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Conserved domains on  [gi|2462600321|ref|XP_054207496|]
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A disintegrin and metalloproteinase with thrombospondin motifs 6 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) ...
 250-465 6.05e-110

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: 339.98  E-value: 6.05e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273     81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273    153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-191 1.82e-45

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: 159.79  E-value: 1.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321   43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562    1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462600321  123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562   65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 669-779 2.10e-38

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: 138.87  E-value: 2.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  669 IEGFFNDSlPRGGYMEVVQIPRGSVHIEVREVAMSKNYIALKSEGDDYYINGAWTID-WPRKFDVAGTAFHYKRPTDEPE 747
Cdd:pfam05986    2 VSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462600321  748 SLEALGPTSENLIVMVLLQ---EQNLGIRYKFNVP 779
Cdd:pfam05986   81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 794-849 4.42e-16

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: 73.26  E-value: 4.42e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  794 WNHQPWSECSATCAGGVQRQEVVCKRLDDNSIVQNNYCDPDSKPPEnQRACNTEPC 849
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPE-TQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 853-909 5.81e-15

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: 70.17  E-value: 5.81e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462600321  853 WFIGDWLECSKTCDGGMRTRAVLCIRKIGPSEEetlDYSGC-LTHRPVEKEPCNNQSC 909
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 568-666 8.01e-15

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: 71.66  E-value: 8.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  568 DFREKQCADFDNMPFR-----GKYYNWK---PYTGGGVKpCALNCLAEGYNFYTERAPAVIDGTQCNAD------SLDIC 633
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGaavPHSQGDAL-CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462600321  634 INGECKHVGCDNILGSDAREDRCRVCGGDGSTC 666
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 2.62e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.62e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462600321  913 WVALDWSECTPKCGPGFKHRIVLCKSSDLSKTFPAAQCPEESKPPVRIRCSLGRC 967
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 972-1021 4.53e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 4.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462600321  972 WVTGDWGQCSAQCGLGQQMRTVQCLSYTG---QASSDCLETVRPPSMQQCESK 1021
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1033-1065 8.42e-08

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 49.07  E-value: 8.42e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462600321 1033 CKDvnKVAYCPLVLKFKFCSRAYFRQMCCKTCQ 1065
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
ADAMTS_CR_2 super family cl39281
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 480-504 2.70e-05

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: 43.10  E-value: 2.70e-05
                           10        20
                   ....*....|....*....|....*
gi 2462600321  480 PGQVYDADEQCRFQYGATSRQCKYG 504
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG 25
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 250-465 6.05e-110

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: 339.98  E-value: 6.05e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273     81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273    153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-191 1.82e-45

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: 159.79  E-value: 1.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321   43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562    1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462600321  123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562   65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 669-779 2.10e-38

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: 138.87  E-value: 2.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  669 IEGFFNDSlPRGGYMEVVQIPRGSVHIEVREVAMSKNYIALKSEGDDYYINGAWTID-WPRKFDVAGTAFHYKRPTDEPE 747
Cdd:pfam05986    2 VSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462600321  748 SLEALGPTSENLIVMVLLQ---EQNLGIRYKFNVP 779
Cdd:pfam05986   81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 250-468 9.72e-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: 120.10  E-value: 9.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRkDIEH---YILSVMNIVAKLYRDSslgNVVNIIVARLIVLTEDQpnLEINHHADKSLDSFC 326
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTVvrqRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  327 KWQKSILSHQSDgntipengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIAH 403
Cdd:pfam01421   75 KWRQEYLKKRKP-----------HDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462600321  404 EIGHNFGMNHDGIGN--SCGTKGheaAKLMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCLDNEP 468
Cdd:pfam01421  138 ELGHNLGMQHDDFNGgcKCPPGG---GCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 794-849 4.42e-16

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: 73.26  E-value: 4.42e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  794 WNHQPWSECSATCAGGVQRQEVVCKRLDDNSIVQNNYCDPDSKPPEnQRACNTEPC 849
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPE-TQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 853-909 5.81e-15

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: 70.17  E-value: 5.81e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462600321  853 WFIGDWLECSKTCDGGMRTRAVLCIRKIGPSEEetlDYSGC-LTHRPVEKEPCNNQSC 909
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 568-666 8.01e-15

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: 71.66  E-value: 8.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  568 DFREKQCADFDNMPFR-----GKYYNWK---PYTGGGVKpCALNCLAEGYNFYTERAPAVIDGTQCNAD------SLDIC 633
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGaavPHSQGDAL-CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462600321  634 INGECKHVGCDNILGSDAREDRCRVCGGDGSTC 666
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 2.62e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.62e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462600321  913 WVALDWSECTPKCGPGFKHRIVLCKSSDLSKTFPAAQCPEESKPPVRIRCSLGRC 967
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 972-1021 4.53e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 4.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462600321  972 WVTGDWGQCSAQCGLGQQMRTVQCLSYTG---QASSDCLETVRPPSMQQCESK 1021
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1033-1065 8.42e-08

