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Conserved domains on  [gi|2462543017|ref|XP_054233390|]
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A disintegrin and metalloproteinase with thrombospondin motifs 17 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 232-493 8.34e-83

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: 268.72  E-value: 8.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  232 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 311
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  312 NEeyggarylgnnQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVvppapfdvregpgsppwwclgrelpeangsqrv 391
Cdd:cd04273     81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTL--------------------------------- 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  392 ipdhsisktweGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPS 468
Cdd:cd04273    116 -----------GLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTG 182

                          250       260
                   ....*....|....*....|....*
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICLL 493
Cdd:cd04273    183 PFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 510-577 8.78e-26

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: 101.27  E-value: 8.78e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  510 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 577
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 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 ...
 781-877 2.76e-23

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: 95.72  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  781 YIEAAVIPAGARRIRVVEDKPAHSFLALK-DSGKGSINSDWKIEL-PGEFQIAGTTVRYVRR-GLWEKISAKGPTKLPLH 857
Cdd:pfam05986   14 YVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSlPALEELHAPGPTQEDLE 93

                           90       100
                   ....*....|....*....|..
gi 2462543017  858 LMVL--LFHDQDYGIHYEYTVP 877
Cdd:pfam05986   94 IQVLrqYGKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 81-180 3.15e-19

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: 84.67  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017   81 LLLHLPAFGRDLYLQLRRDLRFLSRGFEVE---EAGAARRRGR-PAELCFYSGRVLGHPGSLVSLSACgaaGGLVGLIQL 156
Cdd:pfam01562   27 LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTyylDGGTGVESPPvQTDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRT 103

                           90       100
                   ....*....|....*....|....
gi 2462543017  157 GQEQVLIQPLNNSQGPFSGREHLI 180
Cdd:pfam01562  104 ENEEYLIEPLEKYSREEGGHPHVV 127
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 590-642 2.98e-16

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: 73.78  E-value: 2.98e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017   590 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 642
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1015 8.76e-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: 55.54  E-value: 8.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  959 WVAGPWSPCSATCEKGFQHREVTCVYQLQNGTHVATRplyCPG-PRPAAVQSCEGQDC 1015
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE---CSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1019-1061 2.55e-09

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462543017 1019 WEASEWSQCSASCGKGVWKRTVACTNSQGK-------CDASTRPRAEEAC 1061
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivpdseCSAQKKPPETQSC 50
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 674-743 3.88e-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: 55.49  E-value: 3.88e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543017  674 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 743
Cdd:pfam19236   40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 903-955 1.01e-08

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.46  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017  903 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNLHPC 955
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 232-493 8.34e-83

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: 268.72  E-value: 8.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  232 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 311
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  312 NEeyggarylgnnQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVvppapfdvregpgsppwwclgrelpeangsqrv 391
Cdd:cd04273     81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTL--------------------------------- 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  392 ipdhsisktweGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPS 468
Cdd:cd04273    116 -----------GLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTG 182

                          250       260
                   ....*....|....*....|....*
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICLL 493
Cdd:cd04273    183 PFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 510-577 8.78e-26

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: 101.27  E-value: 8.78e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  510 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 577
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 781-877 2.76e-23

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: 95.72  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  781 YIEAAVIPAGARRIRVVEDKPAHSFLALK-DSGKGSINSDWKIEL-PGEFQIAGTTVRYVRR-GLWEKISAKGPTKLPLH 857
Cdd:pfam05986   14 YVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSlPALEELHAPGPTQEDLE 93

                           90       100
                   ....*....|....*....|..
gi 2462543017  858 LMVL--LFHDQDYGIHYEYTVP 877
Cdd:pfam05986   94 IQVLrqYGKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 81-180 3.15e-19

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: 84.67  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017   81 LLLHLPAFGRDLYLQLRRDLRFLSRGFEVE---EAGAARRRGR-PAELCFYSGRVLGHPGSLVSLSACgaaGGLVGLIQL 156
Cdd:pfam01562   27 LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTyylDGGTGVESPPvQTDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRT 103

                           90       100
                   ....*....|....*....|....
gi 2462543017  157 GQEQVLIQPLNNSQGPFSGREHLI 180
Cdd:pfam01562  104 ENEEYLIEPLEKYSREEGGHPHVV 127
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 395-493 7.64e-18

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: 83.12  E-value: 7.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  395 HSISKTWEGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLGMNHDDDHSSC---AGRSHIMSGEWVKgrnPS 468
Cdd:pfam01421   96 VEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SF 172

                           90       100
                   ....*....|....*....|....*
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICLL 493
Cdd:pfam01421  173 PRKFSNCSQEDFEQFLTKQKGACLF 197
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 590-642 2.98e-16

