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Conserved domains on  [gi|1940128051|ref|NP_942056|]
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A disintegrin and metalloproteinase with thrombospondin motifs 5 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-470 6.45e-100

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: 310.71  E-value: 6.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTD--KSLEVSKNAATTLKNFCKWQHQ 344
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDeeSGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 345 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 422
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1940128051 423 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 470
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 730-849 9.44e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 122.69  E-value: 9.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 730 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 808
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1940128051 809 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 849
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 484-551 1.85e-23

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: 94.33  E-value: 1.85e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 484 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 551
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 61-181 1.85e-16

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: 76.58  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051  61 HPQ--PLARQRRSSG-LVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGGIVTA-----GGLSASSGHRGHCF 132
Cdd:pfam01562   4 IPVrlDPSRRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051 133 YRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAESER---VY 181
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 567-619 1.52e-15

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: 71.46  E-value: 1.52e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1940128051  567 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVIPCP 619
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-927 1.28e-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: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940128051 876 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCILSQRPSAFKQCLLKKC 927
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 625-728 2.00e-12

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: 64.73  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 625 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 694
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1940128051 695 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 728
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-470 6.45e-100

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: 310.71  E-value: 6.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTD--KSLEVSKNAATTLKNFCKWQHQ 344
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDeeSGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 345 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 422
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1940128051 423 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 470
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 730-849 9.44e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 122.69  E-value: 9.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 730 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 808
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1940128051 809 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 849
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 268-473 1.78e-27

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


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 110.47  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLTDKS-LEVSKNAATTLKNFCKWQH 343
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDkIDVSGDANDTLRNFLKWRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 344 QHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDDS 420
Cdd:pfam01421  79 EYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDDF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128051 421 K---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDVP 473
Cdd:pfam01421 151 NggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 484-551 1.85e-23

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: 94.33  E-value: 1.85e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 484 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 551
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 61-181 1.85e-16

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: 76.58  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051  61 HPQ--PLARQRRSSG-LVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGGIVTA-----GGLSASSGHRGHCF 132
Cdd:pfam01562   4 IPVrlDPSRRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051 133 YRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAESER---VY 181
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 567-619 1.52e-15

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: 71.46  E-value: 1.52e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1940128051  567 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVIPCP 619
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-927 1.28e-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: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940128051 876 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCILSQRPSAFKQCLLKKC 927
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 625-728 2.00e-12

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: 64.73  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 625 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 694
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1940128051 695 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 728
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
570-618 7.00e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 7.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1940128051 570 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVIPC 618
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 267-445 1.35e-05

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 48.62  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 267 QVELLLVADSSMAKMYGR-GLQHYLLTLASIANRLYSHASIEnhIRLAVVKVVVLTDKSleVSKNAATTLKNFCKWQHQH 345
Cdd:NF038115   20 TIDVNFVVDQAIVESQGReALDKQIEAAISLSNETYLSAGTD--LHFNVRQVVVESDNS--VDATCTSGLGGALDGLLAS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 346 NQLgdDHEEHYDAAILFTREDlcgHHSC------DTLGMA-------DVGTICSPERSCA---------------VIEDD 397
Cdd:NF038115   96 GQI--ACRDAYDEAFNHMDNV---VWDCpspgdnDRVGNAgysygadFWVTIVSGSDGNAngvaqvgmdlqvkgyNVTLD 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128051 398 GLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 445
Cdd:NF038115  171 LYVATQTLAHELGHLFGLYNGhaESAECSEGgyrlmcgslaenfenlFGSSELQRFYNNADSTLDD 236
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 876-927 4.89e-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: 36.03  E-value: 4.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051  876 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCILSQRPSAFKQCLLKKC 927
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-470 6.45e-100

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: 310.71  E-value: 6.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTD--KSLEVSKNAATTLKNFCKWQHQ 344
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDeeSGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 345 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 422
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1940128051 423 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 470
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 268-462 5.31e-34