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 49.07  E-value: 8.42e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462600321 1033 CKDvnKVAYCPLVLKFKFCSRAYFRQMCCKTCQ 1065
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 852-910 1.81e-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: 42.96  E-value: 1.81e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462600321   852 EWfiGDWLECSKTCDGGMRTRAVLCIRKIGPSEEETldysgClTHRPVEKEPCNNQSCP 910
Cdd:smart00209    3 EW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGP-----C-TGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 798-850 2.66e-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: 42.57  E-value: 2.66e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462600321   798 PWSECSATCAGGVQRQEVVCkrLDDNSIVQNNYCDPDSkpPEnQRACNTEPCP 850
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSC--CSPPPQNGGGPCTGED--VE-TRACNEQPCP 53
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 480-504 2.70e-05

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: 43.10  E-value: 2.70e-05
                           10        20
                   ....*....|....*....|....*
gi 2462600321  480 PGQVYDADEQCRFQYGATSRQCKYG 504
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG 25
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 972-1019 6.64e-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: 6.64e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2462600321   972 WVTGDWGQCSAQCGLGQQMRTVQCLSYTGQAS-SDCLET---VRPPSMQQCE 1019
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEdveTRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 250-465 6.05e-110

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: 339.98  E-value: 6.05e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273     81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273    153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-191 1.82e-45

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: 159.79  E-value: 1.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321   43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562    1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462600321  123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562   65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 669-779 2.10e-38

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: 138.87  E-value: 2.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  669 IEGFFNDSlPRGGYMEVVQIPRGSVHIEVREVAMSKNYIALKSEGDDYYINGAWTID-WPRKFDVAGTAFHYKRPTDEPE 747
Cdd:pfam05986    2 VSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462600321  748 SLEALGPTSENLIVMVLLQ---EQNLGIRYKFNVP 779
Cdd:pfam05986   81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 250-457 2.99e-38

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: 2.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRK--DIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCK 327
Cdd:cd04267      1 REIELVVVADHRMVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  328 WQKSilshqsdgntipenGIAHHDNAVLITRYDICTyknkpCGTLGLASVAGMCEPERSCSINEDIG--LGSAFTIAHEI 405
Cdd:cd04267     81 WRAE--------------GPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHEL 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462600321  406 GHNFGMNHDGIGNSCGTKGHEAAKLMaAHITANTNPFSWSACSRDYITSFLD 457
Cdd:cd04267    142 GHNLGAEHDGGDELAFECDGGGNYIM-APVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 250-466 6.66e-36

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: 134.67  E-value: 6.66e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRKD--IEHYILSVMNIVAKLYRDsslgnvVNIIVA--RLIVLTEDQPnLEINHHADKSLDSF 325
Cdd:cd04269      1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYRP------LNIRVVlvGLEIWTDKDK-ISVSGDAGETLNRF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  326 CKWQKSILSHQsdgntIPengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIA 402
Cdd:cd04269     74 LDWKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMA 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462600321  403 HEIGHNFGMNHDGIGNSCGTKGHeaakLMAAHITanTNPFSWSACSRDYITSFLDSGRGTCLDN 466
Cdd:cd04269    137 HELGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 250-468 9.72e-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: 120.10  E-value: 9.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRkDIEH---YILSVMNIVAKLYRDSslgNVVNIIVARLIVLTEDQpnLEINHHADKSLDSFC 326
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTVvrqRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  327 KWQKSILSHQSDgntipengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIAH 403
Cdd:pfam01421   75 KWRQEYLKKRKP-----------HDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462600321  404 EIGHNFGMNHDGIGN--SCGTKGheaAKLMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCLDNEP 468
Cdd:pfam01421  138 ELGHNLGMQHDDFNGgcKCPPGG---GCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 794-849 4.42e-16

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: 73.26  E-value: 4.42e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  794 WNHQPWSECSATCAGGVQRQEVVCKRLDDNSIVQNNYCDPDSKPPEnQRACNTEPC 849
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPE-TQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 853-909 5.81e-15

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: 70.17  E-value: 5.81e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462600321  853 WFIGDWLECSKTCDGGMRTRAVLCIRKIGPSEEetlDYSGC-LTHRPVEKEPCNNQSC 909
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 568-666 8.01e-15

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: 71.66  E-value: 8.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  568 DFREKQCADFDNMPFR-----GKYYNWK---PYTGGGVKpCALNCLAEGYNFYTERAPAVIDGTQCNAD------SLDIC 633
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGaavPHSQGDAL-CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462600321  634 INGECKHVGCDNILGSDAREDRCRVCGGDGSTC 666
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 346-456 4.36e-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: 4.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  346 GIAHHDNAVLITRYDictyknKPCGTLGLASVAGMCEPERSCSINEDIGLGS---AFTIAHEIGHNFGMNHDGIGNSCGT 422
Cdd:cd00203     48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTkegAQTIAHELGHALGFYHDHDRKDRDD 121

