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Conserved domains on  [gi|2023175293|ref|NP_001101903|]
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A disintegrin and metalloproteinase with thrombospondin motifs 19 precursor [Rattus norvegicus]

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) ...
 329-546 1.98e-81

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: 264.87  E-value: 1.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  329 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPADLYIGHHGEKMLESFCKWQ 408
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  409 HeefgrkndihlEMSTSWGEDVASVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 488
Cdd:cd04273     81 K-----------KLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023175293  489 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 546
Cdd:cd04273    149 GHVLGMPHDGDGNSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 795-904 3.90e-32

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: 121.15  E-value: 3.90e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  795 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYiRRGL--W 870
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2023175293  871 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 904
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 563-630 1.01e-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: 89.71  E-value: 1.01e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  563 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCRVEGDTECRTKLDPPMDGTDCDPGKWCKAGECT 630
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 162-277 4.10e-20

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: 87.37  E-value: 4.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  162 EEPSTEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATVDPRppmpsdaSCFYTGTVLRHPGSLASFS 241
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTD-------HCYYQGHVEGHPDSSVALS 92

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2023175293  242 TCgGGLMGFIQLNEDFIFIEPF-NDTMAIIGHPHRLY 277
Cdd:pfam01562   93 TC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1095-1147 1.74e-13

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023175293 1095 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1147
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1044-1086 2.64e-10

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023175293 1044 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREVEDC 1086
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 928-980 7.89e-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: 52.84  E-value: 7.89e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  928 WGDCNATCGGGERKTTVSCTKIMNKniSLVDNKKCKDLTKPePQIRKCNEQPC 980
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1040 6.29e-08

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: 50.14  E-value: 6.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  984 WMMTEWTTCSRTCGKGVQSRQVACTRQLENGTLIrawERDC-IGPKPATMQRCEGQDC 1040
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECsAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 727-793 3.17e-05

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: 44.31  E-value: 3.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  727 CALFCSPVGKEQPVLLSEKVLDGTSCGYQG------LDVCANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 793
Cdd:pfam19236   43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 329-546 1.98e-81

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: 264.87  E-value: 1.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  329 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPADLYIGHHGEKMLESFCKWQ 408
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  409 HeefgrkndihlEMSTSWGEDVASVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 488
Cdd:cd04273     81 K-----------KLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023175293  489 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 546
Cdd:cd04273    149 GHVLGMPHDGDGNSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 795-904 3.90e-32

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: 121.15  E-value: 3.90e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  795 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYiRRGL--W 870
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2023175293  871 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 904
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 331-546 1.80e-27

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: 110.85  E-value: 1.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  331 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLgvqvNLRVIkLILLhETPAD---LYIGHHGEKMLESFC 405
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKEL----NIRVV-LVGL-EIWTDedkIDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  406 KWQHEEFGRKNDiHlemstswgedvasvDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN---LAF 482
Cdd:pfam01421   75 KWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAV 133

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023175293  483 TIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASSCLL 546
Cdd:pfam01421  134 TMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 563-630 1.01e-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: 89.71  E-value: 1.01e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  563 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCRVEGDTECRTKLDPPMDGTDCDPGKWCKAGECT 630
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 162-277 4.10e-20

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: 87.37  E-value: 4.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  162 EEPSTEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATVDPRppmpsdaSCFYTGTVLRHPGSLASFS 241
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTD-------HCYYQGHVEGHPDSSVALS 92

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2023175293  242 TCgGGLMGFIQLNEDFIFIEPF-NDTMAIIGHPHRLY 277
Cdd:pfam01562   93 TC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1095-1147 1.74e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023175293 1095 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1147
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1044-1086 2.64e-10

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023175293 1044 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREVEDC 1086
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 928-980 7.89e-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: 52.84  E-value: 7.89e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  928 WGDCNATCGGGERKTTVSCTKIMNKniSLVDNKKCKDLTKPePQIRKCNEQPC 980
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1040 6.29e-08

