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Conserved domains on  [gi|2217354903|ref|XP_047272839|]
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A disintegrin and metalloproteinase with thrombospondin motifs 19 isoform X9 [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) ...
 1-206 1.53e-75

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: 244.84  E-value: 1.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   1 MVSYHGADAARRFILTILNMVFNLFQHKSLSVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQHEEfGKKNDihl 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKL-NPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  81 emstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEMGHNMGINHDNDH 160
Cdd:cd04273    89 -------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 161 PSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 206
Cdd:cd04273   161 NSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 455-564 3.00e-33

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: 123.84  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 455 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALR-DAGKQSINSDWKIE-HSGAFNLAGTTVHYVRR-GLWE 531
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217354903 532 KISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 564
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 9.06e-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: 86.63  E-value: 9.06e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 223 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 755-807 2.60e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 2.60e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217354903 755 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-350 7.71e-10

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: 55.29  E-value: 7.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217354903  301 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 350
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 704-746 9.70e-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: 52.07  E-value: 9.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217354903 704 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 746
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 644-700 3.27e-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: 50.53  E-value: 3.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 644 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 700
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSI---VPDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 583-640 8.96e-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: 49.37  E-value: 8.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 583 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 640
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-453 3.39e-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: 43.93  E-value: 3.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217354903 387 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 453
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-206 1.53e-75

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: 244.84  E-value: 1.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   1 MVSYHGADAARRFILTILNMVFNLFQHKSLSVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQHEEfGKKNDihl 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKL-NPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  81 emstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEMGHNMGINHDNDH 160
Cdd:cd04273    89 -------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 161 PSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 206
Cdd:cd04273   161 NSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 455-564 3.00e-33

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: 123.84  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 455 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALR-DAGKQSINSDWKIE-HSGAFNLAGTTVHYVRR-GLWE 531
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217354903 532 KISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 564
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 4-207 4.32e-23

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: 97.76  E-value: 4.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   4 YHGAD--AARRFILTILNMVfNLFqHKSLSVQVNLRVIKL------ILLHETPpelyighhgEKMLESFCKWQHEEFGKK 75
Cdd:pfam01421  16 KMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLRNFLKWRQEYLKKR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  76 NDiHlemstnwgedmtsvDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN---LAFTIAHEMGHNM 152
Cdd:pfam01421  85 KP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 153 GINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASNCLLQ 207
Cdd:pfam01421 144 GMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 9.06e-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: 86.63  E-value: 9.06e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 223 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 755-807 2.60e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 2.60e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217354903 755 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-350 7.71e-10

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: 55.29  E-value: 7.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217354903  301 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 350
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 704-746 9.70e-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: 52.07  E-value: 9.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217354903 704 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 746
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
301-349 1.93e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 301 GEWSLWSPCSRTCSAGISSRERKCPGLDSEARDCNGPRKQYRICENPPC 349
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 644-700 3.27e-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: 50.53  E-value: 3.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 644 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 700
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSI---VPDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 583-640 8.96e-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: 49.37  E-value: 8.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 583 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 640
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 647-700 3.21e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 3.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903  647 TEWTPCSRTCGKGMQSRQVACTQQLSngtliRARERDCIGPKPaSAQRCEGQDC 700
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPP-----QNGGGPCTGEDV-ETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-453 3.39e-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: 43.93  E-value: 3.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217354903 387 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 453
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-807 5.52e-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: 41.42  E-value: 5.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903  754 VWRMGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 807
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 717-801 1.70e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 717 GKGIRHRTVR----CTNPRKKCVLST-----------RPREAEDC---EDYSKCYVWrmGDWSKCSITCGKGMQSRVIQC 778
Cdd:PTZ00441  187 GQGINHQFNRllagCRPREGKCKFYSdadweeaknliKPFIAKVCtevERTASCGPW--DEWTPCSVTCGKGTHSRSRPI 264

                          90       100
                  ....*....|....*....|....
gi 2217354903 779 MH-KITGRHGNECFSSEKPAAYRP 801
Cdd:PTZ00441  265 LHeGCTTHMVEECEEEECPVEPEP 288
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 703-748 3.12e-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: 39.49  E-value: 3.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217354903  703 VWEAGVWSECSVKCGKGIRHRTVRCTNPRKKCV---LSTRPREAEDCED 748
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 583-640 5.99e-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: 35.64  E-value: 5.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217354903  583 WTHTS-WEDCDATCGGGERKTTVSCtkimsknISIVDNEKCKYLTKPEPQIRKCNEQPC 640
Cdd:smart00209   1 WSEWSeWSPCSVTCGGGVQTRTRSC-------CSPPPQNGGGPCTGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-206 1.53e-75