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462600321  423 KGHEAAK----------LMAAHITANT--NPFSWSACSRDYITSFL 456
Cdd:cd00203    122 YPTIDDTlnaedddyysVMSYTKGSFSdgQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 2.62e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.62e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462600321  913 WVALDWSECTPKCGPGFKHRIVLCKSSDLSKTFPAAQCPEESKPPVRIRCSLGRC 967
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 972-1021 4.53e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 61.70  E-value: 4.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462600321  972 WVTGDWGQCSAQCGLGQQMRTVQCLSYTG---QASSDCLETVRPPSMQQCESK 1021
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLK 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 251-464 4.87e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.61  E-value: 4.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  251 FVETLVVADKMMVGYHGR-KDIEHYILSVMNIVAKLYRDSSLGNVVniivarlIVLTedqpNLEINHHADKSLDSFCKWQ 329
Cdd:cd04272      2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLKSPRIR-------LLLV----GITISKDPDFEPYIHPINY 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  330 KSILSHQS--DGNT--IPENGIAHHDNAVLITRYDICTYKNKPC--GTLGLASVAGMCEpERSCSINEDIGlGS---AFT 400
Cdd:cd04272     71 GYIDAAETleNFNEyvKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGEDTP-GSyygVYT 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462600321  401 IAHEIGHNFGMNHDGIGNSCGTKGHEAAK--------LMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCL 464
Cdd:cd04272    149 MTHELAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgyIMSYVVNG-ERQYRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
255-443 3.33e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 63.59  E-value: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  255 LVVADKMMVGYHGRKDIEHYILSVMNIVAKL-YRDSSlgnvVNIIVARLIVLTEDQPNleiNHHADKSLDSfckwqKSIL 333
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVyERDFN----ISLGLVNLTISDSTCPY---TPPACSTGDS-----SDRL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  334 SHQSDGNTIpeNGIAHHDNAVLITrydictykNKPCGTLGLASVAGMCEPERSCSINEDIGLGS--------AFTIAHEI 405
Cdd:pfam13688   76 SEFQDFSAW--RGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNvvvstateWQVFAHEI 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462600321  406 GHNFGMNHD-----GIGNSCGTKGHEAAK---LMAAHITANTNPFS 443
Cdd:pfam13688  146 GHNFGAVHDcdsstSSQCCPPSNSTCPAGgryIMNPSSSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 274-414 6.42e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 57.77  E-value: 6.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  274 YILSVMNIVAKLY-RDSSLG-NVVNIIvarlIVLTEDQPNLEINhhADKSLDSFCKWQksilSHQSDGNTIpengiahhD 351
Cdd:pfam13582    2 RIVSLVNRANTIYeRDLGIRlQLAAII----ITTSADTPYTSSD--ALEILDELQEVN----DTRIGQYGY--------D 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462600321  352 NAVLITRYDictyknkPCGTLGLASVAGMCEPERSCSINEDI---GLGSAFTIAHEIGHNFGMNHD 414
Cdd:pfam13582   64 LGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 255-463 5.97e-08

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: 55.07  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  255 LVVADKMMVGYHGRKDIE---HYILSVMNIVAKLYRDSSLGNV----VNIIVARLIVLTEDQPNLEINHHADKSL--DSF 325
Cdd:cd04270      6 LLVADHRFYKYMGRGEEEttiNYLISHIDRVDDIYRNTDWDGGgfkgIGFQIKRIRIHTTPDEVDPGNKFYNKSFpnWGV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  326 CKWQKSILSHQsdgntipengiaHHDNAVLITRYdicTYKNKPCGTLGLASVA--------GMCEPE------RSCSINe 391
Cdd:cd04270     86 EKFLVKLLLEQ------------FSDDVCLAHLF---TYRDFDMGTLGLAYVGsprdnsagGICEKAyyysngKKKYLN- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  392 dIGLGSAF-------------TIAHEIGHNFGMNHDGIGNSCGTKGHEAAK-LMAAHIT----ANTNPFswSACSRDYIT 453
Cdd:cd04270    150 -TGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGESQGGNyIMYARATsgdkENNKKF--SPCSKKSIS 226

                          250
                   ....*....|
gi 2462600321  454 SFLDSGRGTC 463
Cdd:cd04270    227 KVLEVKSNSC 236
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1033-1065 8.42e-08

