 sniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 193-239 4.63e-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: 38.59  E-value: 4.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958795063 193 PYGPCSRTCGGGVQLARRQCSNPTP--ANGGKYCEGVR--VKYRSCNLEPC 239
Cdd:pfam19030   5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKkpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 566-619 7.04e-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: 37.95  E-value: 7.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958795063  566 WELGNWSPCSKSCGRGFKRRPLKCVGHGGRLLARdQCDLRRKpqELDFCVLRPC 619
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-PCTGEDV--ETRACNEQPC 52
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 563-619 9.74e-04

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: 37.31  E-value: 9.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795063 563 CPTWElGNWSPCSKSCGRGFKRRplkcvghggRLLARDQCDLRrkpQELDFCVLRPC 619
Cdd:pfam19035   1 CEEQS-TEWSPCSKTCGMGVSTR---------VSNDNAECKLV---TETRLCQLRPC 44
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 2-41 9.52e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 36.58  E-value: 9.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958795063   2 ADVGTMCDPKRSCSVIEDD---GLPSAFTTAHELGHVFNMPHD 41
Cdd:pfam13582  80 AYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
 
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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