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Conserved domains on  [gi|1039753301|ref|XP_017172900|]
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A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform X1 [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) ...
 173-388 4.84e-110

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 339.60  E-value: 4.84e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 252
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  253 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 332
Cdd:cd04273     81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  333 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 388
Cdd:cd04273    153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 641-752 1.62e-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: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  641 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 719
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753301  720 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 752
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 ...
 403-471 2.14e-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: 74.30  E-value: 2.14e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753301  403 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 471
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 541-639 1.24e-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: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  541 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 607
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039753301  608 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 639
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 882-936 1.42e-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: 63.24  E-value: 1.42e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039753301  882 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 936
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 822-878 7.25e-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: 61.31  E-value: 7.25e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753301  822 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 878
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-818 4.78e-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: 4.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  763 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 818
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 ...
 941-990 3.61e-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: 53.61  E-value: 3.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301  941 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 990
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1004-1036 2.87e-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: 2.87e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039753301 1004 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1036
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 80-114 2.58e-05

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 44.61  E-value: 2.58e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1039753301   80 HGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 114
Cdd:pfam01562   98 RGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 484-536 5.68e-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: 5.68e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301   484 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 536
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) ...
 173-388 4.84e-110

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 339.60  E-value: 4.84e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 252
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  253 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 332
Cdd:cd04273     81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  333 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 388
Cdd:cd04273    153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 173-391 3.20e-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: 121.64  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFC 249
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  250 KWQKSIVSHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAH 326
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753301  327 EIGHTFGMNHDGVGNGCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 391
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 ...
 641-752 1.62e-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: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  641 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 719
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753301  720 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 752
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 ...
 403-471 2.14e-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: 74.30  E-value: 2.14e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753301  403 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 471
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 541-639 1.24e-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: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  541 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 607
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039753301  608 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 639
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 882-936 1.42e-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: 63.24  E-value: 1.42e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039753301  882 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 936
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 822-878 7.25e-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: 61.31  E-value: 7.25e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753301  822 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 878
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-818 4.78e-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: 4.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  763 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 818
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 941-990 3.61e-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: 53.61  E-value: 3.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301  941 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 990
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1004-1036 2.87e-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: 2.87e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039753301 1004 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1036
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 80-114 2.58e-05

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: 44.61  E-value: 2.58e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1039753301   80 HGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 114
Cdd:pfam01562   98 RGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 128
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 804-939 3.66e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 46.78  E-value: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  804 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 878
Cdd:PHA02682    27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753301  879 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 939
Cdd:PHA02682    99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 484-536 5.68e-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: 5.68e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301   484 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 536
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 763-819 1.19e-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: 1.19e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753301   763 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 819
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 941-988 1.49e-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: 1.49e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1039753301   941 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 988
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 886-937 6.23e-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: 6.23e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1039753301   886 DWSECTPSCGPGLRHRVVLCKSADQRstLPPGHCLPAAkpPSTMRCNLRRCP 937
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) ...
 173-388 4.84e-110

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 339.60  E-value: 4.84e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 252
Cdd:cd04273      1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  253 KSIVSHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSINEDIGLATAFTIAHEIGHTF 332
Cdd:cd04273     81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  333 GMNHDGVGNGCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 388
Cdd:cd04273    153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 173-380 5.33e-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: 5.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHgRRDVE---QYVLAIMNIVAKLFQDSSLGNIVNILVTRLILLTEDQPTLEITHHAGKSLDSFC 249
Cdd:cd04267      1 REIELVVVADHRMVSYF-NSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  250 KWQKSivshsghgnaipenGVANHDTAVLITRYDIciyknKPCGTLGLAPVGGMCERERSCSINEDIGLA--TAFTIAHE 327
Cdd:cd04267     80 FWRAE--------------GPIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHE 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301  328 IGHTFGMNHDGVGNGCGARGQDPAKLMAAHITmKTNPFVWSSCSRDYITSFLD 380
Cdd:cd04267    141 LGHNLGAEHDGGDELAFECDGGGNYIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 173-389 8.70e-36

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 134.28  E-value: 8.70e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRRD--VEQYVLAIMNIVAKLFQDSslgNIvNILVTRLILLTEDQPtLEITHHAGKSLDSFCK 250
Cdd:cd04269      1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYRPL---NI-RVVLVGLEIWTDKDK-ISVSGDAGETLNRFLD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  251 WQKSIVSHSghgnaIPengvanHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAHE 327
Cdd:cd04269     76 WKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHE 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753301  328 IGHTFGMNHDGVGNGCGARGQdpakLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 389
Cdd:cd04269    139 LGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 173-391 3.20e-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: 121.64  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQDSslgNIVNILVTRLILLTEDQptLEITHHAGKSLDSFC 249
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DTTvvrQRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  250 KWQKSIVSHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSINEDIG---LATAFTIAH 326
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753301  327 EIGHTFGMNHDGVGNGCGARGQDPAkLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 391
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 ...
 641-752 1.62e-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: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  641 TIEGVFSPAlPGTGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGT-PQPHRLPLAGTTFHLRQGPDQA 719
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSIsLNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753301  720 QSLEALGPINASLIIMVLAQ---AELPALHYRFNAP 752
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 ...
 403-471 2.14e-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: 74.30  E-value: 2.14e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753301  403 PGQAYDADEQCRFQHGVKSRQCKYGE--VCSELWC-LSKSNRCITNSIPAAEGTLCqthtIDKGWCYKRVCV 471
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 174-387 4.41e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 69.69  E-value: 4.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  174 YVETLVVADKMMVAYHGR-RDVEQYVLAIMNIVAKLFQDSSLGNIvNILVTRLILLTEDQPTLEITHHAGKSLDSfckwQ 252
Cdd:cd04272      2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLKSPRI-RLLLVGITISKDPDFEPYIHPINYGYIDA----A 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  253 KSIVSHSGHgnAIPENGVANHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSINEDigLATAF----TIAH 326
Cdd:cd04272     77 ETLENFNEY--VKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753301  327 EIGHTFGMNHDG---VGNGCGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 387
Cdd:cd04272    152 ELAHLLGAPHDGsppPSWVKGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 269-379 7.96e-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: 7.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  269 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSINED---IGLATAFTIAHEIGHTFGMNHDGVGNGC-- 343
Cdd:cd00203     48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039753301  344 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 379
Cdd:cd00203    122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 541-639 1.24e-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: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  541 DFREMQCSEFDSVPFR-----GKFYTWKTY--RGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPD------TVDICV 607
Cdd:pfam19236    4 EFMSQQCARTDGQPLRsspggASFYHWGAAvpHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039753301  608 SGECKHVGCDRVLGSDLREDKCRVCGGDGSAC 639
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 882-936 1.42e-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: 63.24  E-value: 1.42e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039753301  882 WATLDWSECTPSCGPGLRHRVVLCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRC 936
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 822-878 7.25e-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: 61.31  E-value: 7.25e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753301  822 WVVGNWSRCSRSCDAGVRSRSVVCQRRVSAAEEkalDDSAC-PQPRPPVLEACQGPMC 878
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIV---PDSECsAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 763-818 4.78e-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: 4.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  763 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSSAVAPHYCSGHSKlPKRQRACNTEPC 818
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKK-PPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
178-337 5.24e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 5.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  178 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSlgNIvNILVTRLILLTEDQPTleiTHHAGKSLDSFCKWQKSIVS 257
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF--NI-SLGLVNLTISDSTCPY---TPPACSTGDSSDRLSEFQDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  258 HSghgnaipENGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSINEDIGLA--------TAFTIAHEIG 329
Cdd:pfam13688   82 SA-------WRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146


                   ....*...
gi 1039753301  330 HTFGMNHD 337
Cdd:pfam13688  147 HNFGAVHD 154
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 293-379 2.78e-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: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  293 GTLGLAPVGGMCERERSCsINEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NGCGARGQDPA 351
Cdd:pfam13574   85 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 163