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 49.07  E-value: 8.42e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462600321 1033 CKDvnKVAYCPLVLKFKFCSRAYFRQMCCKTCQ 1065
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 275-456 3.74e-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: 372637  Cd Length: 193  Bit Score: 48.78  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  275 ILSVMNIVAKLYRDSSLG-NVVNIIVARLIVLTE--DQPNLEINHHADKS--LDSFCKWQksilshqsdgntipenGIAH 349
Cdd:pfam13574    7 LVNVVNRVNQIYEPDDINiNGGLVNPGEIPATTSasDSGNNYCNSPTTIVrrLNFLSQWR----------------GEQD 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  350 HDNAVLITRYDiCTyknkpCGTLGLASVAGMCEPERSCS-----INEDIGLGSAFT-------IAHEIGHNFGMNHD-GI 416
Cdd:pfam13574   71 YCLAHLVTMGT-FS-----GGELGLAYVGQICQKGASSPktntgLSTTTNYGSFNYptqewdvVAHEVGHNFGATHDcDG 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462600321  417 GNSCGTKGHEAAK----------LMAAhiTANTNPFSWSACSRDYITSFL 456
Cdd:pfam13574  145 SQYASSGCERNAAtsvcsangsfIMNP--ASKSNNDLFSPCSISLICDVL 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 852-910 1.81e-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: 42.96  E-value: 1.81e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462600321   852 EWfiGDWLECSKTCDGGMRTRAVLCIRKIGPSEEETldysgClTHRPVEKEPCNNQSCP 910
Cdd:smart00209    3 EW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGP-----C-TGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 798-850 2.66e-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: 42.57  E-value: 2.66e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462600321   798 PWSECSATCAGGVQRQEVVCkrLDDNSIVQNNYCDPDSkpPEnQRACNTEPCP 850
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSC--CSPPPQNGGGPCTGED--VE-TRACNEQPCP 53
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 480-504 2.70e-05

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: 43.10  E-value: 2.70e-05
                           10        20
                   ....*....|....*....|....*
gi 2462600321  480 PGQVYDADEQCRFQYGATSRQCKYG 504
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG 25
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 972-1019 6.64e-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: 6.64e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2462600321   972 WVTGDWGQCSAQCGLGQQMRTVQCLSYTGQAS-SDCLET---VRPPSMQQCE 1019
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEdveTRACNEQPCP 53
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 250-422 1.07e-04

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 44.53  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  250 RFVETLVVADKMMVGYHGRKD-IEHYILSVMNIVAKLYrdsslGNVVNIivaRLIVLTEDQPNleinhHADKSLDSFCKW 328
Cdd:pfam13583    3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVY-----GRDFNV---SLALISDRDVI-----YTDSSTDSFNAD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  329 QKSILSHQSDGNTIPEN-GIAHHDNAVLITRYDICTYKNkpcgtlGLASVAGMCEPERSCSinedigLGSAF-------- 399
Cdd:pfam13583   70 CSGGDLGNWRLATLTSWrDSLNYDLAYLTLMTGPSGQNV------GVAWVGALCSSARQNA------KASGVarsrdewd 137

                          170       180
                   ....*....|....*....|...
gi 2462600321  400 TIAHEIGHNFGMNHDGIGNSCGT 422
Cdd:pfam13583  138 IFAHEIGHTFGAVHDCSSQGEGL 160
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 256-464 2.28e-03

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: 40.87  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  256 VVAD-KMMVGYHGRKDIEHYILSVMNIVAKLYRDS---SLGnVVNIIVARL---IVLTEDQP-NLEINHHADKS--LDSF 325
Cdd:cd04271      7 VAADcSYTKSFGSVEEARRNILNNVNSASQLYESSfniSLG-LRNLTISDAscpSTAVDSAPwNLPCNSRIDIDdrLSIF 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  326 CKWQksilSHQSDgntipengiahhDNAVLITRYDICtyknkPCG-TLGLASVAGMCEPERSCSINEDIG--LGSAFT-- 400
Cdd:cd04271     86 SQWR----GQQPD------------DGNAFWTLMTAC-----PSGsEVGVAWLGQLCRTGASDQGNETVAgtNVVVRTsn 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600321  401 ----IAHEIGHNFGMNHDGIGNSCGTKGHEAAK---LMAAHITAN----TNPFS------WSACSRDYITSFL--DSGRG 461
Cdd:cd04271    145 ewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQccpLSTSTCDANgqyiMNPSSssgiteFSPCTIGNICSLLgrNPVRT 224


                   ...
gi 2462600321  462 TCL 464
Cdd:cd04271    225 SCL 227
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 798-849 8.87e-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: 35.33  E-value: 8.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462600321  798 PWSECSATCAGGVQ-RQEVVckrlddnsIVQNNY----CdpdskPPENQ-RACNTEPC 849
Cdd:pfam19028    8 EWSECSVTCGGGVQtRTRTV--------IVEPQNggrpC-----PELLErRPCNLPPC 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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