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Conserved domains on  [gi|50845384|ref|NP_008919|]
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A disintegrin and metalloproteinase with thrombospondin motifs 1 preproprotein [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) ...
 258-463 1.31e-112

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: 344.99  E-value: 1.31e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 258 RYVETMLVADQSMAEF-HGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQ 336
Cdd:cd04273   1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 337 KQHNPPSDRDAEHYDTAILFTRQDLCGSQ-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 414
Cdd:cd04273  81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50845384 415 KQCASlngVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECL 463
Cdd:cd04273 161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 726-842 2.66e-36

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: 132.70  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   726 KISGSVTSAK-PGYHDIITIPTGATNIEVKQRNqrgsrNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGS 804
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   805 SAALERIRSFSPLKEPLTIQVLTV-GNALRPKIKYTYFV 842
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 478-546 7.38e-26

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: 101.27  E-value: 7.38e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   478 PGTSYDANRQCQFTFGEDSKHCPDA-ASTCSTLWCTGTSGGVlvCQTKHFPWADGTSCGEGKWCINGKCV 546
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGST--CTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 59-166 2.71e-22

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 93.15  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384    59 ELVVPEL-----------ERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQnVGRKSGSETPLPETDLAHCFYSG 127
Cdd:pfam01562   1 EVVIPVRldpsrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVT-YYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   128 TVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASE 166
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSR 118
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 562-614 3.79e-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: 3.79e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 50845384    562 WGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCP 614
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 858-909 2.97e-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: 2.97e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50845384   858 WVIEEWGECSKSCELGWQRRLVECRDING---QPASECAKEVKPASTRPCADHPC 909
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 912-954 8.92e-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: 8.92e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 50845384   912 WQLGEWSSCSKTCGKGYKKRSLKCL-SHDGGVLSHESCDPLKKP 954
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP 44
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 658-724 1.03e-09

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


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 57.03  E-value: 1.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845384   658 CKLICQAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 724
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) ...
 258-463 1.31e-112

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: 344.99  E-value: 1.31e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 258 RYVETMLVADQSMAEF-HGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQ 336
Cdd:cd04273   1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 337 KQHNPPSDRDAEHYDTAILFTRQDLCGSQ-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 414
Cdd:cd04273  81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50845384 415 KQCASlngVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECL 463
Cdd:cd04273 161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 726-842 2.66e-36

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: 132.70  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   726 KISGSVTSAK-PGYHDIITIPTGATNIEVKQRNqrgsrNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGS 804
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   805 SAALERIRSFSPLKEPLTIQVLTV-GNALRPKIKYTYFV 842
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 478-546 7.38e-26

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: 101.27  E-value: 7.38e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   478 PGTSYDANRQCQFTFGEDSKHCPDA-ASTCSTLWCTGTSGGVlvCQTKHFPWADGTSCGEGKWCINGKCV 546
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGST--CTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 59-166 2.71e-22

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 93.15  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384    59 ELVVPEL-----------ERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQnVGRKSGSETPLPETDLAHCFYSG 127
Cdd:pfam01562   1 EVVIPVRldpsrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVT-YYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   128 TVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASE 166
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSR 118
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 258-467 1.16e-21

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: 93.90  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   258 RYVETMLVADQSMAEFHGSGLKHYLLTLFSVAA---RLYKHPSIRnsVSLVVVKILVihDEQKgPEVTSNAALTLRNFCN 334
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR--VVLVGLEIWT--DEDK-IDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   335 WQKQHNPPSDRdaehYDTAILFTRQDLCGSqtcdTLGMADVGTVCDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 411
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50845384   412 DDAK---QCASLNGvnqdshmmASMLSNLDHSQP--WSPCSAYMITSFLDNGHGECLMDKP 467
Cdd:pfam01421 148 DDFNggcKCPPGGG--------CIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
468-548 1.07e-15

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 74.70  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384    468 QNPIQLPGD----LPGTSYDANRQCQFTFGEDSK----HCPDAAST------------------------CSTLWCTGTS 515
Cdd:smart00608   1 QDGTPCDNGqgycYNGRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedvkCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 50845384    516 G---------------GVLVCQTKHFP---------WADGTSCGEGKWCINGKCVNK 548
Cdd:smart00608  81 ElpllgehatviysniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 562-614 3.79e-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: 3.79e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 50845384    562 WGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCP 614
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 858-909 2.97e-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: 2.97e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50845384   858 WVIEEWGECSKSCELGWQRRLVECRDING---QPASECAKEVKPASTRPCADHPC 909
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 912-954 8.92e-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: 8.92e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 50845384   912 WQLGEWSSCSKTCGKGYKKRSLKCL-SHDGGVLSHESCDPLKKP 954
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP 44
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 658-724 1.03e-09