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: 50.14  E-value: 6.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  984 WMMTEWTTCSRTCGKGVQSRQVACTRQLENGTLIrawERDC-IGPKPATMQRCEGQDC 1040
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECsAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 987-1040 8.11e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.11  E-value: 8.11e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2023175293   987 TEWTTCSRTCGKGVQSRQVACTRQLENGTlirawERDCIGPKPATmQRCEGQDC 1040
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNG-----GGPCTGEDVET-RACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1092-1147 2.25e-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: 2.25e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293  1092 CYVWrvGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 1147
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 727-793 3.17e-05

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: 44.31  E-value: 3.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  727 CALFCSPVGKEQPVLLSEKVLDGTSCGYQG------LDVCANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 793
Cdd:pfam19236   43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1043-1088 6.38e-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: 41.80  E-value: 6.38e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 2023175293  1043 VWEAGVWSECSVKCGKGVRHRTVRCTNPRKKCV---LSTRPREVEDCED 1088
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1087-1141 4.24e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293 1087 EDYSKCYVWrvGDWSKCSITCGKGMQSRVIQCMH-KITGRHGNECFSSEKPAAYRP 1141
Cdd:PTZ00441   235 ERTASCGPW--DEWTPCSVTCGKGTHSRSRPILHeGCTTHMVEECEEEECPVEPEP 288
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 928-980 2.58e-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: 37.18  E-value: 2.58e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2023175293   928 WGDCNATCGGGERKTTVSCtkimNKNISLVDNKKCkdlTKPEPQIRKCNEQPC 980
Cdd:smart00209    7 WSPCSVTCGGGVQTRTRSC----CSPPPQNGGGPC---TGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 329-546 1.98e-81

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: 264.87  E-value: 1.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  329 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPADLYIGHHGEKMLESFCKWQ 408
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  409 HeefgrkndihlEMSTSWGEDVASVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 488
Cdd:cd04273     81 K-----------KLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023175293  489 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 546
Cdd:cd04273    149 GHVLGMPHDGDGNSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 330-546 7.27e-33

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: 126.19  E-value: 7.27e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  330 NIETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQhkslgvQVNLRVIkLILLhE--TPADLY-IGHHGEKMLESF 404
Cdd:cd04269      2 YVELVVVVDNSLYKKYGSNlsKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGL-EiwTDKDKIsVSGDAGETLNRF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  405 CKWqheefgRKNDIHLEMStswgedvasVDAAILITRKDFCVHkdepcdTVGIAYLNGMCSEKRKCIIAED---NGLNLA 481
Cdd:cd04269     74 LDW------KRSNLLPRKP---------HDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNLLLFA 132

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023175293  482 FTIAHEMGHNMGINHDNDHPSCADGLHIMSgewikgQNLGDVS--WSRCSKEDLERFLRSKASSCLL 546
Cdd:cd04269    133 VTMAHELGHNLGMEHDDGGCTCGRSTCIMA------PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 795-904 3.90e-32

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: 121.15  E-value: 3.90e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  795 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYiRRGL--W 870
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2023175293  871 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 904
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 331-546 1.80e-27

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: 110.85  E-value: 1.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  331 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLgvqvNLRVIkLILLhETPAD---LYIGHHGEKMLESFC 405
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKEL----NIRVV-LVGL-EIWTDedkIDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  406 KWQHEEFGRKNDiHlemstswgedvasvDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN---LAF 482
Cdd:pfam01421   75 KWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAV 133

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023175293  483 TIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASSCLL 546
Cdd:pfam01421  134 TMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 331-538 1.77e-22

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: 96.34  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  331 IETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPADLYIGHHGEKMLESFCKWQ 408
Cdd:cd04267      3 IELVVVADHRMVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  409 HEEFGRkndihlemstswgedvasVDAAILITRKDFcvhkdEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNL--AFTIAH 486
Cdd:cd04267     83 AEGPIR------------------HDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAH 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293  487 EMGHNMGINHDND----HPSCADGLHIMSgewIKGQNLGDVSWSRCSKEDLERFLR 538
Cdd:cd04267    140 ELGHNLGAEHDGGdelaFECDGGGNYIMA---PVDSGLNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 563-630 1.01e-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: 89.71  E-value: 1.01e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  563 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCRVEGDTECRTKLDPPMDGTDCDPGKWCKAGECT 630
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 162-277 4.10e-20

