NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|537544566|ref|NP_112219|]
View 

A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform 1 preproprotein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.63e-108

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: 336.52  E-value: 2.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  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 2.77e-31

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: 119.34  E-value: 2.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562    1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562   71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 707-818 2.07e-28

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: 110.36  E-value: 2.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   707 TIEGVFSPAsPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFQLRQGPDQV 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 537544566   786 QSLEALGPINASLIVMVLARTEL---PALRYRFNAP 818
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQYGKgtnPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-537 1.70e-16

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: 74.69  E-value: 1.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537544566   469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 7.99e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 69.54  E-value: 7.99e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 2.65e-13

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: 65.17  E-value: 2.65e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   948 WAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRC 1002
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 607-705 2.21e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.73  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   607 DFREVQCSEFDSIPFR-----GKFYKWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 537544566   674 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 705
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 2.35e-11

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: 59.77  E-value: 2.35e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566   829 WHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 888-944 6.56e-11

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: 58.62  E-value: 6.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 537544566   888 WVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACHGPTC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 7.37e-11

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: 58.23  E-value: 7.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537544566  1007 WVAGEWGECSAQCGVGQRQRSVRCT---SHTGQASHECTEALRPPTTQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1069-1100 5.07e-07

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: 46.76  E-value: 5.07e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSC 30
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 2.63e-108

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: 336.52  E-value: 2.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  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 2.77e-31

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: 119.34  E-value: 2.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562    1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562   71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 1.83e-30

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: 119.33  E-value: 1.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTIAH 392
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   393 EIGHTFGMNHDGVGNSCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421  138 ELGHNLGMQHDDFNGGCKCPPGGGC-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 707-818 2.07e-28

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: 110.36  E-value: 2.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   707 TIEGVFSPAsPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFQLRQGPDQV 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 537544566   786 QSLEALGPINASLIVMVLARTEL---PALRYRFNAP 818
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQYGKgtnPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-537 1.70e-16

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: 74.69  E-value: 1.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537544566   469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 7.99e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 69.54  E-value: 7.99e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 2.65e-13

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: 65.17  E-value: 2.65e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   948 WAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRC 1002
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 607-705 2.21e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.73  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   607 DFREVQCSEFDSIPFR-----GKFYKWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 537544566   674 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 705
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 2.35e-11

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: 59.77  E-value: 2.35e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566   829 WHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 888-944 6.56e-11

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: 58.62  E-value: 6.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 537544566   888 WVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACHGPTC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 7.37e-11

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: 58.23  E-value: 7.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537544566  1007 WVAGEWGECSAQCGVGQRQRSVRCT---SHTGQASHECTEALRPPTTQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
551-601 1.59e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.95  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537544566   551 GPWTPWGDCSRTCGGGVSSSSRHCDSPRPtiGGKYCLGERRRHRSCNTDDC 601
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1069-1100 5.07e-07

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: 46.76  E-value: 5.07e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSC 30
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 867-1005 3.22e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.16  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  867 SAHSKLPKRQRACNTEPCPPDWVVG---NWSL--CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleAChg 941
Cdd:PHA02682   24 SLFTKCPQATIPAPAAPCPPDADVDpldKYSVkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP----AC-- 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537544566  942 PTCPPewAALDWSECTPSCGPGlrhrvvlCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPA 1005
Cdd:PHA02682   96 PACAP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1010-1054 3.88e-04

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: 39.49  E-value: 3.88e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 537544566   1010 GEWGECSAQCGVGQRQRSVRCTSHTGQAS-HECTEAL---RPPTTQQCE 1054
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDvetRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 952-1003 3.07e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 3.07e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 537544566    952 DWSECTPSCGPGLRHRVVLCKsaDHRATLPPAHCSPAAkpPATMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCC--SPPPQNGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 829-885 4.08e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.41  E-value: 4.08e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 537544566    829 WHYAPWTKCSAQCAGGSQVQAVECRNQLDSsaVAPHYCsahSKLPKRQRACNTEPCP 885
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPC---TGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 2.63e-108

