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Conserved domains on  [gi|2462567956|ref|XP_054178239|]
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A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 1.44e-113

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: 336.13  E-value: 1.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462567956 399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-180 6.55e-30

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: 113.95  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956  40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562   1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462567956 120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562  71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
ADAMTS_CR_2 super family cl39281
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-488 1.49e-03

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.


The actual alignment was detected with superfamily member pfam17771:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 37.32  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|
gi 2462567956 469 PGQAYDADEQCRFQHGVKSR 488
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGST 20
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 1.44e-113

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: 336.13  E-value: 1.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462567956 399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 9.74e-31

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: 118.56  E-value: 9.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTIAH 392
Cdd:pfam01421  75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462567956 393 EIGHTFGMNHDGVGNSCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421 138 ELGHNLGMQHDDFNGGCKCPPGGGC-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-180 6.55e-30

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: 113.95  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956  40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562   1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462567956 120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562  71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-488 1.49e-03

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: 37.32  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|
gi 2462567956 469 PGQAYDADEQCRFQHGVKSR 488
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGST 20
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 1.44e-113

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: 336.13  E-value: 1.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462567956 399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 239-446 4.20e-39

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: 141.40  E-value: 4.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHgRRDVE---QYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFC 315
Cdd:cd04267     1 REIELVVVADHRMVSYF-NSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 316 KWQKSivnhsghgnaipenGVANHDTAVLITRYDIciyknKPCGTLGLAPVGGMCERERSCSVNEDIGLA--TAFTIAHE 393
Cdd:cd04267    80 FWRAE--------------GPIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHE 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462567956 394 IGHTFGMNHDGVGNSCGARGQDPAKLMAAHITmKTNPFVWSSCSRDYITSFLD 446
Cdd:cd04267   141 LGHNLGAEHDGGDELAFECDGGGNYIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 239-455 8.99e-37

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: 135.05  E-value: 8.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRRD--VEQYVLAIMNIVAKLFQdsslgsTVNILVTrLILL---TEDQPtLEITHHAGKSLDS 313
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwTDKDK-ISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 314 FCKWQKSIVNHSghgnaIPengvanHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTI 390
Cdd:cd04269    73 FLDWKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTM 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462567956 391 AHEIGHTFGMNHDGVGNSCGARGQdpakLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 455
Cdd:cd04269   136 AHELGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 9.74e-31

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: 118.56  E-value: 9.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTIAH 392
Cdd:pfam01421  75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462567956 393 EIGHTFGMNHDGVGNSCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421 138 ELGHNLGMQHDDFNGGCKCPPGGGC-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-180 6.55e-30

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: 113.95  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956  40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562   1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462567956 120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562  71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 240-453 1.67e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 70.07  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 240 YVETLVVADKMMVAYHGR-RDVEQYVLAIMNIVAKLFQDSSlGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSfckwQ 318
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYGYIDA----A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 319 KSIVNHSGHgnAIPENGVANHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSVNEDigLATAF----TIAH 392
Cdd:cd04272    77 ETLENFNEY--VKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462567956 393 EIGHTFGMNHDG---VGNSCGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 453
Cdd:cd04272   152 ELAHLLGAPHDGsppPSWVKGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 335-445 2.25e-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: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 335 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSVNED---IGLATAFTIAHEIGHTFGMNHDGVGNSC-- 409
Cdd:cd00203    48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462567956 410 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 445
Cdd:cd00203   122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
244-414 3.74e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.44  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 244 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSlgsTVNILVTRLILLTEDQPTleiTHHAGKSLDSfckwqKSIVN 323
Cdd:pfam13688   8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPY---TPPACSTGDS-----SDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 324 HSGHGNAIpeNGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSVNEDIGLA--------TAFTIAHEIG 395
Cdd:pfam13688  77 EFQDFSAW--RGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462567956 396 HTFGMNHD-----------GVGNSCGARGQ 414
Cdd:pfam13688 147 HNFGAVHDcdsstssqccpPSNSTCPAGGR 176
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 359-445 4.70e-10

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: 59.18  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 359 GTLGLAPVGGMCERERSCsVNEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NSCGARGQDPA 417
Cdd:pfam13574  85 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 163

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462567956 418 K---LMAAhiTMKTNPFVWSSCSRDYITSFL 445
Cdd:pfam13574 164 NgsfIMNP--ASKSNNDLFSPCSISLICDVL 192
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 263-403 8.55e-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: 53.91  E-value: 8.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 263 YVLAIMNIVAKLFQdSSLGSTVNilVTRLILLT-EDQPTLEIThhAGKSLDSFckwQKSIVNHSGHGNAipengvanhDT 341
Cdd:pfam13582   2 RIVSLVNRANTIYE-RDLGIRLQ--LAAIIITTsADTPYTSSD--ALEILDEL---QEVNDTRIGQYGY---------DL 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462567956 342 AVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSVNEDI---GLATAFTIAHEIGHTFGMNHD 403
Cdd:pfam13582  65 GHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 359-452 3.13e-06

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: 48.52  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 359 GTLGLAPV--------GGMCERERSCSVNEDI----GLATAF-------------TIAHEIGHTFGMNHDGVGNSCGARG 413
Cdd:cd04270   115 GTLGLAYVgsprdnsaGGICEKAYYYSNGKKKylntGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGE 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462567956 414 QDPAK-LMAAHITM--KTNPFVWSSCSRDYITSFLDSGLGLC 452
Cdd:cd04270   195 SQGGNyIMYARATSgdKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 239-441 5.92e-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: 404471  Cd Length: 203  Bit Score: 47.23  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 239 RYVETLVVADKMMVAYHGRRD-VEQYVLAIMNIVAKLFQdSSLGSTVNILVTRLILLTEDQPTLEITHHAGK-----SLD 312
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVYG-RDFNVSLALISDRDVIYTDSSTDSFNADCSGGdlgnwRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462567956 313 SFCKWQksivnhsghgnaipenGVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERScsvNEDIGLATAFT--- 389
Cdd:pfam13583  82 TLTSWR----------------DSLNYDLAYLTLMT------GPSGQNVGVAWVGALCSSARQ---NAKASGVARSRdew 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462567956 390 --IAHEIGHTFGMNHDGVGNSCGARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 441
Cdd:pfam13583 137 diFAHEIGHTFGAVHDCSSQGEGLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-488 1.49e-03

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: 37.32  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|
gi 2462567956 469 PGQAYDADEQCRFQHGVKSR 488
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGST 20
 
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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