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Conserved domains on  [gi|91064869|ref|NP_766207|]
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A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform 1 preproprotein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 2.25e-109

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: 339.21  E-value: 2.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  319 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273   81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869  399 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 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 7.01e-35

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: 129.36  E-value: 7.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869     40 EIAFPTRVDHNgamlafsppafrRQRRGAGATTE--SRLFYKVAAPSTHFLLNLTRSPRLLAGHVSVEYWTREGLAW--Q 115
Cdd:pfam01562    1 EVVIPVRLDPS------------RRRRSLASESTylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVesP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    116 RAARAHCLYAGHLQGQAGSShVAVSTCGGLHGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 180
Cdd:pfam01562   69 PVQTDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 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 1.73e-29

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: 113.44  E-value: 1.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    707 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 91064869    786 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 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 1.65e-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: 1.65e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064869    469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 1.15e-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: 63.63  E-value: 1.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    948 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 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 1.23e-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: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    607 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 91064869    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 ...
 888-944 5.93e-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: 5.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 91064869    888 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 3.95e-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: 59.00  E-value: 3.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869    829 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 3.10e-09

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 3.10e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 91064869   1007 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1070-1102 2.53e-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: 47.53  E-value: 2.53e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 91064869   1070 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1102
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 4.97e-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: 41.80  E-value: 4.97e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91064869     550 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 2.25e-109

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: 339.21  E-value: 2.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  319 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273   81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869  399 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 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 7.01e-35

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: 129.36  E-value: 7.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869     40 EIAFPTRVDHNgamlafsppafrRQRRGAGATTE--SRLFYKVAAPSTHFLLNLTRSPRLLAGHVSVEYWTREGLAW--Q 115
Cdd:pfam01562    1 EVVIPVRLDPS------------RRRRSLASESTylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVesP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    116 RAARAHCLYAGHLQGQAGSShVAVSTCGGLHGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 180
Cdd:pfam01562   69 PVQTDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 3.85e-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: 121.25  E-value: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    316 KWQKSIVSHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAH 392
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    393 EIGHTFGMNHDGVGNGCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 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 1.73e-29

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: 113.44  E-value: 1.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    707 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 91064869    786 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 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 1.65e-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: 1.65e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064869    469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 1.15e-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: 63.63  E-value: 1.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    948 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 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 1.23e-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: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    607 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 91064869    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 ...
 888-944 5.93e-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: 5.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 91064869    888 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 3.95e-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: 59.00  E-value: 3.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869    829 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 3.10e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 3.10e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 91064869   1007 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1070-1102 2.53e-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: 47.53  E-value: 2.53e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 91064869   1070 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1102
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 870-1005 2.65e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.16  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869   870 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 944
Cdd:PHA02682   27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91064869   945 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 1005
Cdd:PHA02682   99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 4.97e-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: 41.80  E-value: 4.97e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91064869     550 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 829-885 1.02e-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: 41.03  E-value: 1.02e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 91064869     829 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 885
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1007-1054 1.26e-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: 40.65  E-value: 1.26e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 91064869    1007 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 1054
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 952-1003 5.50e-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: 36.03  E-value: 5.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 91064869     952 DWSECTPSCGPGLRHRVVLCKSADQRstLPPGHCLPAAkpPSTMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED--VETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 239-454 2.25e-109

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: 339.21  E-value: 2.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  319 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273   81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869  399 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 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 5.71e-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: 140.63  E-value: 5.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  239 RYVETLVVADKMMVAYHgRRDVE---QYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFC 315
Cdd:cd04267    1 REIELVVVADHRMVSYF-NSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  316 KWQKSivshsghgnaipenGVANHDTAVLITRYDIciyknKPCGTLGLAPVGGMCERERSCSINEDIGLA--TAFTIAHE 393
Cdd:cd04267   80 FWRAE--------------GPIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHE 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 91064869  394 IGHTFGMNHDGVGNGCGARGQDPAKLMAAHITmKTNPFVWSSCSRDYITSFLD 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 1.02e-35

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: 134.28  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  239 RYVETLVVADKMMVAYHGRRD--VEQYVLAIMNIVAKLFQDSslgNIvNILVTRLILLTEDQPtLEITHHAGKSLDSFCK 316
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYRPL---NI-RVVLVGLEIWTDKDK-ISVSGDAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  317 WQKSIVSHSghgnaIPengvanHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAHE 393
Cdd:cd04269   76 WKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHE 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064869  394 IGHTFGMNHDGVGNGCGARGQdpakLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 455
Cdd:cd04269  139 LGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-180 7.01e-35

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: 129.36  E-value: 7.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869     40 EIAFPTRVDHNgamlafsppafrRQRRGAGATTE--SRLFYKVAAPSTHFLLNLTRSPRLLAGHVSVEYWTREGLAW--Q 115
Cdd:pfam01562    1 EVVIPVRLDPS------------RRRRSLASESTylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVesP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    116 RAARAHCLYAGHLQGQAGSShVAVSTCGGLHGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 180
Cdd:pfam01562   69 PVQTDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 239-457 3.85e-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: 121.25  E-value: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    316 KWQKSIVSHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAH 392
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    393 EIGHTFGMNHDGVGNGCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 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 1.73e-29