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 57.03  E-value: 1.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845384   658 CKLICQAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 724
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
565-613 7.01e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.72  E-value: 7.01e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 50845384   565 WGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNLEDC 613
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 858-910 4.03e-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: 44.89  E-value: 4.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50845384    858 WVIEEWGECSKSCELGWQRRLVECRDINGQ-PASECAKEVKpaSTRPCADHPCP 910
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 912-967 1.24e-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: 43.34  E-value: 1.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 50845384    912 WQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVlSHESCDPLKKPKHfidFCTMAECS 967
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN-GGGPCTGEDVETR---ACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 258-463 1.31e-112

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: 344.99  E-value: 1.31e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 258 RYVETMLVADQSMAEF-HGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQ 336
Cdd:cd04273   1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 337 KQHNPPSDRDAEHYDTAILFTRQDLCGSQ-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 414
Cdd:cd04273  81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50845384 415 KQCASlngVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECL 463
Cdd:cd04273 161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 258-456 2.75e-39

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: 144.49  E-value: 2.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 258 RYVETMLVADQSMAEF---HGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCN 334
Cdd:cd04267   1 REIELVVVADHRMVSYfnsDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 335 WQKqhnppsdRDAEHYDTAILFTRQDLCGsqtCDTLGMADVGTVCDPSRSCSVIEDDG--LQAAFTTAHELGHVFNMPHD 412
Cdd:cd04267  81 WRA-------EGPIRHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHD 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50845384 413 DAKQCASLNGVNqDSHMMASMLSNLDhSQPWSPCSAYMITSFLD 456
Cdd:cd04267 151 GGDELAFECDGG-GNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 726-842 2.66e-36

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: 132.70  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   726 KISGSVTSAK-PGYHDIITIPTGATNIEVKQRNqrgsrNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGS 804
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   805 SAALERIRSFSPLKEPLTIQVLTV-GNALRPKIKYTYFV 842
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 258-465 2.21e-27

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: 110.01  E-value: 2.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 258 RYVETMLVADQSMAEFHGSGL---KHYLLTLFSVAARLYKHPSIRnsvslVVVKILVIHDEQKGPEVTSNAALTLRNFCN 334
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNIR-----VVLVGLEIWTDKDKISVSGDAGETLNRFLD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 335 WQKqhnppSDRDAEH-YDTAILFTRQDLCGsqtcDTLGMADVGTVCDPSRSCSVIEDDG---LQAAFTTAHELGHVFNMP 410
Cdd:cd04269  76 WKR-----SNLLPRKpHDNAQLLTGRDFDG----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 50845384 411 HDDAK-QCASLNGVnqdshmMASmlSNLDHSQPWSPCSAYMITSFLDNGHGECLMD 465
Cdd:cd04269 147 HDDGGcTCGRSTCI------MAP--SPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 478-546 7.38e-26

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: 101.27  E-value: 7.38e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   478 PGTSYDANRQCQFTFGEDSKHCPDA-ASTCSTLWCTGTSGGVlvCQTKHFPWADGTSCGEGKWCINGKCV 546
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGST--CTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 59-166 2.71e-22

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 93.15  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384    59 ELVVPEL-----------ERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQnVGRKSGSETPLPETDLAHCFYSG 127
Cdd:pfam01562   1 EVVIPVRldpsrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVT-YYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50845384   128 TVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASE 166
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSR 118
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 258-467 1.16e-21

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: 93.90  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   258 RYVETMLVADQSMAEFHGSGLKHYLLTLFSVAA---RLYKHPSIRnsVSLVVVKILVihDEQKgPEVTSNAALTLRNFCN 334
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR--VVLVGLEIWT--DEDK-IDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   335 WQKQHNPPSDRdaehYDTAILFTRQDLCGSqtcdTLGMADVGTVCDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 411
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50845384   412 DDAK---QCASLNGvnqdshmmASMLSNLDHSQP--WSPCSAYMITSFLDNGHGECLMDKP 467
Cdd:pfam01421 148 DDFNggcKCPPGGG--------CIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
468-548 1.07e-15

