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Conserved domains on  [gi|110825974|ref|NP_055059|]
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A disintegrin and metalloproteinase with thrombospondin motifs 2 isoform 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) ...
266-467 3.31e-99

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: 313.79  E-value: 3.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  266 YNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIeIGNPSQSLENVCRW 345
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  346 AYLQQKPDTGHDEYHDHAIFLTRQDF----GPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 421
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110825974  422 GNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSY--DCLL 467
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
724-837 5.21e-35

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: 129.24  E-value: 5.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   724 VVKGTFTRSPKKhGYIKMFEIPAGARHLLIQEVDATSHHLAVKNlETGKFILNEENDVDASSKTFIAMGVEWEYRD-EDG 802
Cdd:pfam05986    1 TVSGSFTEGRAK-GYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISLNPTYPSLLGTVLEYRRsLPA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 110825974   803 RETLQTMGPLHGTITVLVIPV--GDTRVSLTYKYMIH 837
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQygKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
91-212 7.10e-33

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: 123.96  E-value: 7.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974    91 PVRTPSFP----GGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLG--SCLYVGDVAGL 164
Cdd:pfam01562    5 PVRLDPSRrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQtdHCYYQGHVEGH 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 110825974   165 AEaSSVALSNCDGLAGLIRMEEEEFFIEPLEKGLaaqEAEQGRVHVVY 212
Cdd:pfam01562   85 PD-SSVALSTCSGLRGFIRTENEEYLIEPLEKYS---REEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
482-551 8.83e-21

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.02  E-value: 8.83e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   482 PGLHYSMNEQCRFDFGLGYMMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTMCAPGKHCFKGHCI 551
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
564-616 2.18e-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: 74.16  E-value: 2.18e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 110825974    564 WGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCP 616
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
621-722 5.30e-13

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: 66.66  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   621 DFREEQCRQWD---LYFEHGDAQ-HHW---LPHEHRDAkeRCHLYCesRETGEVVSMKR--MVHDGTRC-----SYKDAF 686
Cdd:pfam19236    4 EFMSQQCARTDgqpLRSSPGGASfYHWgaaVPHSQGDA--LCRHMC--RAIGESFIMKRgdSFLDGTRCmpsgpREDGTL 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 110825974   687 SLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHC 722
Cdd:pfam19236   80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
979-1028 6.32e-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: 61.70  E-value: 6.32e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 110825974   979 WRAGPWSQCSVTCGNGTQERPVLCR------TADDSFgiC-QEERPETARTCRLGPC 1028
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggsIVPDSE--CsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
918-975 3.89e-11

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 3.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825974   918 WVTGEWEPCSQTCGRtGMQVRSVRCIQPlHDNTTrsVHAKHCNDA-RPESRRACSRELC 975
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK-GGGSI--VPDSECSAQkKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
858-913 9.41e-09

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: 52.46  E-value: 9.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110825974   858 WALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKaIRRACNPQEC 913
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
266-467 3.31e-99

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: 313.79  E-value: 3.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  266 YNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIeIGNPSQSLENVCRW 345
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  346 AYLQQKPDTGHDEYHDHAIFLTRQDF----GPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 421
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110825974  422 GNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSY--DCLL 467
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
724-837 5.21e-35

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: 129.24  E-value: 5.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   724 VVKGTFTRSPKKhGYIKMFEIPAGARHLLIQEVDATSHHLAVKNlETGKFILNEENDVDASSKTFIAMGVEWEYRD-EDG 802
Cdd:pfam05986    1 TVSGSFTEGRAK-GYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISLNPTYPSLLGTVLEYRRsLPA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 110825974   803 RETLQTMGPLHGTITVLVIPV--GDTRVSLTYKYMIH 837
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQygKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
91-212 7.10e-33

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: 123.96  E-value: 7.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974    91 PVRTPSFP----GGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLG--SCLYVGDVAGL 164
Cdd:pfam01562    5 PVRLDPSRrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQtdHCYYQGHVEGH 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 110825974   165 AEaSSVALSNCDGLAGLIRMEEEEFFIEPLEKGLaaqEAEQGRVHVVY 212
Cdd:pfam01562   85 PD-SSVALSTCSGLRGFIRTENEEYLIEPLEKYS---REEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
268-470 2.22e-24

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: 101.99  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   268 IEVLLGVDDSVVQFHGK--EHVQKYLLTLMNIVNEIYHdeslGAHINVVLVRIILLSygkSMSLIEI-GNPSQSLENVCR 344
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWT---DEDKIDVsGDANDTLRNFLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   345 W--AYLQQKPDtghdeyHDHAIFLTRQDFGpSGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHD 419
Cdd:pfam01421   76 WrqEYLKKRKP------HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHD 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110825974   420 GQGNRCGDEVRLGSIMAPLVQAAFHRfHWSRCSQQELSRYLHSYD--CLLDDP 470
Cdd:pfam01421  149 DFNGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
482-551 8.83e-21

