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Conserved domains on  [gi|1907093831|ref|XP_036013956|]
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A disintegrin and metalloproteinase with thrombospondin motifs 16 isoform X8 [Mus musculus]

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) ...
 288-489 5.81e-106

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: 319.95  E-value: 5.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 288 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 367
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 368 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 444
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093831 445 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 489
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 88-203 2.81e-32

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 121.27  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831  88 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 167
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907093831 168 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 203
Cdd:pfam01562 100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 506-573 7.83e-20

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: 83.55  E-value: 7.83e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093831 506 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 573
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 587-639 2.25e-18

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: 79.17  E-value: 2.25e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907093831  587 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 639
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 288-489 5.81e-106

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: 319.95  E-value: 5.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 288 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 367
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 368 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 444
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093831 445 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 489
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 290-493 6.93e-35

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: 131.27  E-value: 6.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 290 VETLVVVDRKMMQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW- 366
Cdd:pfam01421   3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 367 QSGLMGKdgTRHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 443
Cdd:pfam01421  78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093831 444 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 493
Cdd:pfam01421 150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 88-203 2.81e-32

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 121.27  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831  88 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 167
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907093831 168 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 203
Cdd:pfam01562 100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 506-573 7.83e-20

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: 83.55  E-value: 7.83e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093831 506 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 573
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 587-639 2.25e-18

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: 79.17  E-value: 2.25e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907093831  587 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 639
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
588-638 2.97e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.58  E-value: 2.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093831 588 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 638
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 288-489 5.81e-106

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: 319.95  E-value: 5.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 288 LNVETLVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 367
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 368 SGLMGKDG---TRHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 444
Cdd:cd04273    81 KKLNPPNDsdpEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093831 445 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 489
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 290-482 8.37e-41

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: 147.57  E-value: 8.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 290 VETLVVVDRKM-MQSHGHENITT-YVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADHTLTSFCQWQ 367
Cdd:cd04267     3 IELVVVADHRMvSYFNSDENILQaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 368 SglmgKDGTRHDHAILLTGLDICSwknepCDTLGFAPISGMCSKYRSCTVNEDSGLGL--AFTIAHESGHNFGMVHDGEG 445
Cdd:cd04267    83 A----EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGD 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907093831 446 ---NMCKKSEGNIMSPTLAGRNGVFsWSSCSRQYLHKFLS 482
Cdd:cd04267   154 elaFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 289-489 5.81e-38

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: 139.67  E-value: 5.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 289 NVETLVVVDRKMMQSHGH--ENITTYVLTILNMVSALFKdgTIggNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW 366
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PL--NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 367 QSGLMGKdGTRHDHAILLTGLDICSwknepcDTLGFAPISGMCSKYRSCTVNEDSG---LGLAFTIAHESGHNFGMVHDG 443
Cdd:cd04269    77 KRSNLLP-RKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093831 444 EGnmCKKSEGN-IMSPTLAgrNGVFSWSSCSRQYLHKFLSTAQAICL 489
Cdd:cd04269   150 GG--CTCGRSTcIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 290-493 6.93e-35

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: 131.27  E-value: 6.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 290 VETLVVVDRKMMQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADHTLTSFCQW- 366
Cdd:pfam01421   3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 367 QSGLMGKdgTRHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 443
Cdd:pfam01421  78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093831 444 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 493
Cdd:pfam01421 150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 88-203 2.81e-32

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 121.27  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831  88 TQPGGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPPEENCFYQGSLRSQGNSSVALSTCQGLLG 167
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907093831 168 MIRTKDTDYFLKPLPPHltsklnrSAQGDSPSHVLY 203
Cdd:pfam01562 100 FIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 506-573 7.83e-20

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: 83.55  E-value: 7.83e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093831 506 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 573
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 288-489 1.17e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 88.18  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 288 LNVETLVVVDRKMMQSHGH-ENITTYVLTILNMVSALFKDgTIGGNINIVIVGLILLEDEQPGLAISHHAD------HTL 360
Cdd:cd04272     1 VYPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYgyidaaETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 361 TSFCQWQSGlmGKDGTRHDHAILLTGLDICSWKNEPCDT--LGFAPISGMCSKYRSCTVnEDSG--LGLAFTIAHESGHN 436
Cdd:cd04272    80 ENFNEYVKK--KRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAHL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093831 437 FGMVHDGEG-----------NMCKKSEGNIMSPTLAGRNGvFSWSSCSRQYLHKFLSTAQAICL 489
Cdd:cd04272   157 LGAPHDGSPppswvkghpgsLDCPWDDGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGASCL 219
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 587-639 2.25e-18

