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Conserved domains on  [gi|1034663648|ref|XP_016869722|]
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A disintegrin and metalloproteinase with thrombospondin motifs 13 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 311-425 4.46e-74

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: 241.15  E-value: 4.46e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  311 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 390
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034663648  391 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 425
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 1-153 1.71e-63

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.


The actual alignment was detected with superfamily member cd04273:

Pssm-ID: 469599  Cd Length: 207  Bit Score: 214.79  E-value: 1.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648    1 MVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLI 80
Cdd:cd04273     53 LIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSI 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663648   81 TEDTGFDLGVTIAHEIGHSFGLEHDGApGSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 153
Cdd:cd04273    133 NEDTGLSSAFTIAHELGHVLGMPHDGD-GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 427-550 9.49e-51

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: 174.30  E-value: 9.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  427 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 505
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034663648  506 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 550
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 171-241 1.34e-17

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: 78.16  E-value: 1.34e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  171 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 241
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 257-309 3.00e-14

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: 68.00  E-value: 3.00e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034663648   257 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 309
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 946-1000 1.81e-10

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: 57.46  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034663648  946 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 825-882 6.24e-08

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: 50.14  E-value: 6.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  825 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 882
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 616-674 5.50e-07

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: 47.83  E-value: 5.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  616 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 674
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-942 6.82e-07

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: 47.45  E-value: 6.82e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663648  886 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 942
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 772-821 1.02e-03

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: 38.59  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034663648  772 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 821
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 311-425 4.46e-74

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: 241.15  E-value: 4.46e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  311 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 390
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034663648  391 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 425
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-153 1.71e-63

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: 214.79  E-value: 1.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648    1 MVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLI 80
Cdd:cd04273     53 LIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSI 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663648   81 TEDTGFDLGVTIAHEIGHSFGLEHDGApGSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 153
Cdd:cd04273    133 NEDTGLSSAFTIAHELGHVLGMPHDGD-GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 427-550 9.49e-51

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: 174.30  E-value: 9.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  427 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 505
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034663648  506 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 550
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 171-241 1.34e-17

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: 78.16  E-value: 1.34e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  171 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 241
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 257-309 3.00e-14

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: 68.00  E-value: 3.00e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034663648   257 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 309
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 12-156 1.40e-10

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: 62.32  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   12 NITANLTSSLLSVCGWSQT-INPEDDTDpgHADLVLYITrfdlelPDGNRQvrGVTQLGGACSPTWSCLITEDTGFD--- 87
Cdd:pfam01421   61 DVSGDANDTLRNFLKWRQEyLKKRKPHD--VAQLLSGVE------FGGTTV--GAAYVGGMCSLEYSGGVNEDHSKNles 130

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663648   88 LGVTIAHEIGHSFGLEHD-GAPGSGCGPSGH-VM-ASDGAAPraGLAWSPCSRRQLLSLLSAGRARCVWDPP 156
Cdd:pfam01421  131 FAVTMAHELGHNLGMQHDdFNGGCKCPPGGGcIMnPSAGSSF--PRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 946-1000 1.81e-10

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: 57.46  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034663648  946 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
258-308 2.93e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  258 SSWGPRSPCSRSCGGGVVTRRRQCNNPRPafGGRACVGADLQAEMCNTQAC 308
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 825-882 6.24e-08

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: 50.14  E-value: 6.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  825 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 882
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 616-674 5.50e-07

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: 47.83  E-value: 5.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  616 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 674
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-942 6.82e-07

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: 47.45  E-value: 6.82e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663648  886 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 942
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 772-821 1.02e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.59  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034663648  772 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 821
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 311-425 4.46e-74

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: 241.15  E-value: 4.46e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  311 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 390
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034663648  391 LCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 425
Cdd:pfam19236   81 LCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-153 1.71e-63

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: 214.79  E-value: 1.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648    1 MVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLI 80
Cdd:cd04273     53 LIVLEDEESGLLISGNAQKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSI 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663648   81 TEDTGFDLGVTIAHEIGHSFGLEHDGApGSGCGPS---GHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVW 153
Cdd:cd04273    133 NEDTGLSSAFTIAHELGHVLGMPHDGD-GNSCGPEgkdGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 427-550 9.49e-51

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: 174.30  E-value: 9.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648  427 PRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVR-IGGRYVVAGKMSISPNTTYPSLLEDGrVEYRValted 505
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKnVQGKYILNGKGSISLNPTYPSLLGTV-LEYRR----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034663648  506 RLPRLEEIRIWGPLQEDADIQVYRRYGEeygnLTRPDITFTYFQP 550
Cdd:pfam05986   75 SLPALEELHAPGPTQEDLEIQVLRQYGK----GTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 171-241 1.34e-17

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: 78.16  E-value: 1.34e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  171 PGLYYSANEQCRVAFGPKAVACTFAREhlDMCQALSCHTDplDQSSCSRLLVPLLDGTECGVEKWCSKGRC 241
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGDE--DVCSKLWCSNP--GGSTCTTKNLPAADGTPCGNKKWCLNGKC 67
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 1-139 5.18e-17

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: 80.54  E-value: 5.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648    1 MVILTEPEGAPNITANLTSSLLSVCGWSQTinpeddtDPGHADLVLYITRFDLELPDGNrqvrGVTQLGGACSPTWSCLI 80
Cdd:cd04267     55 LQILKGEQFAPPIDSDASNTLNSFSFWRAE-------GPIRHDNAVLLTAQDFIEGDIL----GLAYVGSMCNPYSSVGV 123

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663648   81 TEDTGFDL--GVTIAHEIGHSFGLEHDGAP---GSGCGPSGHVMA--SDGAAPRaglAWSPCSRRQ 139
Cdd:cd04267    124 VEDTGFTLltALTMAHELGHNLGAEHDGGDelaFECDGGGNYIMApvDSGLNSY---RFSQCSIGS 186
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 257-309 3.00e-14

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: 68.00  E-value: 3.00e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034663648   257 WSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACE 309
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 64-154 1.08e-13

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: 71.11  E-value: 1.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   64 GVTQLGGACSPTWSCLITEDTG---FDLGVTIAHEIGHSFGLEHDGaPGSGCGPSGHVMASDGAAPRagLAWSPCSRRQL 140
Cdd:cd04269    104 GLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDD-GGCTCGRSTCIMAPSPSSLT--DAFSNCSYEDY 180

                           90
                   ....*....|....
gi 1034663648  141 LSLLSAGRARCVWD 154
Cdd:cd04269    181 QKFLSRGGGQCLLN 194
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 37-151 2.80e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 70.46  E-value: 2.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   37 TDPGHADLVLYITRFDLELPDG---NRQVRGVTQLGGACSpTWSCLITEDT-GFDLGV-TIAHEIGHSFGLEHDGAPGSG 111
Cdd:cd04272     90 RDYFNPDVVFLVTGLDMSTYSGgslQTGTGGYAYVGGACT-ENRVAMGEDTpGSYYGVyTMTHELAHLLGAPHDGSPPPS 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  112 -CGPS----------GHVMASDGAAPRaGLAWSPCSRRQLLSLLSAGRARC 151
Cdd:cd04272    169 wVKGHpgsldcpwddGYIMSYVVNGER-QYRFSQCSQRQIRNVFRRLGASC 218
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 12-156 1.40e-10

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: 62.32  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   12 NITANLTSSLLSVCGWSQT-INPEDDTDpgHADLVLYITrfdlelPDGNRQvrGVTQLGGACSPTWSCLITEDTGFD--- 87
Cdd:pfam01421   61 DVSGDANDTLRNFLKWRQEyLKKRKPHD--VAQLLSGVE------FGGTTV--GAAYVGGMCSLEYSGGVNEDHSKNles 130

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663648   88 LGVTIAHEIGHSFGLEHD-GAPGSGCGPSGH-VM-ASDGAAPraGLAWSPCSRRQLLSLLSAGRARCVWDPP 156
Cdd:pfam01421  131 FAVTMAHELGHNLGMQHDdFNGGCKCPPGGGcIMnPSAGSSF--PRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 946-1000 1.81e-10

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: 57.46  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034663648  946 WHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
258-308 2.93e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  258 SSWGPRSPCSRSCGGGVVTRRRQCNNPRPafGGRACVGADLQAEMCNTQAC 308
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 825-882 6.24e-08

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: 50.14  E-value: 6.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  825 WQY-KLAACSVSCGRGVVRRILYCARAHgeddGEEILLDTQCQGLPRPEPQEACSLEPC 882
Cdd:pfam19030    1 WVAgPWGECSVTCGGGVQTRLVQCVQKG----GGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 616-674 5.50e-07

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: 47.83  E-value: 5.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648  616 WAVGDFGPCSASCGGGLRERPVRCVEAQGslLKTLPPARCraGAQQPAVALETCNPQPC 674
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGG--GSIVPDSEC--SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-942 6.82e-07