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 74.70  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384    468 QNPIQLPGD----LPGTSYDANRQCQFTFGEDSK----HCPDAAST------------------------CSTLWCTGTS 515
Cdd:smart00608   1 QDGTPCDNGqgycYNGRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedvkCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 50845384    516 G---------------GVLVCQTKHFP---------WADGTSCGEGKWCINGKCVNK 548
Cdd:smart00608  81 ElpllgehatviysniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 562-614 3.79e-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: 3.79e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 50845384    562 WGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCP 614
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 351-455 1.59e-14

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: 72.17  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 351 DTAILFTRQDLcgsqTCDTLGMADVGTVCDPSRSCSVIEDDGL---QAAFTTAHELGHVFNMPHD------DAKQCASLN 421
Cdd:cd00203  53 DIAILVTRQDF----DGGTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDDT 128

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50845384 422 GVNQD----SHMMASMLSNLDH-SQPWSPCSAYMITSFL 455
Cdd:cd00203 129 LNAEDddyySVMSYTKGSFSDGqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 858-909 2.97e-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: 2.97e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50845384   858 WVIEEWGECSKSCELGWQRRLVECRDING---QPASECAKEVKPASTRPCADHPC 909
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
256-419 3.77e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 66.29  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   256 SHRYVETMLVADQS-MAEFHGSGLKHYLLTLFSVAARLYKHPSirnSVSLVVVKIlVIHDEQK----GPEVTSNAALTLR 330
Cdd:pfam13688   1 STRTVALLVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNL-TISDSTCpytpPACSTGDSSDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   331 NFcnwQKQHnppSDRDAEHYDTAILFTrqdlcgSQTCDTLGMADVGTVCDPSRSCSVIEDDG--------LQAAFTTAHE 402
Cdd:pfam13688  77 EF---QDFS---AWRGTQNDDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHE 144

                         170
                  ....*....|....*..
gi 50845384   403 LGHVFNMPHDDAKQCAS 419
Cdd:pfam13688 145 IGHNFGAVHDCDSSTSS 161
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 259-463 7.03e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.84  E-value: 7.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 259 YVETMLVADQSMA--EFHGSGLKHYLLTLFSVAARLYKhpSIRN-SVSLVVVKILVIHDEQKGPEV------TSNAALTL 329
Cdd:cd04272   2 YPELFVVVDYDHQseFFSNEQLIRYLAVMVNAANLRYR--DLKSpRIRLLLVGITISKDPDFEPYIhpinygYIDAAETL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 330 RNFCNWQKQhnppsDRDAEHYDTAILFTRQDLC----GSQTCDTLGMADVGTVCDpSRSCSVIEDDG--LQAAFTTAHEL 403
Cdd:cd04272  80 ENFNEYVKK-----KRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDTPgsYYGVYTMTHEL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50845384 404 GHVFNMPHDDAKQCASLNGVN-------QDSHMMaSMLSNLDHSQPWSPCSAYMITSFLDNGHGECL 463
Cdd:cd04272 154 AHLLGAPHDGSPPPSWVKGHPgsldcpwDDGYIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 912-954 8.92e-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: 8.92e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 50845384   912 WQLGEWSSCSKTCGKGYKKRSLKCL-SHDGGVLSHESCDPLKKP 954
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP 44
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 658-724 1.03e-09

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 57.03  E-value: 1.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50845384   658 CKLICQAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 724
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 301-412 1.49e-09

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: 56.61  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   301 SVSLVVVKIlVIHDEQKGPEVTSNAALTLRNFCNWQKQHnppsdRDAEHYDTAILFTRQDLCGsqtcdTLGMADVGTVCD 380
Cdd:pfam13582  19 GIRLQLAAI-IITTSADTPYTSSDALEILDELQEVNDTR-----IGQYGYDLGHLFTGRDGGG-----GGGIAYVGGVCN 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 50845384   381 PSRSCSVIEDD---GLQAAFTTAHELGHVFNMPHD 412
Cdd:pfam13582  88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP_1 pfam00090
Thrombospondin type 1 domain;
565-613 7.01e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.72  E-value: 7.01e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 50845384   565 WGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNLEDC 613
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 565-613 5.68e-07

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 47.27  E-value: 5.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 50845384   565 WGPWGDCSRTCGGGVQYTMRECDNPvPKNGGKYCEGKRVRyRSCNLEDC 613
Cdd:pfam19028   6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 858-910 4.03e-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: 44.89  E-value: 4.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50845384    858 WVIEEWGECSKSCELGWQRRLVECRDINGQ-PASECAKEVKpaSTRPCADHPCP 910
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDV--ETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 566-613 1.16e-05