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: 79.17  E-value: 2.25e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907093831  587 WSDWSPWSPCSRTCGGGISHRDRLCTNPRPSHGGKFCQGSTRTLKLCNSQRCP 639
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 372-481 7.24e-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: 67.16  E-value: 7.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 372 GKDGTRHDHAILLTGLDIcswknePCDTLGFAPISGMCSKYRSCTVNEDSGLG---LAFTIAHESGHNFGMVHDGEGNMC 448
Cdd:cd00203    46 GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907093831 449 KK-------------SEGNIMSPTLAGRNGVFS--WSSCSRQYLHKFL 481
Cdd:cd00203   120 DDyptiddtlnaeddDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
TSP_1 pfam00090
Thrombospondin type 1 domain;
588-638 2.97e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.58  E-value: 2.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093831 588 SDWSPWSPCSRTCGGGISHRDRLCTNPRPshGGKFCQGSTRTLKLCNSQRC 638
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
293-468 2.97e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 293 LVVVDRKMMQSHGHENITTYVLTILNMVSALFKDGTiggNINIVIVGLILLEDEQPGLAISHH---ADHTLTSFcQWQSG 369
Cdd:pfam13688   8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACStgdSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 370 LMGKDgtRHDHAILLTgldicswkNEPCDTLGFAPISGMCSKYRSCTVNEDSG--------LGLAFTIAHESGHNFGMVH 441
Cdd:pfam13688  84 WRGTQ--NDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGAVH 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907093831 442 DGEGNM-----------CKKSEGNIMSPTLAGRNGVFS 468
Cdd:pfam13688 154 DCDSSTssqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 588-638 1.24e-10

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 56.90  E-value: 1.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093831 588 SDWSPWSPCSRTCGGGISHRDRLCTNPrPSHGGKFCQGSTRTLKlCNSQRC 638
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLERRP-CNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 308-474 1.01e-08

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 55.71  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 308 NITTYVLTILNMVSALFKDGTIggNINIVIVGLILLEDEQPGLAiSHHAD--------HTLTSFCQWQsglmgkdGTRHD 379
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDI--NINGGLVNPGEIPATTSASD-SGNNYcnspttivRRLNFLSQWR-------GEQDY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 380 HAILLTGLDICSwknEPcdTLGFAPISGMCSKYRSCtVNEDSGLGLAFT-------------IAHESGHNFGMVHD--GE 444
Cdd:pfam13574  72 CLAHLVTMGTFS---GG--ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdGS 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907093831 445 GNMCKKSEGN------------IMSPTlaGRNGVFSWSSCSR 474
Cdd:pfam13574 146 QYASSGCERNaatsvcsangsfIMNPA--SKSNNDLFSPCSI 185
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 592-638 1.18e-06

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: 45.91  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093831 592 PWSPCSRTCGGGISHRDRLCTNPRP--SHGGKFCQGSTR--TLKLCNSQRC 638
Cdd:pfam19030   5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 332-442 2.49e-06

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: 46.98  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 332 NINIVIVGLILLED-EQPGLAIShhADHTLTSFCQWQSGLMGKDGtrHDHAILLTGLDicswknePCDTLGFAPISGMCS 410
Cdd:pfam13582  19 GIRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDTRIGQYG--YDLGHLFTGRD-------GGGGGGIAYVGGVCN 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907093831 411 KYRSCTVNEDS---GLGLAFTIAHESGHNFGMVHD 442
Cdd:pfam13582  88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 428-488 7.63e-05

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: 44.67  E-value: 7.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093831 428 TIAHESGHNFGMVHDGEGNMCKKSE---GN-IMSP-TLAG---RNGVFswSSCSRQYLHKFLSTAQAIC 488
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYArATSGdkeNNKKF--SPCSKKSISKVLEVKSNSC 236
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 313-481 1.13e-04

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 43.95  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 313 VLTILNMVSALFKDGTiggNINIVIVGLILLEDEQP---------------GLAIshhaDHTLTSFCQWQSGLMGKDgtr 377
Cdd:cd04271    27 ILNNVNSASQLYESSF---NISLGLRNLTISDASCPstavdsapwnlpcnsRIDI----DDRLSIFSQWRGQQPDDG--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093831 378 hdhAILLTGLDICswKNEPcdTLGFAPISGMCSKYRSCTVNED--SGLGLAFT------IAHESGHNFGMVHD------- 442
Cdd:cd04271    97 ---NAFWTLMTAC--PSGS--EVGVAWLGQLCRTGASDQGNETvaGTNVVVRTsnewqvFAHEIGHTFGAVHDctsgtcs 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093831 443 ----GEGNMCKKSEGN-------IMSPTlaGRNGVFSWSSCSRQYLHKFL 481
Cdd:cd04271   170 dgsvGSQQCCPLSTSTcdangqyIMNPS--SSSGITEFSPCTIGNICSLL 217
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 591-607 2.48e-04

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 38.85  E-value: 2.48e-04
                          10
                  ....*....|....*..
gi 1907093831 591 SPWSPCSRTCGGGISHR 607
Cdd:pfam19035   6 TEWSPCSKTCGMGVSTR 22
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 428-458 1.94e-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: 39.91  E-value: 1.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907093831 428 TIAHESGHNFGMVHD----GEGNMCKKSEGN---IMSP 458
Cdd:pfam13583 138 IFAHEIGHTFGAVHDcssqGEGLSSSTEDGSgqtIMSY 175
 
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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