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: 47.45  E-value: 6.82e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663648  886 WKVMSLGPCSASCGLGTARRSVACVQLDqGQDVEVDEaACAALVRPEASVPCLIADC 942
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKG-GGSIVPDS-ECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 36-113 7.57e-07

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: 50.60  E-value: 7.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   36 DTDPGHADLVLYITRFDLELPDGnrqvrGVTQLGGACSPTWSCLITEDTGFD---LGVTIAHEIGHSFGLEHDGAPGSGC 112
Cdd:cd00203     46 GVEIDKADIAILVTRQDFDGGTG-----GWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRD 120


                   .
gi 1034663648  113 G 113
Cdd:cd00203    121 D 121
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 258-308 5.70e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 44.58  E-value: 5.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034663648  258 SSWGPRSPCSRSCGGGVVTRRRQCNNPrPAFGGRACvGADLQAEMCNTQAC 308
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 90-151 1.04e-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: 48.52  E-value: 1.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   90 VTIAHEIGHSFGLEHDgAPGSGCGPSG-----HVM---ASDGAAPRAGLaWSPCSRRQLLSLLSAGRARC 151
Cdd:cd04270    169 LVTAHELGHNFGSPHD-PDIAECAPGEsqggnYIMyarATSGDKENNKK-FSPCSKKSISKVLEVKSNSC 236
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 42-105 5.09e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 44.28  E-value: 5.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663648   42 ADLVLYITRFDlelpdgNRQVRGVTQLGGACSPTWSCLITEDTG--FDLGV-TIAHEIGHSFGLEHD 105
Cdd:pfam13582   62 YDLGHLFTGRD------GGGGGGIAYVGGVCNSGSKFGVNSGSGpvGDTGAdTFAHEIGHNFGLNHT 122
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 2-138 5.62e-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: 45.69  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648    2 VILTEPEGAPnitANLTSSLLSVCGWSQ-TINPEDDTDpgHADLVLYITRFDlelpdGNRQVRGVTQLGGACSPTW---- 76
Cdd:pfam13583   56 VIYTDSSTDS---FNADCSGGDLGNWRLaTLTSWRDSL--NYDLAYLTLMTG-----PSGQNVGVAWVGALCSSARqnak 125

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663648   77 -SCLITEDTGFDlgvTIAHEIGHSFGLEHDGApGSGCGPSGHVMASDG------AAPRAGLAWSPCSRR 138
Cdd:pfam13583  126 aSGVARSRDEWD---IFAHEIGHTFGAVHDCS-SQGEGLSSSTEDGSGqtimsyASTASQTAFSPCTIR 190
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 64-145 1.05e-04

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 44.54  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   64 GVTQLGGACSPTWSCLITED---TGFDLGVT---------IAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAG-- 129
Cdd:pfam13574   88 GLAYVGQICQKGASSPKTNTglsTTTNYGSFnyptqewdvVAHEVGHNFGATHDCDGSQYASSGCERNAATSVCSANGsf 167

                           90       100
                   ....*....|....*....|....*.
gi 1034663648  130 LAW----------SPCSRRQLLSLLS 145
Cdd:pfam13574  168 IMNpasksnndlfSPCSISLICDVLG 193
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
30-124 2.17e-04

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 43.56  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663648   30 TINPEDDTDPGHA----DLVLYITRFDLELPDGNRQV--------------RGVTQLGGACSPTWSCLITEDTGFDLGV- 90
Cdd:pfam13688   53 TISDSTCPYTPPAcstgDSSDRLSEFQDFSAWRGTQNddlaylflmtncsgGGLAWLGQLCNSGSAGSVSTRVSGNNVVv 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034663648   91 -------TIAHEIGHSFGLEHD--GAPGSGCGPSGHVMASDGA 124
Cdd:pfam13688  133 statewqVFAHEIGHNFGAVHDcdSSTSSQCCPPSNSTCPAGG 175
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 81-110 5.30e-04

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 41.81  E-value: 5.30e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034663648   81 TEDTGFDLGVTIAHEIGHSFGLEHDGAPGS 110
Cdd:cd04278    100 SDSGGTDLFSVAAHEIGHALGLGHSSDPDS 129
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 772-821 1.02e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.59  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034663648  772 GSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPgSRREVCQAVPC 821
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 86-113 4.52e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 40.02  E-value: 4.52e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034663648   86 FDLGVTIAHEIGHSFGLEH---DGAPGSGCG 113
Cdd:cd04275    135 YNLGDTATHEVGHWLGLYHtfqGGSPCCTTG 165
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 75-110 4.93e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 39.14  E-value: 4.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1034663648   75 TWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGS 110
Cdd:pfam00413   95 TWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGA 130
 
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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