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.02  E-value: 8.83e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   482 PGLHYSMNEQCRFDFGLGYMMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTMCAPGKHCFKGHCI 551
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
564-616 2.18e-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: 74.16  E-value: 2.18e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 110825974    564 WGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCP 616
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
621-722 5.30e-13

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: 66.66  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   621 DFREEQCRQWD---LYFEHGDAQ-HHW---LPHEHRDAkeRCHLYCesRETGEVVSMKR--MVHDGTRC-----SYKDAF 686
Cdd:pfam19236    4 EFMSQQCARTDgqpLRSSPGGASfYHWgaaVPHSQGDA--LCRHMC--RAIGESFIMKRgdSFLDGTRCmpsgpREDGTL 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 110825974   687 SLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHC 722
Cdd:pfam19236   80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
979-1028 6.32e-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: 61.70  E-value: 6.32e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 110825974   979 WRAGPWSQCSVTCGNGTQERPVLCR------TADDSFgiC-QEERPETARTCRLGPC 1028
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggsIVPDSE--CsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
918-975 3.89e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 3.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825974   918 WVTGEWEPCSQTCGRtGMQVRSVRCIQPlHDNTTrsVHAKHCNDA-RPESRRACSRELC 975
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK-GGGSI--VPDSECSAQkKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
858-913 9.41e-09

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: 52.46  E-value: 9.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110825974   858 WALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKaIRRACNPQEC 913
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
982-1029 1.87e-08

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: 51.82  E-value: 1.87e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 110825974    982 GPWSQCSVTCGNGTQERPVLCRTADDSFG--ICQEERPETaRTCRLGPCP 1029
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVET-RACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
565-615 3.31e-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: 48.04  E-value: 3.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 110825974   565 GAWSPFGSCSRTCGTGVKFRTR---QcdnpHPANGGRTCSGLaYDFQLCSRQDC 615
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRtviV----EPQNGGRPCPEL-LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
917-976 1.41e-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: 46.43  E-value: 1.41e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974    917 VWVTGEWEPCSQTCGRtGMQVRSVRCIQPLHDNttrsvHAKHCNDARPESrRACSRELCP 976
Cdd:smart00209    1 WSEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQN-----GGGPCTGEDVET-RACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
863-914 9.28e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 9.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 110825974    863 WSPCSKPCGGGSQFtkygcRRRLDHKMVHRGFCAALSKPKAIRRACNPQECS 914
Cdd:smart00209    7 WSPCSVTCGGGVQT-----RTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
266-467 3.31e-99

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: 313.79  E-value: 3.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  266 YNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIeIGNPSQSLENVCRW 345
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  346 AYLQQKPDTGHDEYHDHAIFLTRQDF----GPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 421
Cdd:cd04273    80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110825974  422 GNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSY--DCLL 467
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
724-837 5.21e-35

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: 129.24  E-value: 5.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   724 VVKGTFTRSPKKhGYIKMFEIPAGARHLLIQEVDATSHHLAVKNlETGKFILNEENDVDASSKTFIAMGVEWEYRD-EDG 802
Cdd:pfam05986    1 TVSGSFTEGRAK-GYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISLNPTYPSLLGTVLEYRRsLPA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 110825974   803 RETLQTMGPLHGTITVLVIPV--GDTRVSLTYKYMIH 837
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQVLRQygKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
91-212 7.10e-33

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: 123.96  E-value: 7.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974    91 PVRTPSFP----GGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLG--SCLYVGDVAGL 164
Cdd:pfam01562    5 PVRLDPSRrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQtdHCYYQGHVEGH 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 110825974   165 AEaSSVALSNCDGLAGLIRMEEEEFFIEPLEKGLaaqEAEQGRVHVVY 212
Cdd:pfam01562   85 PD-SSVALSTCSGLRGFIRTENEEYLIEPLEKYS---REEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
267-468 2.94e-29

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: 115.79  E-value: 2.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  267 NIEVLLGVDDSVVQFHGK--EHVQKYLLTLMNIVNEIYHDeslgAHINVVLVRIILLSYGksmSLIEI-GNPSQSLENVC 343
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDK---DKISVsGDAGETLNRFL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  344 RW---AYLQQKPdtghdeyHDHAIFLTRQDFgPSGMQGYAPVTGMCHPVRSCTLNHEDG---FSSAFVVAHETGHVLGME 417
Cdd:cd04269    75 DWkrsNLLPRKP-------HDNAQLLTGRDF-DGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110825974  418 HDGQGNRCGdevRLGSIMAPlvQAAFHRFHWSRCSQQELSRYLHSYD--CLLD 468
Cdd:cd04269   147 HDDGGCTCG---RSTCIMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
268-460 1.83e-26