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: 129.08  E-value: 5.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGRG---LQHYLLTLASIANRLYSHASIENHIRLAVVKVVVL--TDKSLEVSKNAATTLKNFCKWQ 342
Cdd:cd04267     3 IELVVVADHRMVSYFNSDeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILkgEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 343 HQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEIGHLLGLSHDDS 420
Cdd:cd04267    83 AEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHDGG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1940128051 421 KFCEENFGStEDKRLMSSILTSIDaSKPWSKCTSATITEFLD 462
Cdd:cd04267   153 DELAFECDG-GGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 730-849 9.44e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 122.69  E-value: 9.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 730 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 808
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1940128051 809 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 849
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 268-471 9.84e-33

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 125.42  E-value: 9.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGRGL---QHYLLTLASIANRLYSHAsienHIRLAVVKVVVLTDKSL-EVSKNAATTLKNFCKWQH 343
Cdd:cd04269     3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPL----NIRVVLVGLEIWTDKDKiSVSGDAGETLNRFLDWKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 344 qhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDS 420
Cdd:cd04269    79 --SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHELGHNLGMEHDDG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051 421 K-FCEENFGstedkrLMSSILTSIdaSKPWSKCTSATITEFLDDGHGNCLLD 471
Cdd:cd04269   151 GcTCGRSTC------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 268-473 1.78e-27

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


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 110.47  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLTDKS-LEVSKNAATTLKNFCKWQH 343
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDkIDVSGDANDTLRNFLKWRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 344 QHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDDS 420
Cdd:pfam01421  79 EYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDDF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128051 421 K---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDVP 473
Cdd:pfam01421 151 NggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 484-551 1.85e-23

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: 94.33  E-value: 1.85e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 484 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 551
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 61-181 1.85e-16

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: 76.58  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051  61 HPQ--PLARQRRSSG-LVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGGIVTA-----GGLSASSGHRGHCF 132
Cdd:pfam01562   4 IPVrlDPSRRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051 133 YRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAESER---VY 181
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 567-619 1.52e-15

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: 71.46  E-value: 1.52e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1940128051  567 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVIPCP 619
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 268-461 3.13e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.85  E-value: 3.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGRGLQ--HYLLTLASIANRLYShaSIEN-HIRLAVVKVVVLTDKSLEV--------SKNAATTLK 336
Cdd:cd04272     3 PELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYR--DLKSpRIRLLLVGITISKDPDFEPyihpinygYIDAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 337 NFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLHaafTVAH 407
Cdd:cd04272    81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY---TMTH 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128051 408 EIGHLLGLSHDDS---KFCEENFGST----EDKRLMSSILTSIDASKpWSKCTSATITEFL 461
Cdd:cd04272   152 ELAHLLGAPHDGSpppSWVKGHPGSLdcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVF 211
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 268-461 3.87e-13

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 68.32  E-value: 3.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKmyGRGLQHYLLTLASIANRLYShasIENHIRLAVVKVVVltdkslevsknaattlknfckwqhqhnq 347
Cdd:cd00203     3 IPYVVVADDRDVE--EENLSAQIQSLILIAMQIWR---DYLNIRFVLVGVEI---------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 348 lgDDHeehyDAAILFTREDlcghHSCDTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDSKFCE 424
Cdd:cd00203    50 --DKA----DIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDR 119

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1940128051 425 ENFGSTEDKR---------LMSSILTSIDA--SKPWSKCTSATITEFL 461
Cdd:cd00203   120 DDYPTIDDTLnaedddyysVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-927 1.28e-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: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940128051 876 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCILSQRPSAFKQCLLKKC 927
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 625-728 2.00e-12

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: 64.73  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 625 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 694
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1940128051 695 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 728
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 310-418 2.75e-12

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: 64.31  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 310 IRLAVVKVVVLTD-KSLEVSKNAATTLKNFCKWQHQHNQLGDdheehYDAAILFTREDLCGhhscdTLGMADVGTICSPE 388
Cdd:pfam13582  20 IRLQLAAIIITTSaDTPYTSSDALEILDELQEVNDTRIGQYG-----YDLGHLFTGRDGGG-----GGGIAYVGGVCNSG 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1940128051 389 RSCAVIEDD---GLHAAFTVAHEIGHLLGLSHD 418
Cdd:pfam13582  90 SKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
267-418 7.55e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.44  E-value: 7.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 267 QVELLLVADSS-MAKMYGRGLQHYLLTLASIANRLYSHASienHIRLAVVKVVVLT-----DKSLEVSKNAATTLKNFC- 339
Cdd:pfam13688   4 TVALLVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDstcpyTPPACSTGDSSDRLSEFQd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 340 --KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHEI 409
Cdd:pfam13688  81 fsAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEI 145