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: 336.52  E-value: 2.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  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 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 537544566  239 RYVETLVVADKMMVAYHgRRDVE---QYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFC 315
Cdd:cd04267     1 REIELVVVADHRMVSYF-NSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  316 KWQKSivnhsghgnaipenGVANHDTAVLITRYDIciyknKPCGTLGLAPVGGMCERERSCSVNEDIGLA--TAFTIAHE 393
Cdd:cd04267    80 FWRAE--------------GPIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHE 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 537544566  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 5.03e-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: 135.05  E-value: 5.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRD--VEQYVLAIMNIVAKLFQdsslgsTVNILVTrLILL---TEDQPtLEITHHAGKSLDS 313
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwTDKDK-ISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  314 FCKWQKSIVNHSghgnaIPengvanHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTI 390
Cdd:cd04269    73 FLDWKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTM 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544566  391 AHEIGHTFGMNHDGVGNSCGARGQdpakLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 455
Cdd:cd04269   136 AHELGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-180 2.77e-31

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: 119.34  E-value: 2.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafsppppRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAAR 119
Cdd:pfam01562    1 EVVIPVRLDPSR----------RRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   120 P--HCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGGPkgsrSPEESGPHVVY 180
Cdd:pfam01562   71 QtdHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYS----REEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 1.83e-30

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: 119.33  E-value: 1.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTIAH 392
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   393 EIGHTFGMNHDGVGNSCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421  138 ELGHNLGMQHDDFNGGCKCPPGGGC-IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 707-818 2.07e-28

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: 110.36  E-value: 2.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   707 TIEGVFSPAsPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFQLRQGPDQV 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 537544566   786 QSLEALGPINASLIVMVLARTEL---PALRYRFNAP 818
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQYGKgtnPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 469-537 1.70e-16

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: 74.69  E-value: 1.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537544566   469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 7.99e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 69.54  E-value: 7.99e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 335-445 2.33e-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: 69.09  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  335 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSVNED---IGLATAFTIAHEIGHTFGMNHDGVGNSC-- 409
Cdd:cd00203    48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 537544566  410 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 445
Cdd:cd00203   122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 240-453 2.63e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 70.46  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  240 YVETLVVADKMMVAYHGR-RDVEQYVLAIMNIVAKLFQDSSlGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSfckwQ 318
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYGYIDA----A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGHgnAIPENGVANHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSVNEDigLATAF----TIAH 392
Cdd:cd04272    77 ETLENFNEY--VKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 537544566  393 EIGHTFGMNHDG---VGNSCGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 453
Cdd:cd04272   152 ELAHLLGAPHDGsppPSWVKGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 2.65e-13

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: 65.17  E-value: 2.65e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   948 WAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRC 1002
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 607-705 2.21e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.73  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   607 DFREVQCSEFDSIPFR-----GKFYKWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 537544566   674 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 705
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 2.35e-11

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: 59.77  E-value: 2.35e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566   829 WHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 888-944 6.56e-11

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: 58.62  E-value: 6.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 537544566   888 WVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACHGPTC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 7.37e-11

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: 58.23  E-value: 7.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 537544566  1007 WVAGEWGECSAQCGVGQRQRSVRCT---SHTGQASHECTEALRPPTTQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
244-414 1.77e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 61.28  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   244 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSlgsTVNILVTRLILLTEDQPTleiTHHAGKSLDSfckwqKSIVN 323
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPY---TPPACSTGDS-----SDRLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   324 HSGHGNAIpeNGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSVNEDIGLA--------TAFTIAHEIG 395
Cdd:pfam13688   77 EFQDFSAW--RGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146