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: 43.60  E-value: 1.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 50845384   566 GPWGDCSRTCGGGVQYTMRECDNPVPK--NGGKYCEGKR--VRYRSCNLEDC 613
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKkpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 912-967 1.24e-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: 43.34  E-value: 1.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 50845384    912 WQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVlSHESCDPLKKPKHfidFCTMAECS 967
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN-GGGPCTGEDVETR---ACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 856-909 2.71e-04

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: 39.57  E-value: 2.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 50845384   856 SAWviEEWGECSKSCELGWQRRLvecRDINGQPA---SECAKEVKpasTRPCADHPC 909
Cdd:pfam19028   4 SEW--SEWSECSVTCGGGVQTRT---RTVIVEPQnggRPCPELLE---RRPCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 282-455 3.71e-04

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: 42.62  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   282 LLTLFSVAARLYKHPSIrnSVSLVVVKILVIhdeqkgpEVTSNAALTLRNFCNWQKQHNPPSD-----RDAEHYDTAILF 356
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDI--NINGGLVNPGEI-------PATTSASDSGNNYCNSPTTIVRRLNflsqwRGEQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   357 TRQDLCGSqtcdTLGMADVGTVCDPSRSCsVIEDDGLQAAFTT-------------AHELGHVFNMPHDDAKQCASLNGV 423
Cdd:pfam13574  78 TMGTFSGG----ELGLAYVGQICQKGASS-PKTNTGLSTTTNYgsfnyptqewdvvAHEVGHNFGATHDCDGSQYASSGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 50845384   424 NQDSH-----------MMASMLSNLDHsqpWSPCSAYMITSFL 455
Cdd:pfam13574 153 ERNAAtsvcsangsfiMNPASKSNNDL---FSPCSISLICDVL 192
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 258-451 7.23e-04

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: 41.84  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   258 RYVETMLVADQSMAEFHGS--GLKHYLLTLFSVAARLYKhpsirnsvSLVVVKILVIHDEQ---KGPEVTSNAALTLRNF 332
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSvdELRANINATVTTANEVYG--------RDFNVSLALISDRDviyTDSSTDSFNADCSGGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384   333 CNWQKQHNPPSDRDAEHYDTAILFtRQDLCGSQTCdtlGMADVGTVCDPSR-----SCSVIEDDGLQaafTTAHELGHVF 407
Cdd:pfam13583  75 LGNWRLATLTSWRDSLNYDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTF 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 50845384   408 NMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQP-WSPCSAYMI 451
Cdd:pfam13583 148 GAVHDCSSQGEGLSSSTEDGSGQTIMSYASTASQTaFSPCTIRNI 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 305-471 1.39e-03

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: 41.59  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 305 VVVKILVIHDEQKgpEVTSNAALTLRNFCNWQKQH--NPPSDRDaEHYDT--AILFTRQDLCGSqtcdTLGMADVGTVCD 380
Cdd:cd04270  55 FQIKRIRIHTTPD--EVDPGNKFYNKSFPNWGVEKflVKLLLEQ-FSDDVclAHLFTYRDFDMG----TLGLAYVGSPRD 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50845384 381 PSRS--CSVIE----------DDGL-------------QAAFTTAHELGHVFNMPHD-DAKQCASLNGVNQDSHMMASML 434
Cdd:cd04270 128 NSAGgiCEKAYyysngkkkylNTGLtttvnygkrvptkESDLVTAHELGHNFGSPHDpDIAECAPGESQGGNYIMYARAT 207

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 50845384 435 SNlDH--SQPWSPCSAYMITSFLDNGHGECLMDkPQNPI 471
Cdd:cd04270 208 SG-DKenNKKFSPCSKKSISKVLEVKSNSCFVE-RSQSF 244
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 915-932 3.24e-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: 3.24e-03
                          10
                  ....*....|....*...
gi 50845384   915 GEWSSCSKTCGKGYKKRS 932
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRT 24
TSP_1 pfam00090
Thrombospondin type 1 domain;
915-935 9.85e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.09  E-value: 9.85e-03
                          10        20
                  ....*....|....*....|.
gi 50845384   915 GEWSSCSKTCGKGYKKRSLKC 935
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTC 24
 
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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