NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|28316229|emb|CAD56159|]
View 

ADAMTS-20 protein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1710-1907 3.79e-102

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


:

Pssm-ID: 462559  Cd Length: 200  Bit Score: 325.72  E-value: 3.79e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1710 FTTCKEIQVKNHIRKDGDYYLNIKGRIIKIYCADMYLENPKEYLTLVQGE-ENFSEVYGFRLKNPYQCPFNGSRREDCEC 1788
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPSGPqENYSEVYGYRLKNPNECPFNGSRRDDCAC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1789 DNGHLA-AGYTVFSKIRIDLTSMQIKATDLLFSKTIFGNAVPFATAGDCYSAFRCPQGQFSINLSGTGMKISSTAKWLTQ 1867
Cdd:pfam08685   81 RQDYPAnAGTTTFSKVRLDLTSLRIITNDFTFARTIRGKPVPFGTAGDCYSAAKCPQGRFSINLTGTGLRVSPDTKWVSQ 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 28316229   1868 GSYTSVSIRRSQDGTRFFGKCGGYCGKCLPHMTTGLPIQV 1907
Cdd:pfam08685  161 GNYAVSKIHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 259-464 5.65e-97

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: 311.09  E-value: 5.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVV-SAHGSNLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINFDGATTLKNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVeFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  338 QTQNDLDDVHPSHHDTAVLITRYDICSSKEKCNMLGLSYLGTICDPLQSCFINEEKGLISAFTIAHELGHTLGVQHDDN- 416
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 28316229  417 PRCKEmKVTKYHVMAPALSFHMSPWSWSNCSRKYVTEFLETGYGECLL 464
Cdd:cd04273  161 NSCGP-EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-186 2.15e-35

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 131.67  E-value: 2.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229     41 EVVIPERVNEFgevfpqshhfsRQKRSSEALEPMPFRTHYRFTAYGQLFQLNLTADASFLAAGYTEVHLGTPERGaWESD 120
Cdd:pfam01562    1 EVVIPVRLDPS-----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG-VESP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28316229    121 AGPSDlrHCFYRGQVNSQEDYKAVVSLCGGLVGTFKGQNGEYFLEPIMKadgnEYEDGHNKPHLIY 186
Cdd:pfam01562   69 PVQTD--HCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEK----YSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 722-838 3.64e-30

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: 116.14  E-value: 3.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    722 TITGVFNSSH-YGYNVVVKIPAGATNVDIRQYSYSGqpddSYLALSDAEGNFLFNGNFLLSTSKKEINVQGTVIEYSGSN 800
Cdd:pfam05986    1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRSL 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 28316229    801 NAVERINSTNRQEKEILIEVLCV-GNLYNPDVHYSFNIP 838
Cdd:pfam05986   77 PALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 479-546 2.03e-18

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: 80.85  E-value: 2.03e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    479 PGSRYDGNKQCELAFGPGSQMCPHI--NICMHLWCTSTEKlhKGCFTQHVPPADGTDCGPGMHCRHGLCV 546
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1360-1413 2.48e-14

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: 69.02  E-value: 2.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1360 WNYGNWGECSQTCGGGIKSRLVICQFPNGQILE-DHNCEIVNKPPSVIQCHMHAC 1413
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1078-1132 1.67e-13

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.71  E-value: 1.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1078 WQVGPWGPCTTTCGHGYQMRDVKCVNELASAVLEDTECHEASRPSDRQSCVLTPC 1132
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1306-1357 2.25e-13

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.32  E-value: 2.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1306 WRTGPWGQCSSSCSGGLQHRAVVCQDENGQSA---SYCDAASKPPELQQCGPGPC 1357
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvpdSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 559-611 2.50e-12

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: 63.37  E-value: 2.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 28316229     559 WGPWEPYSSCSRTCGGGIESATRRCNRPEPRNGGNYCVGRRMKFRSCNTDSCP 611
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1419-1472 9.45e-11

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 58.62  E-value: 9.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1419 WHQEPWTSCSASCGKGRKYREVFCIDQFQRKLE-DTNCSQVQKPPTHKACRSVRC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1528 2.28e-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: 57.85  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1475 WKANSWNECSVTCGSGVQQRDVYCRLKGVGQVV-EEMCDQSTRPCSQRRCWSQDC 1528
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1209-1261 9.05e-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: 55.92  E-value: 9.05e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1209 WQAGDWSPCSASCGHGKTTRQVLCMNYH--QPIDENYCDPEVRPLMEQECSLAAC 1261
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1154-1206 6.60e-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: 6.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1154 WRHGSWTPCSVSCGRGTQARYVSCRDALDRIA-DESYCAHLPRPAEIWDCFT-PC 1206
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKPPETQSCNLkPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1023-1075 1.03e-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: 52.84  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1023 WAASEWSECLVTCGKGTKQRQVWCQLNVDHL--SDGFCNSSTKPESLSPCELHTC 1075
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 616-720 1.11e-08

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: 55.10  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    616 DFREKQCSDFNGKHLDIS-GIPSNVRWLPRYSGVGTKDRCKLYCQVAGTNYFYLLKDMVEDGTPCGTE------THDICV 688
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 28316229    689 QGQCMAAGCDHVLNSSAKIDKCGVCGGDNSSC 720
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1656-1707 2.14e-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: 52.07  E-value: 2.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1656 WKVGKWSKCSVTCGIGIMKRQVKCITKHGLS---SDLCLNHLKPGAQKKCYANDC 1707
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 848-899 3.73e-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: 51.30  E-value: 3.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    848 WDpYGPWEGCTKMC-QGLQRRNITCIHKSDHSVVSDKECDHLPLPSfVTQSCN 899
Cdd:pfam19030    1 WV-AGPWGECSVTCgGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCN 51
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 968-1020 6.21e-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: 50.91  E-value: 6.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229    968 WHYSEWSQCSRSCGGGERSRESYCMNNFGHRL-ADNECQELSR-VTRENCNEFSC 1020
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKpPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 908-959 9.19e-04

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: 38.97  E-value: 9.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    908 VIGK-SECSSQCGQGYRTLDIHCMKYSIHEGqtvqVDDHYCGDQLKPPTQELC 959
Cdd:pfam19030    2 VAGPwGECSVTCGGGVQTRLVQCVQKGGGSI----VPDSECSAQKKPPETQSC 50
 
Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1710-1907 3.79e-102

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


Pssm-ID: 462559  Cd Length: 200  Bit Score: 325.72  E-value: 3.79e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1710 FTTCKEIQVKNHIRKDGDYYLNIKGRIIKIYCADMYLENPKEYLTLVQGE-ENFSEVYGFRLKNPYQCPFNGSRREDCEC 1788
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPSGPqENYSEVYGYRLKNPNECPFNGSRRDDCAC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1789 DNGHLA-AGYTVFSKIRIDLTSMQIKATDLLFSKTIFGNAVPFATAGDCYSAFRCPQGQFSINLSGTGMKISSTAKWLTQ 1867
Cdd:pfam08685   81 RQDYPAnAGTTTFSKVRLDLTSLRIITNDFTFARTIRGKPVPFGTAGDCYSAAKCPQGRFSINLTGTGLRVSPDTKWVSQ 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 28316229   1868 GSYTSVSIRRSQDGTRFFGKCGGYCGKCLPHMTTGLPIQV 1907
Cdd:pfam08685  161 GNYAVSKIHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 259-464 5.65e-97

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: 311.09  E-value: 5.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVV-SAHGSNLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINFDGATTLKNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVeFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  338 QTQNDLDDVHPSHHDTAVLITRYDICSSKEKCNMLGLSYLGTICDPLQSCFINEEKGLISAFTIAHELGHTLGVQHDDN- 416
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 28316229  417 PRCKEmKVTKYHVMAPALSFHMSPWSWSNCSRKYVTEFLETGYGECLL 464
Cdd:cd04273  161 NSCGP-EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-186 2.15e-35

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 131.67  E-value: 2.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229     41 EVVIPERVNEFgevfpqshhfsRQKRSSEALEPMPFRTHYRFTAYGQLFQLNLTADASFLAAGYTEVHLGTPERGaWESD 120
Cdd:pfam01562    1 EVVIPVRLDPS-----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG-VESP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28316229    121 AGPSDlrHCFYRGQVNSQEDYKAVVSLCGGLVGTFKGQNGEYFLEPIMKadgnEYEDGHNKPHLIY 186
Cdd:pfam01562   69 PVQTD--HCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEK----YSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 722-838 3.64e-30

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: 116.14  E-value: 3.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    722 TITGVFNSSH-YGYNVVVKIPAGATNVDIRQYSYSGqpddSYLALSDAEGNFLFNGNFLLSTSKKEINVQGTVIEYSGSN 800
Cdd:pfam05986    1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRSL 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 28316229    801 NAVERINSTNRQEKEILIEVLCV-GNLYNPDVHYSFNIP 838
Cdd:pfam05986   77 PALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 259-467 4.07e-27

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: 110.47  E-value: 4.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    259 RYIEIMVTADAKVVSAHGSNL---QNYILTLMSIVATIYKDPSIgnliHIVVVKLvMIHREEEGPVINFDGATTLKNFCS 335
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNI----RVVLVGL-EIWTDEDKIDVSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    336 WQQTQNdlddVHPSHHDTAVLITRYDICSSKEkcnmlGLSYLGTICDPLQSCFINE---EKGLISAFTIAHELGHTLGVQ 412
Cdd:pfam01421   76 WRQEYL----KKRKPHDVAQLLSGVEFGGTTV-----GAAYVGGMCSLEYSGGVNEdhsKNLESFAVTMAHELGHNLGMQ 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28316229    413 HDDNPR---CKEMKVTkyhVMAPALSfHMSPWSWSNCSRKYVTEFLETGYGECLLDKP 467
Cdd:pfam01421  147 HDDFNGgckCPPGGGC---IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 479-546 2.03e-18

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: 80.85  E-value: 2.03e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    479 PGSRYDGNKQCELAFGPGSQMCPHI--NICMHLWCTSTEKlhKGCFTQHVPPADGTDCGPGMHCRHGLCV 546
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1360-1413 2.48e-14

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: 69.02  E-value: 2.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1360 WNYGNWGECSQTCGGGIKSRLVICQFPNGQILE-DHNCEIVNKPPSVIQCHMHAC 1413
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1078-1132 1.67e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.71  E-value: 1.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1078 WQVGPWGPCTTTCGHGYQMRDVKCVNELASAVLEDTECHEASRPSDRQSCVLTPC 1132
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1306-1357 2.25e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.32  E-value: 2.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1306 WRTGPWGQCSSSCSGGLQHRAVVCQDENGQSA---SYCDAASKPPELQQCGPGPC 1357
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvpdSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 559-611 2.50e-12

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: 63.37  E-value: 2.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 28316229     559 WGPWEPYSSCSRTCGGGIESATRRCNRPEPRNGGNYCVGRRMKFRSCNTDSCP 611
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1419-1472 9.45e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 58.62  E-value: 9.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1419 WHQEPWTSCSASCGKGRKYREVFCIDQFQRKLE-DTNCSQVQKPPTHKACRSVRC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1528 2.28e-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: 57.85  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1475 WKANSWNECSVTCGSGVQQRDVYCRLKGVGQVV-EEMCDQSTRPCSQRRCWSQDC 1528
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1209-1261 9.05e-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: 55.92  E-value: 9.05e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1209 WQAGDWSPCSASCGHGKTTRQVLCMNYH--QPIDENYCDPEVRPLMEQECSLAAC 1261
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1154-1206 6.60e-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: 6.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1154 WRHGSWTPCSVSCGRGTQARYVSCRDALDRIA-DESYCAHLPRPAEIWDCFT-PC 1206
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKPPETQSCNLkPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1023-1075 1.03e-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: 52.84  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1023 WAASEWSECLVTCGKGTKQRQVWCQLNVDHL--SDGFCNSSTKPESLSPCELHTC 1075
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 616-720 1.11e-08