                          170       180       190
                   ....*....|....*....|....*....|
gi 537544566   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 1.04e-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: 372637  Cd Length: 193  Bit Score: 59.18  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   359 GTLGLAPVGGMCERERSCsVNEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NSCGARGQDPA 417
Cdd:pfam13574   85 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 163

                           90       100       110
                   ....*....|....*....|....*....|.
gi 537544566   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 6.68e-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: 55.07  E-value: 6.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   263 YVLAIMNIVAKLFQdSSLGSTVNilVTRLILLT-EDQPTLEIThhAGKSLDSFckwQKSIVNHSGHGNAipengvanhDT 341
Cdd:pfam13582    2 RIVSLVNRANTIYE-RDLGIRLQ--LAAIIITTsADTPYTSSD--ALEILDEL---QEVNDTRIGQYGY---------DL 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544566   342 AVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSVNEDI---GLATAFTIAHEIGHTFGMNHD 403
Cdd:pfam13582   65 GHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP_1 pfam00090
Thrombospondin type 1 domain;
551-601 1.59e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.95  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537544566   551 GPWTPWGDCSRTCGGGVSSSSRHCDSPRPtiGGKYCLGERRRHRSCNTDDC 601
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1069-1100 5.07e-07

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: 46.76  E-value: 5.07e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSC 30
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 359-452 7.10e-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: 7.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  359 GTLGLAPV--------GGMCERERSCSVNEDI----GLATAF-------------TIAHEIGHTFGMNHDGVGNSCGARG 413
Cdd:cd04270   115 GTLGLAYVgsprdnsaGGICEKAYYYSNGKKKylntGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGE 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 537544566  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 1.30e-05

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 47.23  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRRD-VEQYVLAIMNIVAKLFQdSSLGSTVNILVTRLILLTEDQPTLEITHHAGK-----SLD 312
Cdd:pfam13583    3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVYG-RDFNVSLALISDRDVIYTDSSTDSFNADCSGGdlgnwRLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   313 SFCKWQksivnhsghgnaipenGVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERScsvNEDIGLATAFT--- 389
Cdd:pfam13583   82 TLTSWR----------------DSLNYDLAYLTLMT------GPSGQNVGVAWVGALCSSARQ---NAKASGVARSRdew 136

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 537544566   390 --IAHEIGHTFGMNHDGVGNSCGARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 441
Cdd:pfam13583  137 diFAHEIGHTFGAVHDCSSQGEGLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 551-601 2.52e-05

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: 42.65  E-value: 2.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537544566   551 GPWTPWGDCSRTCGGGVSSSSRHCDSPrPTIGGKYClGERRRHRSCNTDDC 601
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 867-1005 3.22e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.16  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  867 SAHSKLPKRQRACNTEPCPPDWVVG---NWSL--CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleAChg 941
Cdd:PHA02682   24 SLFTKCPQATIPAPAAPCPPDADVDpldKYSVkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP----AC-- 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537544566  942 PTCPPewAALDWSECTPSCGPGlrhrvvlCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPA 1005
Cdd:PHA02682   96 PACAP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1010-1054 3.88e-04

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: 39.49  E-value: 3.88e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 537544566   1010 GEWGECSAQCGVGQRQRSVRCTSHTGQAS-HECTEAL---RPPTTQQCE 1054
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDvetRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 554-601 1.53e-03

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: 37.82  E-value: 1.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 537544566   554 TPWGDCSRTCGGGVSSSSRHCDSPRP--TIGGKYCLGERRRH--RSCNTDDC 601
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKPPetQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 952-1003 3.07e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 3.07e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 537544566    952 DWSECTPSCGPGLRHRVVLCKsaDHRATLPPAHCSPAAkpPATMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCC--SPPPQNGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 829-885 4.08e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.41  E-value: 4.08e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 537544566    829 WHYAPWTKCSAQCAGGSQVQAVECRNQLDSsaVAPHYCsahSKLPKRQRACNTEPCP 885
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPC---TGEDVETRACNEQPCP 53
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH