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Conserved domains on  [gi|568983397|ref|XP_006517330|]
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A disintegrin and metalloproteinase with thrombospondin motifs 16 isoform X2 [Mus musculus]

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) ...
 284-485 1.95e-101

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: 319.95  E-value: 1.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  284 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 363
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  364 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 440
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568983397  441 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 485
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 741-852 1.21e-37

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: 1.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   741 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 819
Cdd:pfam05986    1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   820 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 852
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 84-199 2.40e-32

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: 122.42  E-value: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397    84 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 163
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   164 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 199
Cdd:pfam01562  100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 502-569 5.14e-18

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: 79.31  E-value: 5.14e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397   502 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 569
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 583-635 3.43e-16

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: 73.78  E-value: 3.43e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568983397    583 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 635
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 925-980 1.34e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.63  E-value: 1.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568983397   925 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 980
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1124-1174 7.72e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.31  E-value: 7.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568983397  1124 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 1174
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1041 1.55e-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: 60.54  E-value: 1.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983397   984 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 1041
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1184-1214 1.15e-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: 57.16  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568983397  1184 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 1214
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 ...
 639-739 1.68e-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: 50.86  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   639 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 704
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568983397   705 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 739
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1049-1108 9.95e-07

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 46.68  E-value: 9.95e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  1049 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 1108
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) ...
 284-485 1.95e-101

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: 319.95  E-value: 1.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  284 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 363
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  364 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 440
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568983397  441 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 485
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 741-852 1.21e-37

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: 1.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   741 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 819
Cdd:pfam05986    1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   820 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 852
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 286-489 1.70e-34

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: 131.27  E-value: 1.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   286 VETLVVVDRKMMQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW- 362
Cdd:pfam01421    3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   363 QSGLMGKdgTRHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 439
Cdd:pfam01421   78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568983397   440 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 489
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 84-199 2.40e-32

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: 122.42  E-value: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397    84 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 163
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   164 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 199
Cdd:pfam01562  100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 502-569 5.14e-18

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: 79.31  E-value: 5.14e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397   502 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 569
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 583-635 3.43e-16

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: 73.78  E-value: 3.43e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568983397    583 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 635
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 925-980 1.34e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.63  E-value: 1.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568983397   925 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 980
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1124-1174 7.72e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.31  E-value: 7.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568983397  1124 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 1174
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1041 1.55e-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: 60.54  E-value: 1.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983397   984 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 1041
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1184-1214 1.15e-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: 57.16  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568983397  1184 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 1214
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
584-634 1.17e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.12  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568983397   584 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 634
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 ...
 639-739 1.68e-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: 50.86  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   639 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 704
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568983397   705 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 739
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1049-1108 9.95e-07

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 46.68  E-value: 9.95e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  1049 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 1108
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQK---GGGSIVPDSECSAQKKP--PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1122-1175 3.31e-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: 45.27  E-value: 3.31e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568983397   1122 GSWfaSPWSQCTASCGGGVQRRTVQCLLRGQPASDCFLHEKPETSSACNTHFCP 1175
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 923-981 1.96e-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: 42.96  E-value: 1.96e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397    923 SSWSvgNWSVCSRTCGGGTQSRPVRCTRRAhyrdESIPASLCPqPEPPIHQACNSQSCP 981
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.
 984-1013 4.69e-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: 4.69e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568983397    984 WSTGPWAECSRTCGKGWRKRTVACKSTNPS 1013
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ 31
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1052-1109 3.97e-03

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: 36.80  E-value: 3.97e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983397   1052 SAWSQCSVTCQGGTQQRVLRCaekyisgkYRELASKKCLHLPKPDLElERACGLIPCP 1109
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC--------CSPPPQNGGGPCTGEDVE-TRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 284-485 1.95e-101

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: 319.95  E-value: 1.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  284 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 363
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  364 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 440
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568983397  441 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 485
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 286-478 2.91e-40