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: 244.84  E-value: 1.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   1 MVSYHGADAARRFILTILNMVFNLFQHKSLSVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQHEEfGKKNDihl 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKKL-NPPND--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  81 emstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEMGHNMGINHDNDH 160
Cdd:cd04273    89 -------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 161 PSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 206
Cdd:cd04273   161 NSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 455-564 3.00e-33

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: 123.84  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 455 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLALR-DAGKQSINSDWKIE-HSGAFNLAGTTVHYVRR-GLWE 531
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217354903 532 KISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 564
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 1-206 1.09e-27

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 110.78  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   1 MVSYHGAD--AARRFILTILNMVFNLFQhkslsvQVNLRVIkLILLhetppELY-------IGHHGEKMLESFCKWqhee 71
Cdd:cd04269    13 LYKKYGSNlsKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGL-----EIWtdkdkisVSGDAGETLNRFLDW---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  72 fgKKNDIHLEMStnwgedmtsVDAAILITRKDFCVHkdepcdTVGIAYLSGMCSEKRKCIIAED---NGLNLAFTIAHEM 148
Cdd:cd04269    77 --KRSNLLPRKP---------HDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNLLLFAVTMAHEL 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 149 GHNMGINHDNDHPSCADGLHIMSgewikgQNLGDVS--WSRCSKEDLERFLRSKASNCLL 206
Cdd:cd04269   140 GHNLGMEHDDGGCTCGRSTCIMA------PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 4-207 4.32e-23

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: 97.76  E-value: 4.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   4 YHGAD--AARRFILTILNMVfNLFqHKSLSVQVNLRVIKL------ILLHETPpelyighhgEKMLESFCKWQHEEFGKK 75
Cdd:pfam01421  16 KMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLRNFLKWRQEYLKKR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  76 NDiHlemstnwgedmtsvDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN---LAFTIAHEMGHNM 152
Cdd:pfam01421  85 KP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 153 GINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASNCLLQ 207
Cdd:pfam01421 144 GMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 9.06e-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: 86.63  E-value: 9.06e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 223 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 1-198 2.38e-19

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: 86.71  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   1 MVSYHGAD--AARRFILTILNMVFNLFQHKSLSVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQHEEFGKkndi 78
Cdd:cd04267    13 MVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWRAEGPIR---- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  79 hlemstnwgedmtsVDAAILITRKDFcvhkdEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNL--AFTIAHEMGHNMGINH 156
Cdd:cd04267    89 --------------HDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217354903 157 DND----HPSCADGLHIMSgewIKGQNLGDVSWSRCSKEDLERFLR 198
Cdd:cd04267   150 DGGdelaFECDGGGNYIMA---PVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 70-197 2.29e-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: 71.78  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  70 EEFGKKNDIHLEMStNWGEDmtSVDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN---LAFTIAH 146
Cdd:cd00203    32 QIWRDYLNIRFVLV-GVEID--KADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAH 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217354903 147 EMGHNMGINHDND--------------HPSCADGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFL 197
Cdd:cd00203   103 ELGHALGFYHDHDrkdrddyptiddtlNAEDDDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 34-205 1.03e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 68.15  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  34 VNLRVIKLILLHETPPELYIGHHG------EKMLESFckwqhEEFGKKNDiHLEMStnwgedmtsvDAAILITRKDFCVH 107
Cdd:cd04272    46 IRLLLVGITISKDPDFEPYIHPINygyidaAETLENF-----NEYVKKKR-DYFNP----------DVVFLVTGLDMSTY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 108 KDEPCDTV--GIAYLSGMCSEKRKCIIaEDNG--LNLAFTIAHEMGHNMGINHDND--------HPSCA-----DGlHIM 170
Cdd:cd04272   110 SGGSLQTGtgGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHLLGAPHDGSpppswvkgHPGSLdcpwdDG-YIM 187

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217354903 171 SgewikgQNLGDVS---WSRCSKEDLERFLRSKASNCL 205
Cdd:cd04272   188 S------YVVNGERqyrFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 755-807 2.60e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 2.60e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217354903 755 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 807
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 301-350 7.71e-10