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: 87.37  E-value: 4.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  162 EEPSTEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATVDPRppmpsdaSCFYTGTVLRHPGSLASFS 241
Cdd:pfam01562   20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTD-------HCYYQGHVEGHPDSSVALS 92

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2023175293  242 TCgGGLMGFIQLNEDFIFIEPF-NDTMAIIGHPHRLY 277
Cdd:pfam01562   93 TC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 410-537 9.59e-14

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 70.24  E-value: 9.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  410 EEFGRKNDIHLEMStswGEDVASVDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN---LAFTIAH 486
Cdd:cd00203     32 QIWRDYLNIRFVLV---GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAH 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023175293  487 EMGHNMGINHDND--------------HPSCADGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFL 537
Cdd:cd00203    103 ELGHALGFYHDHDrkdrddyptiddtlNAEDDDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1095-1147 1.74e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023175293 1095 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1147
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 374-545 2.26e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 67.76  E-value: 2.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  374 VNLRVIKLILLHETPADLYIGHHG------EKMLESFckwqhEEFGRKNDiHLEMStswgedvasvDAAILITRKDFCVH 447
Cdd:cd04272     46 IRLLLVGITISKDPDFEPYIHPINygyidaAETLENF-----NEYVKKKR-DYFNP----------DVVFLVTGLDMSTY 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  448 KDEPCDTV--GIAYLNGMCSEKRKCIIaEDNG--LNLAFTIAHEMGHNMGINHDND--------HPS---C--ADGlHIM 510
Cdd:cd04272    110 SGGSLQTGtgGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHLLGAPHDGSpppswvkgHPGsldCpwDDG-YIM 187

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2023175293  511 SgewikgQNLGDVS---WSRCSKEDLERFLRSKASSCL 545
Cdd:cd04272    188 S------YVVNGERqyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
334-511 7.11e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 7.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  334 VVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSlgvQVNLRVIKLILLHET-PADLYIGHHG--EKMLESFcKWQHE 410
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTcPYTPPACSTGdsSDRLSEF-QDFSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  411 EFGRKNDihlemstswgedvasvDAAILITrkdfcvhkDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLN--------LAF 482
Cdd:pfam13688   84 WRGTQND----------------DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQ 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2023175293  483 TIAHEMGHNMGINHDND----HPSC--------ADGLHIMS 511
Cdd:pfam13688  140 VFAHEIGHNFGAVHDCDsstsSQCCppsnstcpAGGRYIMN 180
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1044-1086 2.64e-10

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023175293 1044 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREVEDC 1086
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 928-980 7.89e-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: 52.84  E-value: 7.89e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  928 WGDCNATCGGGERKTTVSCTKIMNKniSLVDNKKCKDLTKPePQIRKCNEQPC 980
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 483-544 2.72e-08

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: 56.23  E-value: 2.72e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023175293  483 TIAHEMGHNMGINHDNDHPSCA-----DGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFLRSKASSC 544
Cdd:cd04270    170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 984-1040 6.29e-08

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: 50.14  E-value: 6.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175293  984 WMMTEWTTCSRTCGKGVQSRQVACTRQLENGTLIrawERDC-IGPKPATMQRCEGQDC 1040
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECsAQKKPPETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 354-497 2.55e-07

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: 50.45  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  354 ILTILNMVFNLFQHKsLGVQVNLRVIKLILLHETPadlYIGHHGEKMLESFCKWQHEEFGRKNdihlemstswgedvasV 433
Cdd:pfam13582    3 IVSLVNRANTIYERD-LGIRLQLAAIIITTSADTP---YTSSDALEILDELQEVNDTRIGQYG----------------Y 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023175293  434 DAAILITRKDFCvhkdepcDTVGIAYLNGMCSEKRKCIIAED---NGLNLAFTIAHEMGHNMGINHD 497
Cdd:pfam13582   63 DLGHLFTGRDGG-------GGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 987-1040 8.11e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.11  E-value: 8.11e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2023175293   987 TEWTTCSRTCGKGVQSRQVACTRQLENGTlirawERDCIGPKPATmQRCEGQDC 1040
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNG-----GGPCTGEDVET-RACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1092-1147 2.25e-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: 2.25e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293  1092 CYVWrvGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 1147
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 727-793 3.17e-05