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: 107.89  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  268 IEVLLGVDDSVV-QFHGKE-HVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSyGKSMSLIEIGNPSQSLENVCRW 345
Cdd:cd04267     3 IELVVVADHRMVsYFNSDEnILQAYITELINIANSIYRSTNLRLGIRISLEGLQILK-GEQFAPPIDSDASNTLNSFSFW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  346 aylqQKPDTGHdeyHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTL--NHEDGFSSAFVVAHETGHVLGMEHDGqGN 423
Cdd:cd04267    82 ----RAEGPIR---HDNAVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDG-GD 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 110825974  424 RCGDEVRLGS--IMAPLVQAAFHRfHWSRCSQQELSRYL 460
Cdd:cd04267   154 ELAFECDGGGnyIMAPVDSGLNSY-RFSQCSIGSIREFL 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
268-470 2.22e-24

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: 101.99  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   268 IEVLLGVDDSVVQFHGK--EHVQKYLLTLMNIVNEIYHdeslGAHINVVLVRIILLSygkSMSLIEI-GNPSQSLENVCR 344
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWT---DEDKIDVsGDANDTLRNFLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   345 W--AYLQQKPDtghdeyHDHAIFLTRQDFGpSGMQGYAPVTGMCHPVRSCTLN---HEDGFSSAFVVAHETGHVLGMEHD 419
Cdd:pfam01421   76 WrqEYLKKRKP------HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHD 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110825974   420 GQGNRCGDEVRLGSIMAPLVQAAFHRfHWSRCSQQELSRYLHSYD--CLLDDP 470
Cdd:pfam01421  149 DFNGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
482-551 8.83e-21

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.02  E-value: 8.83e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   482 PGLHYSMNEQCRFDFGLGYMMCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTMCAPGKHCFKGHCI 551
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
564-616 2.18e-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: 74.16  E-value: 2.18e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 110825974    564 WGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCP 616
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
621-722 5.30e-13

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: 66.66  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   621 DFREEQCRQWD---LYFEHGDAQ-HHW---LPHEHRDAkeRCHLYCesRETGEVVSMKR--MVHDGTRC-----SYKDAF 686
Cdd:pfam19236    4 EFMSQQCARTDgqpLRSSPGGASfYHWgaaVPHSQGDA--LCRHMC--RAIGESFIMKRgdSFLDGTRCmpsgpREDGTL 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 110825974   687 SLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHC 722
Cdd:pfam19236   80 SLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
979-1028 6.32e-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: 61.70  E-value: 6.32e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 110825974   979 WRAGPWSQCSVTCGNGTQERPVLCR------TADDSFgiC-QEERPETARTCRLGPC 1028
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggsIVPDSE--CsAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
268-460 1.47e-11

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: 64.08  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  268 IEVLLGVDDSVVQFhgkEHVQKYLLTLMNIVNEIYHDESLgahINVVLVRIILLSygksmslieignpsqslenvcrway 347
Cdd:cd00203     3 IPYVVVADDRDVEE---ENLSAQIQSLILIAMQIWRDYLN---IRFVLVGVEIDK------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  348 lqqkpdtghdeyHDHAIFLTRQDFgPSGMQGYAPVTGMCHPVRSCTL---NHEDGFSSAFVVAHETGHVLGMEHDGQGNR 424
Cdd:cd00203    52 ------------ADIAILVTRQDF-DGGTGGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDRKD 118
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110825974  425 CGDEV-----------RLGSIMAPLVQAAFH--RFHWSRCSQQELSRYL 460
Cdd:cd00203   119 RDDYPtiddtlnaeddDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
918-975 3.89e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 59.39  E-value: 3.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825974   918 WVTGEWEPCSQTCGRtGMQVRSVRCIQPlHDNTTrsVHAKHCNDA-RPESRRACSRELC 975
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK-GGGSI--VPDSECSAQkKPPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
270-437 6.91e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 6.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   270 VLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESlgaHINVVLVRIILLSYGKSMSLIEIGNPSQSlenvcrwAYLQ 349
Cdd:pfam13688    7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDSS-------DRLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   350 QKPDTG---HDEYHDHAIFLTRQDFGPSGMqGYAPVTGMCHPVRSCTLNHEDGF------SSAFVVAHETGHVLGMEHDG 420
Cdd:pfam13688   77 EFQDFSawrGTQNDDLAYLFLMTNCSGGGL-AWLGQLCNSGSAGSVSTRVSGNNvvvstaTEWQVFAHEIGHNFGAVHDC 155
                          170       180
                   ....*....|....*....|....*.
gi 110825974   421 QGNRCGDEVRLGS---------IMAP 437
Cdd:pfam13688  156 DSSTSSQCCPPSNstcpaggryIMNP 181
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
267-466 7.95e-11

