NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|569003829|ref|XP_006525982|]
View 

A disintegrin and metalloproteinase with thrombospondin motifs 19 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 328-545 1.12e-80

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: 262.94  E-value: 1.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  328 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVLKLILLHETPADLYIGHHGEKMLESFCKWQ 407
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  408 HEefgrrndvhleMSTSWGEDIAAVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 487
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003829  488 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 545
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 ...
 794-903 1.12e-31

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: 119.99  E-value: 1.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   794 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSFLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYlRRGL--W 869
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 569003829   870 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 903
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 ...
 562-629 1.81e-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: 88.94  E-value: 1.81e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829   562 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEAECRTKLDPPMDGTDCDPGKWCKAGECT 629
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 158-276 1.04e-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: 88.91  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   158 AQQEEPSAEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATADPGSsllpdasCFYTGTVLRHPGSLA 237
Cdd:pfam01562   17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH-------CYYQGHVEGHPDSSV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 569003829   238 SFSTCgGGLMGFIQLNEDFLFIEPF-NDTMAIIGHPHRLY 276
Cdd:pfam01562   90 ALSTC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1118-1170 1.77e-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: 1.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569003829  1118 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1170
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1067-1109 1.38e-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: 54.77  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003829  1067 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREAEDC 1109
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1063 2.20e-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: 51.68  E-value: 2.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829  1007 WMMTEWTTCSRTCGKGVQSRQVACTQQLENGTLIrawERDCLG-PKPATVQRCEGQDC 1063
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 927-979 2.36e-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: 51.30  E-value: 2.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 569003829   927 WGDCNATCGGGERKTMVSCTKIMSKniSLVDNKKCKDLTKPePQIRKCNEQPC 979
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--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 ...
 726-792 4.54e-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: 4.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003829   726 CALFCSPVGKEQPVLLSEKVMDGTSCGYQG------LDICANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 792
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) ...
 328-545 1.12e-80

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: 262.94  E-value: 1.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  328 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVLKLILLHETPADLYIGHHGEKMLESFCKWQ 407
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  408 HEefgrrndvhleMSTSWGEDIAAVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 487
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003829  488 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 545
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 ...
 794-903 1.12e-31

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: 119.99  E-value: 1.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   794 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSFLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYlRRGL--W 869
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 569003829   870 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 903
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 330-545 1.27e-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: 111.24  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   330 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLGVQVNLRVLKL------ILLHETPadlyighhgEKMLE 401
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   402 SFCKWQHEEFGRRNDvHlemstswgediaavDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN--- 478
Cdd:pfam01421   72 NFLKWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNles 130

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   479 LAFTIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASSCLL 545
Cdd:pfam01421  131 FAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 562-629 1.81e-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: 88.94  E-value: 1.81e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829   562 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEAECRTKLDPPMDGTDCDPGKWCKAGECT 629
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 158-276 1.04e-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: 88.91  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   158 AQQEEPSAEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATADPGSsllpdasCFYTGTVLRHPGSLA 237
Cdd:pfam01562   17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH-------CYYQGHVEGHPDSSV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 569003829   238 SFSTCgGGLMGFIQLNEDFLFIEPF-NDTMAIIGHPHRLY 276
Cdd:pfam01562   90 ALSTC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1118-1170 1.77e-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: 1.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569003829  1118 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1170
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1067-1109 1.38e-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: 54.77  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003829  1067 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREAEDC 1109
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1063 2.20e-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: 51.68  E-value: 2.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829  1007 WMMTEWTTCSRTCGKGVQSRQVACTQQLENGTLIrawERDCLG-PKPATVQRCEGQDC 1063
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 927-979 2.36e-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: 51.30  E-value: 2.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 569003829   927 WGDCNATCGGGERKTMVSCTKIMSKniSLVDNKKCKDLTKPePQIRKCNEQPC 979
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1115-1170 2.19e-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: 2.19e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003829   1115 CYVWrvGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 1170
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1010-1063 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 569003829   1010 TEWTTCSRTCGKGVQSRQVACTQQLENGTlirawERDCLGPKPATvQRCEGQDC 1063
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNG-----GGPCTGEDVET-RACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 726-792 4.54e-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: 4.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003829   726 CALFCSPVGKEQPVLLSEKVMDGTSCGYQG------LDICANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 792
Cdd:pfam19236   43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1066-1111 8.32e-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: 8.32e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 569003829   1066 VWEAGVWSECSVKCGKGVRHRTVRCTNPRKKCV---LSTRPREAEDCED 1111
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1110-1164 4.26e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 4.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003829 1110 EDYSKCYVWrvGDWSKCSITCGKGMQSRVIQCMH-KITGRHGNECFSSEKPAAYRP 1164
Cdd:PTZ00441  235 ERTASCGPW--DEWTPCSVTCGKGTHSRSRPILHeGCTTHMVEECEEEECPVEPEP 288
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 328-545 1.12e-80