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: 147.57  E-value: 2.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  286 VETLVVVDRKM-MQSHGHENITT-YVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 363
Cdd:cd04267     3 IELVVVADHRMvSYFNSDENILQaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  364 SglmgKDGTRHDHAILLTGLDICSwknepCDTLGFAPISGMCSKYRSCTVNEDSGLGL--AFTIAHESGHNFGMVHDGEG 441
Cdd:cd04267    83 A----EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGD 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568983397  442 ---NMCKKSEGNIMSPTLAGRNGVFsWSSCSRQYLHKFLS 478
Cdd:cd04267   154 elaFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 741-852 1.21e-37

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: 1.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   741 THRGLYSKHHStNQYYHMVTIPSGARSIHIYETNISTSYISVRNSLKRYYLNGHWSVD-WPGRYKFSGATFNYKRSYKEP 819
Cdd:pfam05986    1 TVSGSFTEGRA-KGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   820 ENLTSPGPTNETLIVELLFQ---GRNPGVAWEFSLP 852
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 285-485 3.73e-37

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: 138.52  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  285 NVETLVVVDRKMMQSHGH--ENITTYVLTILNMVSALFKdgTIggNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW 362
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PL--NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  363 QSGLMGKdGTRHDHAILLTGLDICSwknepcDTLGFAPISGMCSKYRSCTVNEDSG---LGLAFTIAHESGHNFGMVHDG 439
Cdd:cd04269    77 KRSNLLP-RKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568983397  440 EGnmCKKSEGN-IMSPTLAgrNGVFSWSSCSRQYLHKFLSTAQAICL 485
Cdd:cd04269   150 GG--CTCGRSTcIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 286-489 1.70e-34

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: 131.27  E-value: 1.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   286 VETLVVVDRKMMQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW- 362
Cdd:pfam01421    3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   363 QSGLMGKdgTRHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 439
Cdd:pfam01421   78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568983397   440 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 489
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 84-199 2.40e-32

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: 122.42  E-value: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397    84 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 163
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568983397   164 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 199
Cdd:pfam01562  100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 284-485 3.06e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 87.79  E-value: 3.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  284 LNVETLVVVDRKMMQSHGH-ENITTYVLTILNMVSALFKDgTIGGNINIVIVGLILLEDEQPGLAISHHAD------HTL 356
Cdd:cd04272     1 VYPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYgyidaaETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  357 TSFCQWQSGlmGKDGTRHDHAILLTGLDICSWKNEPCDT--LGFAPISGMCSKYRSCTVnEDSG--LGLAFTIAHESGHN 432
Cdd:cd04272    80 ENFNEYVKK--KRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568983397  433 FGMVHDGEG-----------NMCKKSEGNIMSPTLAGRNGvFSWSSCSRQYLHKFLSTAQAICL 485
Cdd:cd04272   157 LGAPHDGSPppswvkghpgsLDCPWDDGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGASCL 219
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 502-569 5.14e-18

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: 79.31  E-value: 5.14e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397   502 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 569
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 583-635 3.43e-16