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: 113.44  E-value: 1.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    707 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 785
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 91064869    786 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 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 1.65e-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: 1.65e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064869    469 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 537
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 240-453 5.72e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 69.30  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  240 YVETLVVADKMMVAYHGR-RDVEQYVLAIMNIVAKLFQDSSLGNIvNILVTRLILLTEDQPTLEITHHAGKSLDSfckwQ 318
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLKSPRI-RLLLVGITISKDPDFEPYIHPINYGYIDA----A 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  319 KSIVSHSGHgnAIPENGVANHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSINEDigLATAF----TIAH 392
Cdd:cd04272   77 ETLENFNEY--VKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91064869  393 EIGHTFGMNHDG---VGNGCGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 453
Cdd:cd04272  152 ELAHLLGAPHDGsppPSWVKGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 335-445 8.53e-13

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 67.55  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  335 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSINED---IGLATAFTIAHEIGHTFGMNHDGVGNGC-- 409
Cdd:cd00203   48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 91064869  410 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 445
Cdd:cd00203  122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-1002 1.15e-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: 63.63  E-value: 1.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 91064869    948 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 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 1.23e-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: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    607 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 673
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 91064869    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 ...
 888-944 5.93e-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: 5.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 91064869    888 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 944
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 829-884 3.95e-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: 59.00  E-value: 3.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869    829 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 884
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
244-403 7.40e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.44  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    244 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSlgNIvNILVTRLILLTEDQPTleiTHHAGKSLDSFCKWQKSIVS 323
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF--NI-SLGLVNLTISDSTCPY---TPPACSTGDSSDRLSEFQDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    324 HSghgnaipENGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSINEDIGLA--------TAFTIAHEIG 395
Cdd:pfam13688   82 SA-------WRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146


                   ....*...
gi 91064869    396 HTFGMNHD 403
Cdd:pfam13688  147 HNFGAVHD 154
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 359-445 2.97e-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: 58.02  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    359 GTLGLAPVGGMCERERSCsINEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NGCGARGQDPA 417
Cdd:pfam13574   85 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 163

                           90       100       110
                   ....*....|....*....|....*....|.
gi 91064869    418 K---LMAAhiTMKTNPFVWSSCSRDYITSFL 445
Cdd:pfam13574  164 NgsfIMNP--ASKSNNDLFSPCSISLICDVL 192
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1007-1056 3.10e-09

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.00  E-value: 3.10e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 91064869   1007 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 1056
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 263-403 1.90e-08

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 53.53  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    263 YVLAIMNIVAKLFQ-DSSLG-NIVNILVTRLilltEDQPTLEIThhAGKSLDSFckwQKSIVSHSGHGNAipengvanhD 340
Cdd:pfam13582    2 RIVSLVNRANTIYErDLGIRlQLAAIIITTS----ADTPYTSSD--ALEILDEL---QEVNDTRIGQYGY---------D 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91064869    341 TAVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSINEDI---GLATAFTIAHEIGHTFGMNHD 403
Cdd:pfam13582   64 LGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1070-1102 2.53e-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: 47.53  E-value: 2.53e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 91064869   1070 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1102
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 239-441 1.74e-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: 46.84  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    239 RYVETLVVADKMMVAYHGRRD-VEQYVLAIMNIVAKLFQdSSLGNIVNILVTRLILLTEDQPTLEITHHAGK-----SLD 312
Cdd:pfam13583    3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVYG-RDFNVSLALISDRDVIYTDSSTDSFNADCSGGdlgnwRLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869    313 SFCKWQksivshsghgnaipenGVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERScsiNEDIGLATAFT--- 389
Cdd:pfam13583   82 TLTSWR----------------DSLNYDLAYLTLMT------GPSGQNVGVAWVGALCSSARQ---NAKASGVARSRdew 136

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 91064869    390 --IAHEIGHTFGMNHDGVGNGCGARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 441
Cdd:pfam13583  137 diFAHEIGHTFGAVHDCSSQGEGLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 244-452 1.82e-05

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


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 47.37  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  244 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKL--------FQDSSLGNIvNILVTRLILLTEDQPTleithhagksldsfc 315
Cdd:cd04270    6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKGI-GFQIKRIRIHTTPDEV--------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  316 kwqksiVSHSGHGNAIPEN-GVANHDTAVLITRY--DICI-----YKNKPCGTLGLAPV--------GGMCERE------ 373
Cdd:cd04270   70 ------DPGNKFYNKSFPNwGVEKFLVKLLLEQFsdDVCLahlftYRDFDMGTLGLAYVgsprdnsaGGICEKAyyysng 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869  374 RSCSINedIGLATAF-------------TIAHEIGHTFGMNHDGVGNGCGARGQDPAK-LMAAHITM--KTNPFVWSSCS 437
Cdd:cd04270  144 KKKYLN--TGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGESQGGNyIMYARATSgdKENNKKFSPCS 221

                        250
                 ....*....|....*
gi 91064869  438 RDYITSFLDSGLGLC 452
Cdd:cd04270  222 KKSISKVLEVKSNSC 236
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 870-1005 2.65e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.16  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064869   870 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 944
Cdd:PHA02682   27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91064869   945 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 1005
Cdd:PHA02682   99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 550-602 4.97e-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: 41.80  E-value: 4.97e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91064869     550 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 829-885 1.02e-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: 41.03  E-value: 1.02e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 91064869     829 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 885
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1007-1054 1.26e-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: 40.65  E-value: 1.26e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 91064869    1007 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 1054
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
1008-1053 3.55e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 3.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 91064869   1008 VTSEWGECSTQCGLGQQQRTVRC--TSHTGQPSRECTEALRPSTMQQC 1053
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCksPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 952-1003 5.50e-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: 36.03  E-value: 5.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 91064869     952 DWSECTPSCGPGLRHRVVLCKSADQRstLPPGHCLPAAkpPSTMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED--VETRACNEQPCP 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.
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