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: 73.78  E-value: 2.98e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017   590 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 642
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
591-641 4.82e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.89  E-value: 4.82e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462543017  591 SPWGAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCPGASVEHAVCENLPC 641
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1015 8.76e-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: 55.54  E-value: 8.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  959 WVAGPWSPCSATCEKGFQHREVTCVYQLQNGTHVATRplyCPG-PRPAAVQSCEGQDC 1015
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE---CSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1019-1061 2.55e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462543017 1019 WEASEWSQCSASCGKGVWKRTVACTNSQGK-------CDASTRPRAEEAC 1061
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivpdseCSAQKKPPETQSC 50
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 674-743 3.88e-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: 55.49  E-value: 3.88e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543017  674 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 743
Cdd:pfam19236   40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 903-955 1.01e-08

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.46  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017  903 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNLHPC 955
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 962-1015 8.96e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.42  E-value: 8.96e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462543017   962 GPWSPCSATCEKGFQHREVTCV-YQLQNGTHvatrplYCPGPRPaAVQSCEGQDC 1015
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCsPPPQNGGG------PCTGEDV-ETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1019-1050 1.23e-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: 37.95  E-value: 1.23e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462543017  1019 WEASEWSQCSASCGKGVWKRTVACTNSQGKCD 1050
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNG 33
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 232-493 8.34e-83

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: 268.72  E-value: 8.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  232 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 311
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  312 NEeyggarylgnnQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVvppapfdvregpgsppwwclgrelpeangsqrv 391
Cdd:cd04273     81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTL--------------------------------- 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  392 ipdhsisktweGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPS 468
Cdd:cd04273    116 -----------GLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTG 182

                          250       260
                   ....*....|....*....|....*
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICLL 493
Cdd:cd04273    183 PFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 510-577 8.78e-26

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: 101.27  E-value: 8.78e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  510 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 577
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 234-493 1.67e-25

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: 105.00  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  234 VETLVVADADMVQYHG--AEAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVLL-----RQrpaKLSIGHHGERSLES 306
Cdd:cd04269      3 VELVVVVDNSLYKKYGsnLSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwtdKD---KISVSGDAGETLNR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  307 FCHWQNeeyggaRYLGNNQVPggkddpplvDAAVFVTRTDFCVHKDepcdtvvppapfdvregpgsppwwclgrelpean 386
Cdd:cd04269     73 FLDWKR------SNLLPRKPH---------DNAQLLTGRDFDGNTV---------------------------------- 103

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  387 gsqrvipdhsisktweGIAYLGGVCSAKRKCVLAED---NGLNLAFTIAHELGHNLGMNHDDDHSSCAGRSHIMSgewvk 463
Cdd:cd04269    104 ----------------GLAYVGGMCSPKYSGGVVQDhsrNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIMA----- 162

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462543017  464 gRNPSDLS--WSSCSRDDLENFLKSKVSICLL 493
Cdd:cd04269    163 -PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 781-877 2.76e-23

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: 95.72  E-value: 2.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  781 YIEAAVIPAGARRIRVVEDKPAHSFLALK-DSGKGSINSDWKIEL-PGEFQIAGTTVRYVRR-GLWEKISAKGPTKLPLH 857
Cdd:pfam05986   14 YVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSlPALEELHAPGPTQEDLE 93

                           90       100
                   ....*....|....*....|..
gi 2462543017  858 LMVL--LFHDQDYGIHYEYTVP 877
Cdd:pfam05986   94 IQVLrqYGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 233-485 2.80e-20

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: 89.79  E-value: 2.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  233 TVETLVVADADMVQYHGA--EAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHW 310
Cdd:cd04267      2 EIELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  311 QNEEyggarylgnnqvpggkddPPLVDAAVFVTRTDFcvhkdEPCDTVvppapfdvregpgsppwwclgrelpeangsqr 390
Cdd:cd04267     82 RAEG------------------PIRHDNAVLLTAQDF-----IEGDIL-------------------------------- 106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  391 vipdhsisktweGIAYLGGVCSAKRKCVLAEDNGLNL--AFTIAHELGHNLGMNHDDD----HSSCAGRSHIMSGEWVKG 464
Cdd:cd04267    107 ------------GLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGdelaFECDGGGNYIMAPVDSGL 174

                          250       260
                   ....*....|....*....|.
gi 2462543017  465 RNpsdLSWSSCSRDDLENFLK 485
Cdd:cd04267    175 NS---YRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 81-180 3.15e-19

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: 84.67  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017   81 LLLHLPAFGRDLYLQLRRDLRFLSRGFEVE---EAGAARRRGR-PAELCFYSGRVLGHPGSLVSLSACgaaGGLVGLIQL 156
Cdd:pfam01562   27 LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTyylDGGTGVESPPvQTDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRT 103

                           90       100
                   ....*....|....*....|....
gi 2462543017  157 GQEQVLIQPLNNSQGPFSGREHLI 180
Cdd:pfam01562  104 ENEEYLIEPLEKYSREEGGHPHVV 127
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 395-493 7.64e-18

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: 83.12  E-value: 7.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  395 HSISKTWEGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLGMNHDDDHSSC---AGRSHIMSGEWVKgrnPS 468
Cdd:pfam01421   96 VEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SF 172

                           90       100
                   ....*....|....*....|....*
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICLL 493
Cdd:pfam01421  173 PRKFSNCSQEDFEQFLTKQKGACLF 197
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 590-642 2.98e-16

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: 73.78  E-value: 2.98e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017   590 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 642
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 403-492 2.67e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 67.38  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  403 GIAYLGGVCSaKRKCVLAEDNG--LNLAFTIAHELGHNLGMNHDDDH--SSCAGRS----------HIMSgeWVKGrNPS 468
Cdd:cd04272    120 GYAYVGGACT-ENRVAMGEDTPgsYYGVYTMTHELAHLLGAPHDGSPppSWVKGHPgsldcpwddgYIMS--YVVN-GER 195

                           90       100
                   ....*....|....*....|....
gi 2462543017  469 DLSWSSCSRDDLENFLKSKVSICL 492
Cdd:cd04272    196 QYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 403-484 3.73e-12

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: 65.62  E-value: 3.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543017  403 GIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLGMNHDDDHSSCA--------------GRSHIMSGEWVKGR 465
Cdd:cd00203     69 GWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDdyptiddtlnaeddDYYSVMSYTKGSFS 148

                           90
                   ....*....|....*....
gi 2462543017  466 NPSDLSWSSCSRDDLENFL 484
Cdd:cd00203    149 DGQRKDFSQCDIDQINKLY 167
TSP_1 pfam00090
Thrombospondin type 1 domain;
591-641 4.82e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.89  E-value: 4.82e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462543017  591 SPWGAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCPGASVEHAVCENLPC 641
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 959-1015 8.76e-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: 55.54  E-value: 8.76e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543017  959 WVAGPWSPCSATCEKGFQHREVTCVYQLQNGTHVATRplyCPG-PRPAAVQSCEGQDC 1015
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE---CSAqKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1019-1061 2.55e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462543017 1019 WEASEWSQCSASCGKGVWKRTVACTNSQGK-------CDASTRPRAEEAC 1061
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivpdseCSAQKKPPETQSC 50
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 674-743 3.88e-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: 55.49  E-value: 3.88e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543017  674 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 743
Cdd:pfam19236   40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 403-444 8.80e-09

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: 54.68  E-value: 8.80e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462543017  403 GIAYLGGVCSAKRKCVLAED---NGLNLAFTIAHELGHNLGMNHD 444
Cdd:pfam13582   78 GIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 903-955 1.01e-08

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 52.46  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462543017  903 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNLHPC 955
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 591-641 2.23e-08

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: 51.51  E-value: 2.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462543017  591 SPWGAWSMCSRTCGTGARFRQRKCDNPPPGpGGTHCPgASVEHAVCENLPC 641
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPCP-ELLERRPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 430-491 2.90e-07

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 53.15  E-value: 2.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462543017  430 TIAHELGHNLGMNHDDDHSSCA-----GRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFLKSKVSIC 491
Cdd:cd04270    170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 403-454 2.59e-05

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 46.47  E-value: 2.59e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462543017  403 GIAYLGGVCSAKRKCVlAEDNGLNLAFT-------------IAHELGHNLGMNHDDDHSSCAGRS 454
Cdd:pfam13574   88 GLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGSQYASSG 151
TSP_1 pfam00090
Thrombospondin type 1 domain;
962-1015 5.10e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.63  E-value: 5.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462543017  962 GPWSPCSATCEKGFQHREVTCVYQLQNGTHvatrplyCPGPRpAAVQSCEGQDC 1015
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKSPFPGGEP-------CTGDD-IETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 962-1015 8.96e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.42  E-value: 8.96e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462543017   962 GPWSPCSATCEKGFQHREVTCV-YQLQNGTHvatrplYCPGPRPaAVQSCEGQDC 1015
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCsPPPQNGGG------PCTGEDV-ETRACNEQPC 52
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
403-449 1.83e-04

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 43.95  E-value: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462543017  403 GIAYLGGVCSAKRKCVLAEDNGLN--------LAFTIAHELGHNLGMNHDDDHSS 449
Cdd:pfam13688  105 GLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIGHNFGAVHDCDSST 159
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1019-1050 1.23e-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: 37.95  E-value: 1.23e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462543017  1019 WEASEWSQCSASCGKGVWKRTVACTNSQGKCD 1050
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNG 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 955-989 1.73e-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: 37.64  E-value: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462543017  955 CQ-SRWvaGPWSPCSATCEKGFQHREVTCVYQLQNG 989
Cdd:pfam19028    1 CVvSEW--SEWSECSVTCGGGVQTRTRTVIVEPQNG 34
 
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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