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: 73.78  E-value: 3.43e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568983397    583 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 635
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 368-477 9.32e-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: 9.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  368 GKDGTRHDHAILLTGLDIcswknePCDTLGFAPISGMCSKYRSCTVNEDSGLG---LAFTIAHESGHNFGMVHDGEGNMC 444
Cdd:cd00203    46 GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568983397  445 KK-------------SEGNIMSPTLAGRNGVFS--WSSCSRQYLHKFL 477
Cdd:cd00203   120 DDyptiddtlnaeddDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 925-980 1.34e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.63  E-value: 1.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568983397   925 WSVGNWSVCSRTCGGGTQSRPVRCtRRAHYRDESiPASLC-PQPEPPIHQACNSQSC 980
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQC-VQKGGGSIV-PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1124-1174 7.72e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.31  E-value: 7.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568983397  1124 WFASPWSQCTASCGGGVQRRTVQCL----LRGQPASDCFLHEKPETSSACNTHFC 1174
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkggGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1041 1.55e-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: 60.54  E-value: 1.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983397   984 WSTGPWAECSRTCGKGWRKRTVACKSTNPsarAQLLHDTACTSEPKPRTHEICLLKRC 1041
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG---GSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1184-1214 1.15e-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: 57.16  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568983397  1184 CKDLFHWCYLVPQHGMCGHRFYSKQCCNTCS 1214
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
289-464 1.42e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 61.67  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   289 LVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTiggNINIVIVGLILLEDEQPGLAISHH---ADHTLTSFcQWQSG 365
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACStgdSSDRLSEF-QDFSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   366 LMGKDgtRHDHAILLTgldicswkNEPCDTLGFAPISGMCSKYRSCTVNEDSG--------LGLAFTIAHESGHNFGMVH 437
Cdd:pfam13688   84 WRGTQ--NDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGAVH 153

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568983397   438 DGEGNM-----------CKKSEGNIMSPTLAGRNGVFS 464
Cdd:pfam13688  154 DCDSSTssqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
TSP_1 pfam00090
Thrombospondin type 1 domain;
584-634 1.17e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.12  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568983397   584 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 634
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 ...
 584-634 3.98e-09

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: 53.44  E-value: 3.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568983397   584 SDWSPWSPCSRTCGGGISHRDRLCTNPrPSHGGKFCQGSTRTLKlCNSQRC 634
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLERRP-CNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 304-470 1.98e-08

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: 55.71  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   304 NITTYVLTILNMVSALFKDGTIggNINIVIVGLILLEDEQPGLAiSHHAD--------HTLTSFCQWQsglmgkdGTRHD 375
Cdd:pfam13574    2 NVTENLVNVVNRVNQIYEPDDI--NINGGLVNPGEIPATTSASD-SGNNYcnspttivRRLNFLSQWR-------GEQDY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   376 HAILLTGLDICSwknEPcdTLGFAPISGMCSKYRSCtVNEDSGLGLAFT-------------IAHESGHNFGMVHD--GE 440
Cdd:pfam13574   72 CLAHLVTMGTFS---GG--ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdGS 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 568983397   441 GNMCKKSEGN------------IMSPTlaGRNGVFSWSSCSR 470
Cdd:pfam13574  146 QYASSGCERNaatsvcsangsfIMNPA--SKSNNDLFSPCSI 185
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 639-739 1.68e-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: 50.86  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   639 VDFRAAQCAEYNSKRFR-----GWLYKWK---PYTQleDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRN 704
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGaavPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568983397   705 VCIDGMCERVGCDNVLGSDATEDSCGVCKGNNSDC 739
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1049-1108 9.95e-07

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 46.68  E-value: 9.95e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  1049 WLVSAWSQCSVTCQGGTQQRVLRCAEKyisGKYRELASKKCLHLPKPdlELERACGLIPC 1108
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQK---GGGSIVPDSECSAQKKP--PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1122-1175 3.31e-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: 45.27  E-value: 3.31e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568983397   1122 GSWfaSPWSQCTASCGGGVQRRTVQCLLRGQPASDCFLHEKPETSSACNTHFCP 1175
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 328-438 4.68e-06

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 46.98  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397   328 NINIVIVGLILLED-EQPGLAIShhADHTLTSFCQWQSGLMGKDGtrHDHAILLTGLDicswknePCDTLGFAPISGMCS 406
Cdd:pfam13582   19 GIRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDTRIGQYG--YDLGHLFTGRD-------GGGGGGIAYVGGVCN 87