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: 262.94  E-value: 1.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  328 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVLKLILLHETPADLYIGHHGEKMLESFCKWQ 407
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  408 HEefgrrndvhleMSTSWGEDIAAVDAAILITRKDFCvHKDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNLAFTIAHEM 487
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003829  488 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASSCLL 545
Cdd:cd04273   149 GHVLGMPHDGDGNSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 329-545 4.78e-32

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: 123.88  E-value: 4.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  329 NIETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQhkslgvQVNLRVLkLILLhE--TPADLY-IGHHGEKMLESF 403
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSNlsKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGL-EiwTDKDKIsVSGDAGETLNRF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  404 CKWQHEEFGRRNdVHlemstswgediaavDAAILITRKDFCVHkdepcdTVGIAYLNGMCSEKRKCIIAED---NGLNLA 480
Cdd:cd04269    74 LDWKRSNLLPRK-PH--------------DNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNLLLFA 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003829  481 FTIAHEMGHNMGINHDNDHPSCADGLHIMSgewikgQNLGDVS--WSRCSKEDLERFLRSKASSCLL 545
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 ...
 794-903 1.12e-31

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: 119.99  E-value: 1.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   794 VIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSFLALRDAS-KQSINSDWKIE-HSGAFSLAGTTVHYlRRGL--W 869
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQgKYILNGKGSISlNPTYPSLLGTVLEY-RRSLpaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 569003829   870 EKISAKGPTTTPLHLLVL--LFQDQNYGLHYEYTVP 903
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 330-545 1.27e-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: 111.24  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   330 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLGVQVNLRVLKL------ILLHETPadlyighhgEKMLE 401
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   402 SFCKWQHEEFGRRNDvHlemstswgediaavDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN--- 478
Cdd:pfam01421   72 NFLKWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNles 130

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   479 LAFTIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASSCLL 545
Cdd:pfam01421  131 FAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 330-537 1.37e-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: 96.72  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  330 IETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQHKSLGVQVNLRVLKLILLHETPADLYIGHHGEKMLESFCKWQ 407
Cdd:cd04267     3 IELVVVADHRMVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  408 HEEFGRRndvhlemstswgediaavDAAILITRKDFcvhkdEPCDTVGIAYLNGMCSEKRKCIIAEDNGLNL--AFTIAH 485
Cdd:cd04267    83 AEGPIRH------------------DNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAH 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003829  486 EMGHNMGINHDND----HPSCADGLHIMSgewIKGQNLGDVSWSRCSKEDLERFLR 537
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 ...
 562-629 1.81e-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: 88.94  E-value: 1.81e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829   562 PGMAYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEAECRTKLDPPMDGTDCDPGKWCKAGECT 629
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 158-276 1.04e-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: 88.91  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   158 AQQEEPSAEEVLLRIPALSRDLYLLLRRDGRFLAQRFAVEQWPKPGPDPTRATADPGSsllpdasCFYTGTVLRHPGSLA 237
Cdd:pfam01562   17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH-------CYYQGHVEGHPDSSV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 569003829   238 SFSTCgGGLMGFIQLNEDFLFIEPF-NDTMAIIGHPHRLY 276
Cdd:pfam01562   90 ALSTC-SGLRGFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 426-536 1.74e-13

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 69.86  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  426 GEDIAAVDAAILITRKDFcvhkdePCDTVGIAYLNGMCSEKRKCIIAEDNGLN---LAFTIAHEMGHNMGINHDND---- 498
Cdd:cd00203    46 GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDrkdr 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 569003829  499 ----------HPSCADGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFL 536
Cdd:cd00203   120 ddyptiddtlNAEDDDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1118-1170 1.77e-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: 1.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569003829  1118 WRVGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 1170
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 373-544 6.82e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.22  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  373 VNLRVLKLILLHETPADLYIGHHG------EKMLESFCKWqheEFGRRndvHLEMStswgediaavDAAILITRKDFCVH 446
Cdd:cd04272    46 IRLLLVGITISKDPDFEPYIHPINygyidaAETLENFNEY---VKKKR---DYFNP----------DVVFLVTGLDMSTY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829  447 KDEPCDTV--GIAYLNGMCSEKRKCIIaEDNG--LNLAFTIAHEMGHNMGINHDND--------HPS---C--ADGlHIM 509
Cdd:cd04272   110 SGGSLQTGtgGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHLLGAPHDGSpppswvkgHPGsldCpwDDG-YIM 187