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1039753301  352 K---LMAAhiTMKTNPFVWSSCSRDYITSFL 379
Cdd:pfam13574  164 NgsfIMNP--ASKSNNDLFSPCSISLICDVL 192
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 941-990 3.61e-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: 53.61  E-value: 3.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301  941 WVTSEWGECSTQCGLGQQQRTVRCT---SHTGQPSRECTEALRPSTMQQCEAK 990
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPDSECSAQKKPPETQSCNLK 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 197-337 1.78e-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: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  197 YVLAIMNIVAKLFQ-DSSLG-NIVNILVTRLilltEDQPTLEIThhAGKSLDSFckwQKSIVSHSGHGNAipengvanhD 274
Cdd:pfam13582    2 RIVSLVNRANTIYErDLGIRlQLAAIIITTS----ADTPYTSSD--ALEILDEL---QEVNDTRIGQYGY---------D 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753301  275 TAVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSINEDI---GLATAFTIAHEIGHTFGMNHD 337
Cdd:pfam13582   64 LGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1004-1036 2.87e-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: 2.87e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039753301 1004 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTCQ 1036
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYRQFCCRSCS 31
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 173-375 1.63e-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: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  173 RYVETLVVADKMMVAYHGRRD-VEQYVLAIMNIVAKLFQdSSLGNIVNILVTRLILLTEDQPTLEITHHAGK-----SLD 246
Cdd:pfam13583    3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVYG-RDFNVSLALISDRDVIYTDSSTDSFNADCSGGdlgnwRLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  247 SFCKWQksivshsghgnaipenGVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERScsiNEDIGLATAFT--- 323
Cdd:pfam13583   82 TLTSWR----------------DSLNYDLAYLTLMT------GPSGQNVGVAWVGALCSSARQ---NAKASGVARSRdew 136

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753301  324 --IAHEIGHTFGMNHDGVGNGCGARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 375
Cdd:pfam13583  137 diFAHEIGHTFGAVHDCSSQGEGLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 178-386 1.69e-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: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  178 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKL--------FQDSSLGNIvNILVTRLILLTEDQPTleithhagksldsfc 249
Cdd:cd04270      6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKGI-GFQIKRIRIHTTPDEV--------------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  250 kwqksiVSHSGHGNAIPEN-GVANHDTAVLITRY--DICI-----YKNKPCGTLGLAPV--------GGMCERE------ 307
Cdd:cd04270     70 ------DPGNKFYNKSFPNwGVEKFLVKLLLEQFsdDVCLahlftYRDFDMGTLGLAYVgsprdnsaGGICEKAyyysng 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  308 RSCSINedIGLATAF-------------TIAHEIGHTFGMNHDGVGNGCGARGQDPAK-LMAAHITM--KTNPFVWSSCS 371
Cdd:cd04270    144 KKKYLN--TGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGESQGGNyIMYARATSgdKENNKKFSPCS 221

                          250
                   ....*....|....*
gi 1039753301  372 RDYITSFLDSGLGLC 386
Cdd:cd04270    222 KKSISKVLEVKSNSC 236
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 80-114 2.58e-05

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: 44.61  E-value: 2.58e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1039753301   80 HGLIVADDEEYLIEPLqggpKGHRGPEESGPHVVY 114
Cdd:pfam01562   98 RGFIRTENEEYLIEPL----EKYSREEGGHPHVVY 128
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 804-939 3.66e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 46.78  E-value: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753301  804 SKLPKRQRACNTEPCPPDWVVGNWSR-----CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleacQGPMC 878
Cdd:PHA02682    27 TKCPQATIPAPAAPCPPDADVDPLDKysvkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP------ACPAC 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753301  879 PPewATLDWSECTPSCGPGlrhrvvlCKSADQRSTLPPGHCLPAAKPPSTMRCNLRRCPPA 939
Cdd:PHA02682    99 AP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 484-536 5.68e-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: 5.68e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1039753301   484 WGPWTPWGDCSRSCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTNDCP 536
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 763-819 1.19e-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: 1.19e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753301   763 WHYAPWTKCSAQCAGGSQVQVVECRNQLDSsaVAPHYCSGHSklpKRQRACNTEPCP 819
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ--NGGGPCTGED---VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 941-988 1.49e-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: 1.49e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1039753301   941 WVTSEWGECSTQCGLGQQQRTVRCTSHTGQ-PSRECTEAL---RPSTMQQCE 988
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDvetRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
942-987 4.15e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 4.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039753301  942 VTSEWGECSTQCGLGQQQRTVRC--TSHTGQPSRECTEALRPSTMQQC 987
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCksPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 886-937 6.23e-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: 6.23e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1039753301   886 DWSECTPSCGPGLRHRVVLCKSADQRstLPPGHCLPAAkpPSTMRCNLRRCP 937
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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