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: 44.31  E-value: 3.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023175293  727 CALFCSPVGKEQPVLLSEKVLDGTSCGYQG------LDVCANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 793
Cdd:pfam19236   43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1043-1088 6.38e-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: 41.80  E-value: 6.38e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 2023175293  1043 VWEAGVWSECSVKCGKGVRHRTVRCTNPRKKCV---LSTRPREVEDCED 1088
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 987-1040 8.67e-05

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.11  E-value: 8.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293  987 TEWTTCSRTCGKGVQSRQVACTRQLENGtlirawERDCigpkPATMQR--CEGQDC 1040
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRTRTVIVEPQNG------GRPC----PELLERrpCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 454-530 1.29e-04

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 44.54  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  454 TVGIAYLNGMCSEKRKCIiAEDNGLNLAFT-------------IAHEMGHNMGINHDND-----HPSC----------AD 505
Cdd:pfam13574   86 ELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsqyaSSGCernaatsvcsAN 164

                           90       100
                   ....*....|....*....|....*
gi 2023175293  506 GLHIMSGEWIKGQNLgdvsWSRCSK 530
Cdd:pfam13574  165 GSFIMNPASKSNNDL----FSPCSI 185
TSP_1 pfam00090
Thrombospondin type 1 domain;
987-1040 3.39e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.32  E-value: 3.39e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023175293  987 TEWTTCSRTCGKGVQSRQVACTRQLENGTlirawerDCIGPKPATmQRCEGQDC 1040
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGE-------PCTGDDIET-QACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
1098-1147 3.81e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.32  E-value: 3.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023175293 1098 GDWSKCSITCGKGMQSRVIQCMHKITGrhGNECfsSEKPAAYRPCHLQPC 1147
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPC--TGDDIETQACKMDKC 49
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 335-511 4.02e-04

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 42.99  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  335 VVADPAMVSYHGA-DAARRFI---LTILNMVFNlfqhKSLGVQvnLRVI---KLILLHETPADLYIGHHGEKMlesfckw 407
Cdd:pfam13583    9 VATDCTYSASFGSvDELRANInatVTTANEVYG----RDFNVS--LALIsdrDVIYTDSSTDSFNADCSGGDL------- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175293  408 qheefgrkNDIHLEMSTSWgEDVASVDAAILITrkDFCVHKDEpcdtVGIAYLNGMCSEKRKCiiAEDNGLNLAF----T 483
Cdd:pfam13583   76 --------GNWRLATLTSW-RDSLNYDLAYLTL--MTGPSGQN----VGVAWVGALCSSARQN--AKASGVARSRdewdI 138

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2023175293  484 IAHEMGHNMGINHDNDHPSC--------ADGLHIMS 511
Cdd:pfam13583  139 FAHEIGHTFGAVHDCSSQGEglssstedGSGQTIMS 174
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1087-1141 4.24e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023175293 1087 EDYSKCYVWrvGDWSKCSITCGKGMQSRVIQCMH-KITGRHGNECFSSEKPAAYRP 1141
Cdd:PTZ00441   235 ERTASCGPW--DEWTPCSVTCGKGTHSRSRPILHeGCTTHMVEECEEEECPVEPEP 288
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 928-980 2.58e-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: 37.18  E-value: 2.58e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2023175293   928 WGDCNATCGGGERKTTVSCtkimNKNISLVDNKKCkdlTKPEPQIRKCNEQPC 980
Cdd:smart00209    7 WSPCSVTCGGGVQTRTRSC----CSPPPQNGGGPC---TGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
1049-1082 8.17e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 8.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2023175293 1049 WSECSVKCGKGVRHRTVRCTNPRKK---CVLSTRPRE 1082
Cdd:pfam00090    6 WSPCSVTCGKGIQVRQRTCKSPFPGgepCTGDDIETQ 42
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1041-1064 8.87e-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: 8.87e-03
                           10        20
                   ....*....|....*....|....
gi 2023175293 1041 MTVWeaGVWSECSVKCGKGVRHRT 1064
Cdd:pfam19028    3 VSEW--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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