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 63.14  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  267 NIEVLLGVDDSVVQFHGK-EHVQKYLLTLMNIVNEIYHDESlGAHINVVLVRIILLSYGKSMSLIEIGNP-----SQSLE 340
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYgyidaAETLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974  341 NVCrwAYLQQKPDTGhdeYHDHAIFLTRQDFGP-------SGMQGYAPVTGMC--HPVRSCtlnhED---GFSSAFVVAH 408
Cdd:cd04272    81 NFN--EYVKKKRDYF---NPDVVFLVTGLDMSTysggslqTGTGGYAYVGGACteNRVAMG----EDtpgSYYGVYTMTH 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110825974  409 ETGHVLGMEHDGQG-----------NRCGDEvrLGSIMAPLVQAAFHrFHWSRCSQQELSRYLHSYD--CL 466
Cdd:cd04272   152 ELAHLLGAPHDGSPppswvkghpgsLDCPWD--DGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGasCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
858-913 9.41e-09

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: 52.46  E-value: 9.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110825974   858 WALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKaIRRACNPQEC 913
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
982-1029 1.87e-08

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: 51.82  E-value: 1.87e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 110825974    982 GPWSQCSVTCGNGTQERPVLCRTADDSFG--ICQEERPETaRTCRLGPCP 1029
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVET-RACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
565-615 3.31e-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: 48.04  E-value: 3.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 110825974   565 GAWSPFGSCSRTCGTGVKFRTR---QcdnpHPANGGRTCSGLaYDFQLCSRQDC 615
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRtviV----EPQNGGRPCPEL-LERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
564-615 1.35e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 110825974   564 WGAWSPfgsCSRTCGTGVKFRTRQCDnpHPANGGRTCSGLAYDFQLCSRQDC 615
Cdd:pfam00090    3 WSPWSP---CSVTCGKGIQVRQRTCK--SPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
917-976 1.41e-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: 46.43  E-value: 1.41e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974    917 VWVTGEWEPCSQTCGRtGMQVRSVRCIQPLHDNttrsvHAKHCNDARPESrRACSRELCP 976
Cdd:smart00209    1 WSEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQN-----GGGPCTGEDVET-RACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
982-1028 5.25e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 5.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 110825974   982 GPWSQCSVTCGNGTQERPVLCRTADDSFGICQEERPETaRTCRLGPC 1028
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIET-QACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
569-615 1.14e-04

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 40.90  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 110825974   569 PFGSCSRTCGTGVKFRTRQCDNPHP--ANGGRTCSGLA--YDFQLCSRQDC 615
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKkpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
863-914 9.28e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 9.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 110825974    863 WSPCSKPCGGGSQFtkygcRRRLDHKMVHRGFCAALSKPKAIRRACNPQECS 914
Cdd:smart00209    7 WSPCSVTCGGGVQT-----RTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
270-437 1.58e-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: 41.07  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   270 VLLGVDDSVVQFHG-KEHVQKYLLTLMNIVNEIYhDESLGAHINVVLVRIILLSYGKSMSLieigNPSQSLENVCRWAyl 348
Cdd:pfam13583    7 VAVATDCTYSASFGsVDELRANINATVTTANEVY-GRDFNVSLALISDRDVIYTDSSTDSF----NADCSGGDLGNWR-- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825974   349 QQKPDTGHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSctlNHE-DGFSSAF----VVAHETGHVLGMEHDGQGN 423
Cdd:pfam13583   80 LATLTSWRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKaSGVARSRdewdIFAHEIGHTFGAVHDCSSQ 156
                          170
                   ....*....|....*....
gi 110825974   424 RCG-----DEVRLGSIMAP 437
Cdd:pfam13583  157 GEGlssstEDGSGQTIMSY 175
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
982-998 2.49e-03

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 37.26  E-value: 2.49e-03
                           10
                   ....*....|....*..
gi 110825974   982 GPWSQCSVTCGNGTQER 998
Cdd:pfam19028    7 SEWSECSVTCGGGVQTR 23
TSP_1 pfam00090
Thrombospondin type 1 domain;
863-913 3.67e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 3.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 110825974   863 WSPCSKPCGGGSQFTkygcRRRLDHKMVHRGFCAAlskPKAIRRACNPQEC 913
Cdd:pfam00090    6 WSPCSVTCGKGIQVR----QRTCKSPFPGGEPCTG---DDIETQACKMDKC 49
 
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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