                  ....*....
gi 1940128051 410 GHLLGLSHD 418
Cdd:pfam13688 146 GHNFGAVHD 154
TSP_1 pfam00090
Thrombospondin type 1 domain;
570-618 7.00e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 7.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1940128051 570 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVIPC 618
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 568-618 6.58e-06

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: 44.19  E-value: 6.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1940128051 568 GSWGPWGQCSRSCGGGVQFAYRHCNNPaPRNSGRYCTGKRAIyRSCSVIPC 618
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 267-445 1.35e-05

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 48.62  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 267 QVELLLVADSSMAKMYGR-GLQHYLLTLASIANRLYSHASIEnhIRLAVVKVVVLTDKSleVSKNAATTLKNFCKWQHQH 345
Cdd:NF038115   20 TIDVNFVVDQAIVESQGReALDKQIEAAISLSNETYLSAGTD--LHFNVRQVVVESDNS--VDATCTSGLGGALDGLLAS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 346 NQLgdDHEEHYDAAILFTREDlcgHHSC------DTLGMA-------DVGTICSPERSCA---------------VIEDD 397
Cdd:NF038115   96 GQI--ACRDAYDEAFNHMDNV---VWDCpspgdnDRVGNAgysygadFWVTIVSGSDGNAngvaqvgmdlqvkgyNVTLD 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128051 398 GLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 445
Cdd:NF038115  171 LYVATQTLAHELGHLFGLYNGhaESAECSEGgyrlmcgslaenfenlFGSSELQRFYNNADSTLDD 236
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 571-618 3.44e-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: 42.05  E-value: 3.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1940128051 571 GPWGQCSRSCGGGVQfaYR--HCNNPAPR--NSGRYCTGKRA--IYRSCSVIPC 618
Cdd:pfam19030   4 GPWGECSVTCGGGVQ--TRlvQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 290-461 1.40e-04

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 43.77  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 290 LLTLASIANRLYSHASIEnhIRLAVVKVVvltdkSLEVSKNAATTLKNFCK---WQHQHNQLGDD--HEEHYDAAILFTR 364
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDIN--INGGLVNPG-----EIPATTSASDSGNNYCNsptTIVRRLNFLSQwrGEQDYCLAHLVTM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 365 EDLCGhhscDTLGMADVGTICSPERSCaVIEDDGLHAAFT-------------VAHEIGHLLGLSHD------DSKFCEE 425
Cdd:pfam13574  80 GTFSG----GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdgsqyASSGCER 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1940128051 426 NFGSTEDKRLMSSIL--TSIDASKPWSKCTSATITEFL 461
Cdd:pfam13574 155 NAATSVCSANGSFIMnpASKSNNDLFSPCSISLICDVL 192
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 268-457 1.17e-03

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: 41.07  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 268 VELLLVADSSMAKMYGR--GLQHYLLTLASIANRLYSHaSIENHIRLAVVKVVVLTDKS-----LEVSKNAATT--LKNF 338
Cdd:pfam13583   5 YRVAVATDCTYSASFGSvdELRANINATVTTANEVYGR-DFNVSLALISDRDVIYTDSStdsfnADCSGGDLGNwrLATL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128051 339 CKWQHQHNqlgddheehYDAAILFtREDLCGHHSCdtlGMADVGTICSPER-----SCAVIEDDGLHaafTVAHEIGHLL 413
Cdd:pfam13583  84 TSWRDSLN---------YDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTF 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1940128051 414 GLSHDDSKFCEENFGSTEDKRlMSSILT--SIDASKPWSKCTSATI 457
Cdd:pfam13583 148 GAVHDCSSQGEGLSSSTEDGS-GQTIMSyaSTASQTAFSPCTIRNI 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 876-927 4.89e-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: 36.03  E-value: 4.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1940128051  876 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCILSQRPSAFKQCLLKKC 927
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 403-417 6.88e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.37  E-value: 6.88e-03
                          10
                  ....*....|....*.
gi 1940128051 403 FTVA-HEIGHLLGLSH 417
Cdd:pfam00413 109 FLVAaHEIGHALGLGH 124
 
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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