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Conserved domains on  [gi|2462601166|ref|XP_054207905|]
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A disintegrin and metalloproteinase with thrombospondin motifs 19 isoform X5 [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) ...
 87-304 1.37e-82

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: 265.64  E-value: 1.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  87 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQ 166
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 167 HEEfGKKNDihlemstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEM 246
Cdd:cd04273    81 KKL-NPPND----------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 247 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 304
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 ...
 553-673 6.34e-29

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: 111.90  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 553 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLgnlcyrhredpTLR-DAGKQSINSDWKIE-HSGAFNLAGTT 630
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL-----------AVKnVQGKYILNGKGSISlNPTYPSLLGTV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462601166 631 VHYVRR-GLWEKISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 673
Cdd:pfam05986  70 LEYRRSlPALEELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 321-388 3.90e-21

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


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.79  E-value: 3.90e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 321 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 388
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 864-916 1.27e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.24  E-value: 1.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462601166 864 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 916
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 399-448 3.56e-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: 56.44  E-value: 3.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462601166  399 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 448
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-855 5.29e-09

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.84  E-value: 5.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462601166 813 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 855
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 753-809 1.76e-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: 1.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 753 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 809
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 ...
 692-749 4.99e-08

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.14  E-value: 4.99e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 692 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 749
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 ...
 485-551 2.56e-05

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 44.31  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462601166 485 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 551
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 7-35 6.94e-03

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 37.68  E-value: 6.94e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462601166   7 GFIQLNEDFIFIEPL-NDTMAITGHPHRVY 35
Cdd:pfam01562  99 GFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 87-304 1.37e-82

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: 265.64  E-value: 1.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  87 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQ 166
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 167 HEEfGKKNDihlemstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEM 246
Cdd:cd04273    81 KKL-NPPND----------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 247 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 304
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 ...
 553-673 6.34e-29

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: 111.90  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 553 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLgnlcyrhredpTLR-DAGKQSINSDWKIE-HSGAFNLAGTT 630
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL-----------AVKnVQGKYILNGKGSISlNPTYPSLLGTV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462601166 631 VHYVRR-GLWEKISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 673
Cdd:pfam05986  70 LEYRRSlPALEELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 89-305 2.93e-26

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: 107.00  E-value: 2.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  89 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLGVQVNLRVIKL------ILLHETPpelyighhgEKMLE 160
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 161 SFCKWQHEEFGKKNDiHlemstnwgedmtsvDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN--- 237
Cdd:pfam01421  72 NFLKWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNles 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 238 LAFTIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASNCLLQ 305
Cdd:pfam01421 131 FAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 321-388 3.90e-21

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.79  E-value: 3.90e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 321 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 388
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 864-916 1.27e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.24  E-value: 1.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462601166 864 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 916
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 399-448 3.56e-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: 56.44  E-value: 3.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462601166  399 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 448
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-855 5.29e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.84  E-value: 5.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462601166 813 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 855
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
399-447 1.13e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 1.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462601166 399 GEWSLWSPCSRTCSAGISSRERKCPGLDSEARDCNGPRKQYRICENPPC 447
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 753-809 1.76e-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: 1.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 753 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 809
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSI---VPDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 692-749 4.99e-08

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.14  E-value: 4.99e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 692 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 749
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 756-809 1.65e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.96  E-value: 1.65e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166  756 TEWTPCSRTCGKGMQSRQVACTQQLSngtliRARERDCIGPKPaSAQRCEGQDC 809
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 ...
 485-551 2.56e-05

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 44.31  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462601166 485 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 551
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 863-916 3.12e-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: 3.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166  863 VWRMGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 916
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 812-857 1.78e-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: 40.26  E-value: 1.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462601166  812 VWEAGVWSECSVKCGKGIRHRTVRCTNPRKKCV---LSTRPREAEDCED 857
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 826-910 1.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 826 GKGIRHRTVR----CTNPRKKCVLST-----------RPREAEDC---EDYSKCYVWrmGDWSKCSITCGKGMQSRVIQC 887
Cdd:PTZ00441  187 GQGINHQFNRllagCRPREGKCKFYSdadweeaknliKPFIAKVCtevERTASCGPW--DEWTPCSVTCGKGTHSRSRPI 264

                          90       100
                  ....*....|....*....|....
gi 2462601166 888 MH-KITGRHGNECFSSEKPAAYRP 910
Cdd:PTZ00441  265 LHeGCTTHMVEECEEEECPVEPEP 288
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 692-749 3.45e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.41  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462601166  692 WTHTS-WEDCDATCGGGERKTTVSCtkimsknISIVDNEKCKYLTKPEPQIRKCNEQPC 749
Cdd:smart00209   1 WSEWSeWSPCSVTCGGGVQTRTRSC-------CSPPPQNGGGPCTGEDVETRACNEQPC 52
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 7-35 6.94e-03

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: 37.68  E-value: 6.94e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462601166   7 GFIQLNEDFIFIEPL-NDTMAITGHPHRVY 35
Cdd:pfam01562  99 GFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 87-304 1.37e-82

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: 265.64  E-value: 1.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  87 YNIETVVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQ 166
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 167 HEEfGKKNDihlemstnwgEDMTSVDAAILITRKDFCvHKDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNLAFTIAHEM 246
Cdd:cd04273    81 KKL-NPPND----------SDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 247 GHNMGINHDNDHPSCAD---GLHIMSGEWikGQNLGDVSWSRCSKEDLERFLRSKASNCLL 304
Cdd:cd04273   149 GHVLGMPHDGDGNSCGPegkDGHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 88-304 2.56e-31

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: 121.57  E-value: 2.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  88 NIETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQhkslgvQVNLRVIkLILLhetppELY-------IGHHGEKM 158
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSNlsKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGL-----EIWtdkdkisVSGDAGET 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 159 LESFCKWqheefgKKNDIHLEMStnwgedmtsVDAAILITRKDFCVHkdepcdTVGIAYLSGMCSEKRKCIIAED---NG 235
Cdd:cd04269    70 LNRFLDW------KRSNLLPRKP---------HDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNL 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 236 LNLAFTIAHEMGHNMGINHDNDHPSCADGLHIMSgewikgQNLGDVS--WSRCSKEDLERFLRSKASNCLL 304
Cdd:cd04269   129 LLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIMA------PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 553-673 6.34e-29

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: 111.90  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 553 IIKGDFNHTRGAGYVEVLVIPAGARRIKVVEEKPAHSYLgnlcyrhredpTLR-DAGKQSINSDWKIE-HSGAFNLAGTT 630
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL-----------AVKnVQGKYILNGKGSISlNPTYPSLLGTV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462601166 631 VHYVRR-GLWEKISAKGPTTAPLHLLVL--LFQDQNYGLHYEYTIP 673
Cdd:pfam05986  70 LEYRRSlPALEELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 89-305 2.93e-26

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: 107.00  E-value: 2.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  89 IETVVVADPAMVSYHGAD--AARRFILTILNMVfNLFqHKSLGVQVNLRVIKL------ILLHETPpelyighhgEKMLE 160
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDttVVRQRVFQVVNLV-NSI-YKELNIRVVLVGLEIwtdedkIDVSGDA---------NDTLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 161 SFCKWQHEEFGKKNDiHlemstnwgedmtsvDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN--- 237
Cdd:pfam01421  72 NFLKWRQEYLKKRKP-H--------------DVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNles 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601166 238 LAFTIAHEMGHNMGINHDNDHPSC---ADGLHIMSGEWIKgqnLGDVSWSRCSKEDLERFLRSKASNCLLQ 305
Cdd:pfam01421 131 FAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 89-296 5.21e-23

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: 97.49  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  89 IETVVVADPAMVSYHGAD--AARRFILTILNMVFNLFQHKSLGVQVNLRVIKLILLHETPPELYIGHHGEKMLESFCKWQ 166
Cdd:cd04267     3 IELVVVADHRMVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 167 HEEFGKkndihlemstnwgedmtsVDAAILITRKDFcvhkdEPCDTVGIAYLSGMCSEKRKCIIAEDNGLNL--AFTIAH 244
Cdd:cd04267    83 AEGPIR------------------HDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAH 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462601166 245 EMGHNMGINHDND----HPSCADGLHIMSgewIKGQNLGDVSWSRCSKEDLERFLR 296
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 ...
 321-388 3.90e-21

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 87.79  E-value: 3.90e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 321 PGMTYTADEQCQILFGPLASFCQEMQHVICTGLWCKVEGEKECRTKLDPPMDGTDCDLGKWCKAGECT 388
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 168-295 2.61e-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: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 168 EEFGKKNDIHLEMStNWGEDmtSVDAAILITRKDFcvhkdePCDTVGIAYLSGMCSEKRKCIIAEDNGLN---LAFTIAH 244
Cdd:cd00203    32 QIWRDYLNIRFVLV-GVEID--KADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAH 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462601166 245 EMGHNMGINHDND--------------HPSCADGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFL 295
Cdd:cd00203   103 ELGHALGFYHDHDrkdrddyptiddtlNAEDDDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 864-916 1.27e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 63.24  E-value: 1.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462601166 864 WRMGDWSKCSITCGKGMQSRVIQCMHKITGR--HGNECFSSEKPAAYRPCHLQPC 916
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 132-303 1.58e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 67.76  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 132 VNLRVIKLILLHETPPELYIGHHG------EKMLESFckwqhEEFGKKNDiHLEMStnwgedmtsvDAAILITRKDFCVH 205
Cdd:cd04272    46 IRLLLVGITISKDPDFEPYIHPINygyidaAETLENF-----NEYVKKKR-DYFNP----------DVVFLVTGLDMSTY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 206 KDEPCDTV--GIAYLSGMCSEKRKCIIaEDNG--LNLAFTIAHEMGHNMGINHDND--------HPSCA-----DGlHIM 268
Cdd:cd04272   110 SGGSLQTGtgGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHLLGAPHDGSpppswvkgHPGSLdcpwdDG-YIM 187

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462601166 269 SgewikgQNLGDVS---WSRCSKEDLERFLRSKASNCL 303
Cdd:cd04272   188 S------YVVNGERqyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
92-269 8.69e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 65.13  E-value: 8.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166  92 VVVADPAMVSYHGADAARRFILTILNMVFNLFQHKSlgvQVNLRVIKLILLHETPPELYIGHH---GEKMLESFcKWQHE 168
Cdd:pfam13688   8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACStgdSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 169 EFGKKNDihlemstnwgedmtsvDAAILITrkdfcvhkDEPCDTVGIAYLSGMCSEKRKCIIAEDNGLN--------LAF 240
Cdd:pfam13688  84 WRGTQND----------------DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQ 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462601166 241 TIAHEMGHNMGINHDND----HPSC--------ADGLHIMS 269
Cdd:pfam13688 140 VFAHEIGHNFGAVHDCDsstsSQCCppsnstcpAGGRYIMN 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 399-448 3.56e-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: 56.44  E-value: 3.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462601166  399 GEWSLWSPCSRTCSAGISSRERKC--PGLDSEARDCNGPRKQYRICENPPCP 448
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-855 5.29e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.84  E-value: 5.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462601166 813 WEAGVWSECSVKCGKGIRHRTVRC-------TNPRKKCVLSTRPREAEDC 855
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsIVPDSECSAQKKPPETQSC 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
399-447 1.13e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 1.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462601166 399 GEWSLWSPCSRTCSAGISSRERKCPGLDSEARDCNGPRKQYRICENPPC 447
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 753-809 1.76e-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: 1.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 753 WMMTEWTPCSRTCGKGMQSRQVACTQQLSNGTlirARERDC-IGPKPASAQRCEGQDC 809
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSI---VPDSECsAQKKPPETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 241-302 2.91e-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: 2.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462601166 241 TIAHEMGHNMGINHDNDHPSCA-----DGLHIMSGEWIKGQNLGDVSWSRCSKEDLERFLRSKASNC 302
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 692-749 4.99e-08

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.14  E-value: 4.99e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601166 692 WTHTSWEDCDATCGGGERKTTVSCTKIMSKniSIVDNEKCKYLTKPePQIRKCNEQPC 749
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG--SIVPDSECSAQKKP-PETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 112-255 8.21e-08

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 51.60  E-value: 8.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 112 ILTILNMVFNLFQHKsLGVQVNLRVIKLILLHETPpelYIGHHGEKMLESFCKWQHEEFGKKNdihlemstnwgedmtsV 191
Cdd:pfam13582   3 IVSLVNRANTIYERD-LGIRLQLAAIIITTSADTP---YTSSDALEILDELQEVNDTRIGQYG----------------Y 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462601166 192 DAAILITRKDFCvhkdepcDTVGIAYLSGMCSEKRKCIIAED---NGLNLAFTIAHEMGHNMGINHD 255
Cdd:pfam13582  63 DLGHLFTGRDGG-------GGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 756-809 1.65e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.96  E-value: 1.65e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166  756 TEWTPCSRTCGKGMQSRQVACTQQLSngtliRARERDCIGPKPaSAQRCEGQDC 809
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 ...
 485-551 2.56e-05

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 44.31  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462601166 485 CALFCSPVGKEQPILLSEKVMDGTSCGYQG------LDICANGRCQKVGCDGLLGSLAREDHCGVCNGNGKSC 551
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredgtLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 863-916 3.12e-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: 3.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166  863 VWRMGDWSKCSITCGKGMQSRVIQCMHKITGRHGNECfsSEKPAAYRPCHLQPC 916
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC--TGEDVETRACNEQPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 212-288 3.94e-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: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 212 TVGIAYLSGMCSEKRKCIiAEDNGLNLAFT-------------IAHEMGHNMGINHDND-----HPSC----------AD 263
Cdd:pfam13574  86 ELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsqyaSSGCernaatsvcsAN 164

                          90       100
                  ....*....|....*....|....*
gi 2462601166 264 GLHIMSGEWIKGQNLgdvsWSRCSK 288
Cdd:pfam13574 165 GSFIMNPASKSNNDL----FSPCSI 185
TSP_1 pfam00090
Thrombospondin type 1 domain;
756-809 4.48e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.63  E-value: 4.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166 756 TEWTPCSRTCGKGMQSRQVACTQQLSNGTlirarerDCIGPKpASAQRCEGQDC 809
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 ...
 399-436 8.44e-05

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.11  E-value: 8.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462601166 399 GEWSLWSPCSRTCSAGISSRERK-----------CPGLdSEARDCNGPR 436
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTvivepqnggrpCPEL-LERRPCNLPP 51
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 404-447 1.61e-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: 40.01  E-value: 1.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462601166 404 WSPCSRTCSAGISSRERkcpgldSEARDCNgPRKQYRICENPPC 447
Cdd:pfam19035   8 WSPCSKTCGMGVSTRVS------NDNAECK-LVTETRLCQLRPC 44
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 756-809 1.75e-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: 39.96  E-value: 1.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462601166 756 TEWTPCSRTCGKGMQSRQVACTQQLSNGtlirarERDCigPKPASAQRCEGQDC 809
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRTRTVIVEPQNG------GRPC--PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 812-857 1.78e-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: 40.26  E-value: 1.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462601166  812 VWEAGVWSECSVKCGKGIRHRTVRCTNPRKKCV---LSTRPREAEDCED 857
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpCTGEDVETRACNE 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 826-910 1.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601166 826 GKGIRHRTVR----CTNPRKKCVLST-----------RPREAEDC---EDYSKCYVWrmGDWSKCSITCGKGMQSRVIQC 887
Cdd:PTZ00441  187 GQGINHQFNRllagCRPREGKCKFYSdadweeaknliKPFIAKVCtevERTASCGPW--DEWTPCSVTCGKGTHSRSRPI 264

                          90       100
                  ....*....|....*....|....
gi 2462601166 888 MH-KITGRHGNECFSSEKPAAYRP 910
Cdd:PTZ00441  265 LHeGCTTHMVEECEEEECPVEPEP 288
TSP_1 pfam00090
Thrombospondin type 1 domain;
867-916 6.98e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.17  E-value: 6.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462601166 867 GDWSKCSITCGKGMQSRVIQCMHKITGrhGNECfsSEKPAAYRPCHLQPC 916
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPC--TGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 692-749 3.45e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.41  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462601166  692 WTHTS-WEDCDATCGGGERKTTVSCtkimsknISIVDNEKCKYLTKPEPQIRKCNEQPC 749
Cdd:smart00209   1 WSEWSeWSPCSVTCGGGVQTRTRSC-------CSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
818-852 4.19e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 4.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462601166 818 WSECSVKCGKGIRHRTVRCTNPRKK---CVLSTRPREA 852
Cdd:pfam00090   6 WSPCSVTCGKGIQVRQRTCKSPFPGgepCTGDDIETQA 43
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 7-35 6.94e-03

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: 37.68  E-value: 6.94e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462601166   7 GFIQLNEDFIFIEPL-NDTMAITGHPHRVY 35
Cdd:pfam01562  99 GFIRTENEEYLIEPLeKYSREEGGHPHVVY 128
 
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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