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: 55.29  E-value: 7.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217354903  301 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 350
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
2-171 8.37e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.97  E-value: 8.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903   2 VSYHGADAARRFILTILNMVFNLFQHKSlsvQVNLRVIKLILLHETPPELYIGHH---GEKMLESFcKWQHEEFGKKNDi 78
Cdd:pfam13688  16 VAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACStgdSSDRLSEF-QDFSAWRGTQND- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  79 hlemstnwgedmtsvDAAILITrkdfcvhkDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLN--------LAFTIAHEMGH 150
Cdd:pfam13688  91 ---------------DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIGH 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217354903 151 NMGINHDND----HPSC--------ADGLHIMS 171
Cdd:pfam13688 148 NFGAVHDCDsstsSQCCppsnstcpAGGRYIMN 180
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 704-746 9.70e-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: 52.07  E-value: 9.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217354903 704 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 746
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
301-349 1.93e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 301 GEWSLWSPCSRTCSAGISSRERKCPGLDSEARDCNGPRKQYRICENPPC 349
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 143-204 2.29e-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: 55.84  E-value: 2.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217354903 143 TIAHEMGHNMGINHDNDHPSCA-----DGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFLRSKASNC 204
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 644-700 3.27e-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: 50.53  E-value: 3.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 644 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 700
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSI---VPDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 583-640 8.96e-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: 49.37  E-value: 8.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217354903 583 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 640
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 84-157 1.12e-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: 51.22  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903  84 TNWGEDMTSVDAAILITRKDF-------CVHKDEPCDTVGIAYLSGMCSEKRKCIIAED---NGLNLAFTIAHEMGHNMG 153
Cdd:pfam13582  39 SSDALEILDELQEVNDTRIGQygydlghLFTGRDGGGGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFG 118


                  ....
gi 2217354903 154 INHD 157
Cdd:pfam13582 119 LNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 647-700 3.21e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.19  E-value: 3.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903  647 TEWTPCSRTCGKGMQSRQVACTQQLSngtliRARERDCIGPKPaSAQRCEGQDC 700
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPP-----QNGGGPCTGEDV-ETRACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-453 3.39e-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: 43.93  E-value: 3.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217354903 387 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 453
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 114-190 3.44e-05

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: 45.70  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 114 TVGIAYLSGMCSEKRKCIiAEDNGLNLAFT-------------IAHEMGHNMGINHDND-----HPSC----------AD 165
Cdd:pfam13574  86 ELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsqyaSSGCernaatsvcsAN 164

                          90       100
                  ....*....|....*....|....*
gi 2217354903 166 GLHIMSGEWIKGQNLgdvsWSRCSK 190
Cdd:pfam13574 165 GSFIMNPASKSNNDL----FSPCSI 185
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 754-807 5.52e-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: 41.42  E-value: 5.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903  754 VWRMGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 807
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
647-700 8.16e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.86  E-value: 8.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903 647 TEWTPCSRTCGKGMQSRQVACTQQLSNGTlirarerDCIGPKpASAQRCEGQDC 700
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGE-------PCTGDD-IETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 301-338 1.34e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 40.34  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217354903 301 GEWSLWSPCSRTCSAGISSRERK-----------CPGLdSEARDCNGPR 338
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTvivepqnggrpCPEL-LERRPCNLPP 51
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 717-801 1.70e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354903 717 GKGIRHRTVR----CTNPRKKCVLST-----------RPREAEDC---EDYSKCYVWrmGDWSKCSITCGKGMQSRVIQC 778
Cdd:PTZ00441  187 GQGINHQFNRllagCRPREGKCKFYSdadweeaknliKPFIAKVCtevERTASCGPW--DEWTPCSVTCGKGTHSRSRPI 264

                          90       100
                  ....*....|....*....|....
gi 2217354903 779 MH-KITGRHGNECFSSEKPAAYRP 801
Cdd:PTZ00441  265 LHeGCTTHMVEECEEEECPVEPEP 288
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 647-700 2.75e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217354903 647 TEWTPCSRTCGKGMQSRQVACTQQLSNGtlirarERDCigPKPASAQRCEGQDC 700
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRTRTVIVEPQNG------GRPC--PELLERRPCNLPPC 52
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 306-349 2.78e-04

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 39.24  E-value: 2.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217354903 306 WSPCSRTCSAGISSRERkcpgldSEARDCNgPRKQYRICENPPC 349
Cdd:pfam19035   8 WSPCSKTCGMGVSTRVS------NDNAECK-LVTETRLCQLRPC 44
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 703-748 3.12e-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: 39.49  E-value: 3.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217354903  703 VWEAGVWSECSVKCGKGIRHRTVRCTNPRKKCV---LSTRPREAEDCED 748
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
758-807 1.22e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.40  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217354903 758 GDWSKCSITCGKGMQSRVIQCMHKITGrhGNECfsSEKPAAYRPCHLQPC 807
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPC--TGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 583-640 5.99e-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: 35.64  E-value: 5.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217354903  583 WTHTS-WEDCDATCGGGERKTTVSCtkimsknISIVDNEKCKYLTKPEPQIRKCNEQPC 640
Cdd:smart00209   1 WSEWSeWSPCSVTCGGGVQTRTRSC-------CSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
709-743 6.60e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 6.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217354903 709 WSECSVKCGKGIRHRTVRCTNPRKK---CVLSTRPREA 743
Cdd:pfam00090   6 WSPCSVTCGKGIQVRQRTCKSPFPGgepCTGDDIETQA 43
 
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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