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 569003829  510 SgewikgQNLGDVS---WSRCSKEDLERFLRSKASSCL 544
Cdd:cd04272   188 S------YVVNGERqyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
333-510 3.58e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 60.51  E-value: 3.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   333 VVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSlgvQVNLRVLKLILLHET-PADLYIGHHG--EKMLESFckwqhe 409
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTcPYTPPACSTGdsSDRLSEF------ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   410 efgrrndvhlEMSTSWGEDIAAvDAAILITrkdfcvhkDEPCDTVGIAYLNGMCSEKRKCIIAEDNGLN--------LAF 481
Cdd:pfam13688   79 ----------QDFSAWRGTQND-DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQ 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 569003829   482 TIAHEMGHNMGINHDND----HPSC--------ADGLHIMS 510
Cdd:pfam13688  140 VFAHEIGHNFGAVHDCDsstsSQCCppsnstcpAGGRYIMN 180
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1067-1109 1.38e-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: 54.77  E-value: 1.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003829  1067 WEAGVWSECSVKCGKGVRHRTVRC-------TNPRKKCVLSTRPREAEDC 1109
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1063 2.20e-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: 51.68  E-value: 2.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 569003829  1007 WMMTEWTTCSRTCGKGVQSRQVACTQQLENGTLIrawERDCLG-PKPATVQRCEGQDC 1063
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 927-979 2.36e-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: 51.30  E-value: 2.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 569003829   927 WGDCNATCGGGERKTMVSCTKIMSKniSLVDNKKCKDLTKPePQIRKCNEQPC 979
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 482-543 2.78e-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: 2.78e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003829  482 TIAHEMGHNMGINHDNDHPSCA-----DGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFLRSKASSC 543
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 353-496 1.64e-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: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   353 ILTILNMVFNLFQHKsLGVQVNLRVLKLILLHETPadlYIGHHGEKMLESFCKWQHEEFGRRNdvhlemstswgEDIAAV 432
Cdd:pfam13582    3 IVSLVNRANTIYERD-LGIRLQLAAIIITTSADTP---YTSSDALEILDELQEVNDTRIGQYG-----------YDLGHL 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003829   433 daailitrkdfcVHKDEPCDTVGIAYLNGMCSEKRKCIIAED---NGLNLAFTIAHEMGHNMGINHD 496
Cdd:pfam13582   68 ------------FTGRDGGGGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1115-1170 2.19e-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: 2.19e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003829   1115 CYVWrvGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 1170
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1010-1063 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 569003829   1010 TEWTTCSRTCGKGVQSRQVACTQQLENGTlirawERDCLGPKPATvQRCEGQDC 1063
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNG-----GGPCTGEDVET-RACNEQPC 52
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 726-792 4.54e-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: 4.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003829   726 CALFCSPVGKEQPVLLSEKVMDGTSCGYQG------LDICANGRCQKAGCDGLLGSLAREDHCGVCNGNGKSC 792
Cdd:pfam19236   43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1066-1111 8.32e-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: 8.32e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 569003829   1066 VWEAGVWSECSVKCGKGVRHRTVRCTNPRKKCV---LSTRPREAEDCED 1111
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
1010-1063 8.71e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.25  E-value: 8.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 569003829  1010 TEWTTCSRTCGKGVQSRQVACTQQLENGTlirawerDCLGPKPATvQRCEGQDC 1063
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGE-------PCTGDDIET-QACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1010-1063 9.56e-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: 9.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 569003829  1010 TEWTTCSRTCGKGVQSRQVACTQQLENGtlirawERDClgPKPATVQRCEGQDC 1063
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRTRTVIVEPQNG------GRPC--PELLERRPCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 453-529 1.31e-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: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003829   453 TVGIAYLNGMCSEKRKCIiAEDNGLNLAFT-------------IAHEMGHNMGINHDND-----HPSC----------AD 504
Cdd:pfam13574   86 ELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsqyaSSGCernaatsvcsAN 164

                           90       100
                   ....*....|....*....|....*
gi 569003829   505 GLHIMSGEWIKGQNLgdvsWSRCSK 529
Cdd:pfam13574  165 GSFIMNPASKSNNDL----FSPCSI 185
TSP_1 pfam00090
Thrombospondin type 1 domain;
1121-1170 3.56e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.32  E-value: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003829  1121 GDWSKCSITCGKGMQSRVIQCMHKITGrhGNECfsSEKPAAYRPCHLQPC 1170
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPC--TGDDIETQACKMDKC 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1110-1164 4.26e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 4.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003829 1110 EDYSKCYVWrvGDWSKCSITCGKGMQSRVIQCMH-KITGRHGNECFSSEKPAAYRP 1164
Cdd:PTZ00441  235 ERTASCGPW--DEWTPCSVTCGKGTHSRSRPILHeGCTTHMVEECEEEECPVEPEP 288
TSP_1 pfam00090
Thrombospondin type 1 domain;
1072-1106 3.20e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 3.20e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 569003829  1072 WSECSVKCGKGVRHRTVRCTNPRKK---CVLSTRPREA 1106
Cdd:pfam00090    6 WSPCSVTCGKGIQVRQRTCKSPFPGgepCTGDDIETQA 43
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1064-1087 8.95e-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: 8.95e-03
                           10        20
                   ....*....|....*....|....
gi 569003829  1064 MTVWeaGVWSECSVKCGKGVRHRT 1087
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH