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Conserved domains on  [gi|2024508823|ref|XP_040530684|]
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A disintegrin and metalloproteinase with thrombospondin motifs 14 isoform X1 [Gallus gallus]

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) ...
 239-440 1.09e-96

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: 306.09  E-value: 1.09e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  239 YNIEVLLAVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIVLVRMIMVGYRQSVSLIeRGNPSRSLEQVCRW 318
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  319 AHAQQRSDPDHAEHHDHAVFLTRQDF----GPAGMQGYAPVTGMCHPLRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 394
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024508823  395 GNRCADETSMGSIMAPLVQAAFHRYHWSRCSKQELNRYIHSY--DCLL 440
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 71-193 3.86e-32

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: 121.65  E-value: 3.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823   71 PARRRRGAHHASSQHGagsrPIYFNVTVLGRELHLRLRPNTGLVPPRAVAEW-QEDFGLRLRQP-LQHHCLFTGDITGVP 148
Cdd:pfam01562   10 PSRRRRSLASESTYLD----TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPvQTDHCYYQGHVEGHP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024508823  149 GGAVAISNCDGLAGLIRTDSGEFFIEPLERGQQDTEarGRAHVVY 193
Cdd:pfam01562   86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG--GHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 455-524 6.75e-22

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: 90.10  E-value: 6.75e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  455 PGINYSMDEQCRFDFGVGYKTCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECSLGKWCFKGHCI 524
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
ADAMTS_spacer1 super family cl20316
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 698-812 1.96e-20

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.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 87.63  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  698 TVKGTLakTPKQPGSVLKMFEIPAGARHVQIEEMEPASHSIAVKNqATGNFILNAKGQ-ETTSKTFIEMGLEWEYTV-EQ 775
Cdd:pfam05986    1 TVSGSF--TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLP 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024508823  776 GKESLKTSGPLHEAISVLLVAR-EEAVRSSLMYRYIIH 812
Cdd:pfam05986   78 ALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 538-590 4.23e-17

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: 76.09  E-value: 4.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024508823   538 WSSWSKFGSCSRTCGGGVRSRSRSCSNPPPAYGGRNCPGATYEHQVCNSEECP 590
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 894-951 1.34e-11

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 60.54  E-value: 1.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024508823  894 WVAEEWSACSKSCGKlGLQVRAVQCVQRlrdGTNRTLHAKYCS-AERPETRRPCSRLPC 951
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK---GGGSIVPDSECSaQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-889 2.67e-10

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 56.69  E-value: 2.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024508823  834 WALKSWSQCSKACGGGIQYTKYGCRRRSDNRMVHRNLCDNGKKPkPIRRRCNLQEC 889
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 595-696 7.61e-09

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: 54.71  E-value: 7.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  595 DFRAQQCSKRDSYYTHRD----SKHAW---LPYEHPDDAqkCELICQSEGTGDVVFMNQVVHDGTRCSYRDP-----YSI 662
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024508823  663 CVRGECVHVGCDKEVGSLKQEDKCGVCGGDNSHC 696
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1003 2.14e-07

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: 48.60  E-value: 2.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024508823  955 WRTGAWSQCSASCGDGVQQRQVVCR-----GEESGGRC-HGDKPEAIRGCHVAVC 1003
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggSIVPDSECsAQKKPPETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-440 1.09e-96

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: 306.09  E-value: 1.09e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  239 YNIEVLLAVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIVLVRMIMVGYRQSVSLIeRGNPSRSLEQVCRW 318
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  319 AHAQQRSDPDHAEHHDHAVFLTRQDF----GPAGMQGYAPVTGMCHPLRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 394
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024508823  395 GNRCADETSMGSIMAPLVQAAFHRYHWSRCSKQELNRYIHSY--DCLL 440
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 71-193 3.86e-32

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: 121.65  E-value: 3.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823   71 PARRRRGAHHASSQHGagsrPIYFNVTVLGRELHLRLRPNTGLVPPRAVAEW-QEDFGLRLRQP-LQHHCLFTGDITGVP 148
Cdd:pfam01562   10 PSRRRRSLASESTYLD----TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPvQTDHCYYQGHVEGHP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024508823  149 GGAVAISNCDGLAGLIRTDSGEFFIEPLERGQQDTEarGRAHVVY 193
Cdd:pfam01562   86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG--GHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 241-443 1.89e-24

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 101.99  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  241 IEVLLAVDDSVVRFHGK--EHVQNYVLTLMNIVDEIYHdeslGVHINIVLVRM--IMVGYRQSVSlierGNPSRSLEQVC 316
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeiWTDEDKIDVS----GDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  317 RWAHAQ--QRSDpdhaehHDHAVFLTRQDFGpAGMQGYAPVTGMCHPLRSCTLN---HEDGFSSAFVVAHETGHVLGMEH 391
Cdd:pfam01421   75 KWRQEYlkKRKP------HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQH 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024508823  392 DGQGNRCADETSMGSIMAPLVQAAFHRyHWSRCSKQELNRYIHSYD--CLLDDP 443
Cdd:pfam01421  148 DDFNGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 455-524 6.75e-22

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: 90.10  E-value: 6.75e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  455 PGINYSMDEQCRFDFGVGYKTCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECSLGKWCFKGHCI 524
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 698-812 1.96e-20

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: 87.63  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  698 TVKGTLakTPKQPGSVLKMFEIPAGARHVQIEEMEPASHSIAVKNqATGNFILNAKGQ-ETTSKTFIEMGLEWEYTV-EQ 775
Cdd:pfam05986    1 TVSGSF--TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLP 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024508823  776 GKESLKTSGPLHEAISVLLVAR-EEAVRSSLMYRYIIH 812
Cdd:pfam05986   78 ALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 538-590 4.23e-17

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: 76.09  E-value: 4.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024508823   538 WSSWSKFGSCSRTCGGGVRSRSRSCSNPPPAYGGRNCPGATYEHQVCNSEECP 590
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 894-951 1.34e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 60.54  E-value: 1.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024508823  894 WVAEEWSACSKSCGKlGLQVRAVQCVQRlrdGTNRTLHAKYCS-AERPETRRPCSRLPC 951
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK---GGGSIVPDSECSaQKKPPETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 539-589 1.18e-10

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: 57.67  E-value: 1.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024508823  539 SSWSKFGSCSRTCGGGVRSRSRSCSNpPPAYGGRNCPgATYEHQVCNSEEC 589
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPCP-ELLERRPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-889 2.67e-10

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 56.69  E-value: 2.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024508823  834 WALKSWSQCSKACGGGIQYTKYGCRRRSDNRMVHRNLCDNGKKPkPIRRRCNLQEC 889
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 595-696 7.61e-09

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: 54.71  E-value: 7.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  595 DFRAQQCSKRDSYYTHRD----SKHAW---LPYEHPDDAqkCELICQSEGTGDVVFMNQVVHDGTRCSYRDP-----YSI 662
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024508823  663 CVRGECVHVGCDKEVGSLKQEDKCGVCGGDNSHC 696
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1003 2.14e-07

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: 48.60  E-value: 2.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024508823  955 WRTGAWSQCSASCGDGVQQRQVVCR-----GEESGGRC-HGDKPEAIRGCHVAVC 1003
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggSIVPDSECsAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 955-1003 5.81e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.50  E-value: 5.81e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2024508823   955 WRTGAWSQCSASCGDGVQQRQVVC---RGEESGGRCHGDKPEaIRGCHVAVC 1003
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCcspPPQNGGGPCTGEDVE-TRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 897-952 9.46e-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: 41.03  E-value: 9.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024508823   897 EEWSACSKSCGKlGLQVRAVQCVQRlrdgtNRTLHAKYCSAERPETrRPCSRLPCP 952
Cdd:smart00209    5 SEWSPCSVTCGG-GVQTRTRSCCSP-----PPQNGGGPCTGEDVET-RACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 838-890 3.18e-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: 36.80  E-value: 3.18e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024508823   838 SWSQCSKACGGGIQYtkygcRRRSDNRMVHRNLCDNGKKPKPIRRRCNLQECS 890
Cdd:smart00209    6 EWSPCSVTCGGGVQT-----RTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-440 1.09e-96

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: 306.09  E-value: 1.09e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  239 YNIEVLLAVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIVLVRMIMVGYRQSVSLIeRGNPSRSLEQVCRW 318
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  319 AHAQQRSDPDHAEHHDHAVFLTRQDF----GPAGMQGYAPVTGMCHPLRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQ 394
Cdd:cd04273     80 QKKLNPPNDSDPEHHDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024508823  395 GNRCADETSMGSIMAPLVQAAFHRYHWSRCSKQELNRYIHSY--DCLL 440
Cdd:cd04273    160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 71-193 3.86e-32

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: 121.65  E-value: 3.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823   71 PARRRRGAHHASSQHGagsrPIYFNVTVLGRELHLRLRPNTGLVPPRAVAEW-QEDFGLRLRQP-LQHHCLFTGDITGVP 148
Cdd:pfam01562   10 PSRRRRSLASESTYLD----TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPvQTDHCYYQGHVEGHP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024508823  149 GGAVAISNCDGLAGLIRTDSGEFFIEPLERGQQDTEarGRAHVVY 193
Cdd:pfam01562   86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG--GHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 240-441 8.73e-30

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: 117.33  E-value: 8.73e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  240 NIEVLLAVDDSVVRFHGK--EHVQNYVLTLMNIVDEIYHDeslgVHINIVLVRMIMVGYRQSVSLieRGNPSRSLEQVCR 317
Cdd:cd04269      2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  318 WahaqQRSDPDHAEHHDHAVFLTRQDFGPaGMQGYAPVTGMCHPLRSCTLNHEDG---FSSAFVVAHETGHVLGMEHDGQ 394
Cdd:cd04269     76 W----KRSNLLPRKPHDNAQLLTGRDFDG-NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDG 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2024508823  395 GNRCADETsmgSIMAPlvQAAFHRYHWSRCSKQELNRYIHSYD--CLLD 441
Cdd:cd04269    151 GCTCGRST---CIMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 241-433 1.17e-29

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: 116.75  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  241 IEVLLAVDDSVVR-FHGKE-HVQNYVLTLMNIVDEIYHDESLGVHINIVLVRMIMVGYRQSVSLIErGNPSRSLEQVCRW 318
Cdd:cd04267      3 IELVVVADHRMVSyFNSDEnILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPID-SDASNTLNSFSFW 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  319 ahaqQRSDPdhaEHHDHAVFLTRQDFGPAGMQGYAPVTGMCHPLRSCTL--NHEDGFSSAFVVAHETGHVLGMEHDGQGN 396
Cdd:cd04267     82 ----RAEGP---IRHDNAVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGGDE 154

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2024508823  397 RCADETSMGS-IMAPlVQAAFHRYHWSRCSKQELNRYI 433
Cdd:cd04267    155 LAFECDGGGNyIMAP-VDSGLNSYRFSQCSIGSIREFL 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 241-443 1.89e-24

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 101.99  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  241 IEVLLAVDDSVVRFHGK--EHVQNYVLTLMNIVDEIYHdeslGVHINIVLVRM--IMVGYRQSVSlierGNPSRSLEQVC 316
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeiWTDEDKIDVS----GDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  317 RWAHAQ--QRSDpdhaehHDHAVFLTRQDFGpAGMQGYAPVTGMCHPLRSCTLN---HEDGFSSAFVVAHETGHVLGMEH 391
Cdd:pfam01421   75 KWRQEYlkKRKP------HDVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQH 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024508823  392 DGQGNRCADETSMGSIMAPLVQAAFHRyHWSRCSKQELNRYIHSYD--CLLDDP 443
Cdd:pfam01421  148 DDFNGGCKCPPGGGCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 455-524 6.75e-22

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: 90.10  E-value: 6.75e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  455 PGINYSMDEQCRFDFGVGYKTCTAFrTFDPCKQLWCSHPDNPYfCKTKKGPPLDGTECSLGKWCFKGHCI 524
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 698-812 1.96e-20

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: 87.63  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  698 TVKGTLakTPKQPGSVLKMFEIPAGARHVQIEEMEPASHSIAVKNqATGNFILNAKGQ-ETTSKTFIEMGLEWEYTV-EQ 775
Cdd:pfam05986    1 TVSGSF--TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLP 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024508823  776 GKESLKTSGPLHEAISVLLVAR-EEAVRSSLMYRYIIH 812
Cdd:pfam05986   78 ALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 538-590 4.23e-17

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: 76.09  E-value: 4.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024508823   538 WSSWSKFGSCSRTCGGGVRSRSRSCSNPPPAYGGRNCPGATYEHQVCNSEECP 590
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 241-433 9.35e-14

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 70.24  E-value: 9.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  241 IEVLLAVDDsvvRFHGKEHVQNYVLTLMNIVDEIYHDEsLGVHINIVLVRMImvgyrqsvsliergnpsrsleqvcrwah 320
Cdd:cd00203      3 IPYVVVADD---RDVEEENLSAQIQSLILIAMQIWRDY-LNIRFVLVGVEID---------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  321 aqqrsdpdhaeHHDHAVFLTRQDFgPAGMQGYAPVTGMCHPLRSCTL---NHEDGFSSAFVVAHETGHVLGMEHDGQGNR 397
Cdd:cd00203     51 -----------KADIAILVTRQDF-DGGTGGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDRKD 118

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2024508823  398 CADE-----------TSMGSIMAPLVQAAFH--RYHWSRCSKQELNRYI 433
Cdd:cd00203    119 RDDYptiddtlnaedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 894-951 1.34e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 60.54  E-value: 1.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024508823  894 WVAEEWSACSKSCGKlGLQVRAVQCVQRlrdGTNRTLHAKYCS-AERPETRRPCSRLPC 951
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQK---GGGSIVPDSECSaQKKPPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
243-410 2.30e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 63.98  E-value: 2.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  243 VLLAVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESlgvHINIVLVRMIMVGYRQSVSLIERGNPSRSLeqvcRWAHAQ 322
Cdd:pfam13688    7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDSSD----RLSEFQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  323 QRSDPDHAEHHDHAVFLTRQDFGPAGMqgyAPVTGMCHPL--RSCTLNHEDGF------SSAFVVAHETGHVLGMEHDGQ 394
Cdd:pfam13688   80 DFSAWRGTQNDDLAYLFLMTNCSGGGL---AWLGQLCNSGsaGSVSTRVSGNNvvvstaTEWQVFAHEIGHNFGAVHDCD 156

                          170       180
                   ....*....|....*....|....*
gi 2024508823  395 GNRCADETSMGS---------IMAP 410
Cdd:pfam13688  157 SSTSSQCCPPSNstcpaggryIMNP 181
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 539-589 1.18e-10

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: 57.67  E-value: 1.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024508823  539 SSWSKFGSCSRTCGGGVRSRSRSCSNpPPAYGGRNCPgATYEHQVCNSEEC 589
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPCP-ELLERRPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-889 2.67e-10

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 56.69  E-value: 2.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024508823  834 WALKSWSQCSKACGGGIQYTKYGCRRRSDNRMVHRNLCDNGKKPkPIRRRCNLQEC 889
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 240-439 9.75e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 60.06  E-value: 9.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  240 NIEVLLAVDDSVVRFHGK-EHVQNYVLTLMNIVDEIYHDESlGVHINIVLVRMIMVGYRQSVSLIERGNP-----SRSLE 313
Cdd:cd04272      2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYgyidaAETLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  314 QVCrwAHAQQRSDPdhaEHHDHAVFLTRQDF-----GPA--GMQGYAPVTGMCHPLRSCTLnhED---GFSSAFVVAHET 383
Cdd:cd04272     81 NFN--EYVKKKRDY---FNPDVVFLVTGLDMstysgGSLqtGTGGYAYVGGACTENRVAMG--EDtpgSYYGVYTMTHEL 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024508823  384 GHVLGMEHDGQ---GNRCADETSM------GSIMAPLVQAAFHrYHWSRCSKQELNRYIHSYD--CL 439
Cdd:cd04272    154 AHLLGAPHDGSpppSWVKGHPGSLdcpwddGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGasCL 219
TSP_1 pfam00090
Thrombospondin type 1 domain;
538-589 4.65e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.19  E-value: 4.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024508823  538 WSSWSkfgSCSRTCGGGVRSRSRSCSNPPPayGGRNCPGATYEHQVCNSEEC 589
Cdd:pfam00090    3 WSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 595-696 7.61e-09

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: 54.71  E-value: 7.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  595 DFRAQQCSKRDSYYTHRD----SKHAW---LPYEHPDDAqkCELICQSEGTGDVVFMNQVVHDGTRCSYRDP-----YSI 662
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgtLSL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024508823  663 CVRGECVHVGCDKEVGSLKQEDKCGVCGGDNSHC 696
Cdd:pfam19236   82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 955-1003 2.14e-07

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: 48.60  E-value: 2.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024508823  955 WRTGAWSQCSASCGDGVQQRQVVCR-----GEESGGRC-HGDKPEAIRGCHVAVC 1003
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgggSIVPDSECsAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 955-1003 5.81e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.50  E-value: 5.81e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2024508823   955 WRTGAWSQCSASCGDGVQQRQVVC---RGEESGGRCHGDKPEaIRGCHVAVC 1003
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCcspPPQNGGGPCTGEDVE-TRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
957-1003 5.83e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.63  E-value: 5.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2024508823  957 TGAWSQCSASCGDGVQQRQVVCRGEESGG-RCHGDKpEAIRGCHVAVC 1003
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGePCTGDD-IETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 897-952 9.46e-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: 41.03  E-value: 9.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024508823   897 EEWSACSKSCGKlGLQVRAVQCVQRlrdgtNRTLHAKYCSAERPETrRPCSRLPCP 952
Cdd:smart00209    5 SEWSPCSVTCGG-GVQTRTRSCCSP-----PPQNGGGPCTGEDVET-RACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 543-589 9.51e-05

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: 41.28  E-value: 9.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024508823  543 KFGSCSRTCGGGVRSRSRSCSNP--PPAYGGRNCPGAT--YEHQVCNSEEC 589
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKggGSIVPDSECSAQKkpPETQSCNLKPC 55
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-410 9.29e-04

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 41.84  E-value: 9.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  243 VLLAVDDSVVRFHG-KEHVQNYVLTLMNIVDEIYhDESLGVHINIVLVRMIMVGYRQSVSLiergNPSRSLEQVCRWAHA 321
Cdd:pfam13583    7 VAVATDCTYSASFGsVDELRANINATVTTANEVY-GRDFNVSLALISDRDVIYTDSSTDSF----NADCSGGDLGNWRLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  322 QQRSDPDHAEhhDHAVFLTRQDFGPAGMQGYAPVTGMCHPLRSctlNHE-DGFSSAF----VVAHETGHVLGMEHD---- 392
Cdd:pfam13583   82 TLTSWRDSLN--YDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKaSGVARSRdewdIFAHEIGHTFGAVHDcssq 156

                          170
                   ....*....|....*....
gi 2024508823  393 GQGNRCADETSMG-SIMAP 410
Cdd:pfam13583  157 GEGLSSSTEDGSGqTIMSY 175
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 838-890 3.18e-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: 36.80  E-value: 3.18e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024508823   838 SWSQCSKACGGGIQYtkygcRRRSDNRMVHRNLCDNGKKPKPIRRRCNLQECS 890
Cdd:smart00209    6 EWSPCSVTCGGGVQT-----RTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 833-889 3.72e-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: 36.49  E-value: 3.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024508823  833 EWAlkSWSQCSKACGGGIQYtkygcrrRSdnRMVHRNlCDNGKKPKPI---RRRCNLQEC 889
Cdd:pfam19028    5 EWS--EWSECSVTCGGGVQT-------RT--RTVIVE-PQNGGRPCPElleRRPCNLPPC 52
 
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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