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568983397   407 KYRSCTVNEDS---GLGLAFTIAHESGHNFGMVHD 438
Cdd:pfam13582   88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 923-981 1.96e-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: 42.96  E-value: 1.96e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397    923 SSWSvgNWSVCSRTCGGGTQSRPVRCTRRAhyrdESIPASLCPqPEPPIHQACNSQSCP 981
Cdd:smart00209    2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPP----PQNGGGPCT-GEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 588-634 3.06e-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: 42.83  E-value: 3.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568983397   588 PWSPCSRTCGGGISHRDRLCTNPRP--SHGGKFCQGSTR--TLKLCNSQRC 634
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKppETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 984-1013 4.69e-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: 4.69e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 568983397    984 WSTGPWAECSRTCGKGWRKRTVACKSTNPS 1013
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ 31
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 424-484 2.35e-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: 44.29  E-value: 2.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983397  424 TIAHESGHNFGMVHDGEGNMCKKSE---GN-IMSP-TLAG---RNGVFswSSCSRQYLHKFLSTAQAIC 484
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYArATSGdkeNNKKF--SPCSKKSISKVLEVKSNSC 236
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 916-980 4.01e-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: 39.18  E-value: 4.01e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983397   916 CKVSPcpssWSvgNWSVCSRTCGGGTQSRpvrcTRR--AHYRDESIPaslCPQPEppIHQACNSQSC 980
Cdd:pfam19028    1 CVVSE----WS--EWSECSVTCGGGVQTR----TRTviVEPQNGGRP---CPELL--ERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
986-1012 2.26e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.01  E-value: 2.26e-03
                           10        20
                   ....*....|....*....|....*..
gi 568983397   986 TGPWAECSRTCGKGWRKRTVACKSTNP 1012
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP 29
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 587-603 3.43e-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: 36.54  E-value: 3.43e-03
                           10
                   ....*....|....*..
gi 568983397   587 SPWSPCSRTCGGGISHR 603
Cdd:pfam19035    6 TEWSPCSKTCGMGVSTR 22
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 309-477 3.65e-03

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


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 40.48  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  309 VLTILNMVSALFKDGTiggNINIVIVGLILLEDEQPGLAISHHA-----------DHTLTSFCQWQSGLMGKDgtrhdhA 377
Cdd:cd04271    27 ILNNVNSASQLYESSF---NISLGLRNLTISDASCPSTAVDSAPwnlpcnsridiDDRLSIFSQWRGQQPDDG------N 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983397  378 ILLTGLDICswKNEPcdTLGFAPISGMCSKYRSCTVNE--DSGLGLAFT------IAHESGHNFGMVHD----------- 438
Cdd:cd04271    98 AFWTLMTAC--PSGS--EVGVAWLGQLCRTGASDQGNEtvAGTNVVVRTsnewqvFAHEIGHTFGAVHDctsgtcsdgsv 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568983397  439 GEGNMCKKSEGN-------IMSPTlaGRNGVFSWSSCSRQYLHKFL 477
Cdd:cd04271   174 GSQQCCPLSTSTcdangqyIMNPS--SSSGITEFSPCTIGNICSLL 217
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 424-454 3.78e-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: 3.78e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568983397   424 TIAHESGHNFGMVHD----GEGNMCKKSEGN---IMSP 454
Cdd:pfam13583  138 IFAHEIGHTFGAVHDcssqGEGLSSSTEDGSgqtIMSY 175
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1052-1109 3.97e-03

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: 36.80  E-value: 3.97e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983397   1052 SAWSQCSVTCQGGTQQRVLRCaekyisgkYRELASKKCLHLPKPDLElERACGLIPCP 1109
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC--------CSPPPQNGGGPCTGEDVE-TRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1052-1108 4.84e-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: 4.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568983397  1052 SAWSQCSVTCQGGTQQRvlrcaekyisgkYREL------ASKKClhlpkPDLELERACGLIPC 1108
Cdd:pfam19028    7 SEWSECSVTCGGGVQTR------------TRTVivepqnGGRPC-----PELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1127-1144 8.92e-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: 35.72  E-value: 8.92e-03
                           10
                   ....*....|....*...
gi 568983397  1127 SPWSQCTASCGGGVQRRT 1144
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRT 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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