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: 55.10  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    616 DFREKQCSDFNGKHLDIS-GIPSNVRWLPRYSGVGTKDRCKLYCQVAGTNYFYLLKDMVEDGTPCGTE------THDICV 688
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 28316229    689 QGQCMAAGCDHVLNSSAKIDKCGVCGGDNSSC 720
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1656-1707 2.14e-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: 52.07  E-value: 2.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1656 WKVGKWSKCSVTCGIGIMKRQVKCITKHGLS---SDLCLNHLKPGAQKKCYANDC 1707
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 848-899 3.73e-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: 51.30  E-value: 3.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    848 WDpYGPWEGCTKMC-QGLQRRNITCIHKSDHSVVSDKECDHLPLPSfVTQSCN 899
Cdd:pfam19030    1 WV-AGPWGECSVTCgGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 968-1020 6.21e-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: 50.91  E-value: 6.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229    968 WHYSEWSQCSRSCGGGERSRESYCMNNFGHRL-ADNECQELSR-VTRENCNEFSC 1020
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1206-1262 1.24e-07

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: 49.89  E-value: 1.24e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 28316229    1206 CGEWqaGDWSPCSASCGHGKTTRQVLCMNYHQPIDENYCDPEVRplMEQECSLAACP 1262
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 968-1021 9.23e-07

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: 47.58  E-value: 9.23e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 28316229     968 WHYSEWSQCSRSCGGGERSRESYCmNNFGHRLADNECQELSRVTREnCNEFSCP 1021
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTGEDVETRA-CNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
560-610 8.20e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 8.20e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28316229    560 GPWEPYSSCSRTCGGGIESATRRCNRPEPrnGGNYCVGRRMKFRSCNTDSC 610
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 249-427 4.25e-04

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 44.95  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    249 SRKKRLISYPRYIEIMVTADAKvvsahGSNLQNYILTLMSIVATIYKDPsigNLIHIVVVKLVMihrEEEGPVINFDGAT 328
Cdd:TIGR03935  206 SQSRAVPSEPKTLYVILIREKG-----STGYPHEVTAQMQDAANSLKRL---VNNHFVLVEYTT---EYSCPSGGADESK 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    329 TLKNFCSWQQTqndlDDVHPSHHDTAVLITRYDICSSkekcNMLGLSYLGTICDPLQScfiNEEKGLISA------FTIA 402
Cdd:TIGR03935  275 GLDGFTASLKS----NPKAKGYDKQIYILIRWGTWDN----NILGIGWLNSYNVNTAS---NFEASGMSTtqlmypGTLA 343

                          170       180
                   ....*....|....*....|....*
gi 28316229    403 HELGHTLGVQHDDNPrcKEMKVTKY 427
Cdd:TIGR03935  344 HELGHILGAEHTDNE--KDLMYTWY 366
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1026-1075 5.70e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 5.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 28316229    1026 SEWSECLVTCGKGTKQRQVWCQLNVDHLSDGFCnSSTKPESlSPCELHTC 1075
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC-TGEDVET-RACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1360-1414 5.70e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 5.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229    1360 WNYGNWGECSQTCGGGIKSRLVICQFPNGQiLEDHNCEIVNkpPSVIQCHMHACP 1414
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1479-1523 6.87e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 6.87e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 28316229    1479 SWNECSVTCGSGVQQRDVYCrLKGVGQVVEEMC---DQSTRPCSQRRC 1523
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCtgeDVETRACNEQPC 52
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1206-1275 7.12e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 7.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28316229  1206 CGEWQagDWSPCSASCGHGKTTRQvlcmnyhQPIDENYCDPEvrplMEQECSLAACPPAHSHFP-SSPVQP 1275
Cdd:PTZ00441  240 CGPWD--EWTPCSVTCGKGTHSRS-------RPILHEGCTTH----MVEECEEEECPVEPEPLPvPAPVPP 297
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 908-959 9.19e-04

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: 38.97  E-value: 9.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    908 VIGK-SECSSQCGQGYRTLDIHCMKYSIHEGqtvqVDDHYCGDQLKPPTQELC 959
Cdd:pfam19030    2 VAGPwGECSVTCGGGVQTRLVQCVQKGGGSI----VPDSECSAQKKPPETQSC 50
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1306-1358 1.41e-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: 38.34  E-value: 1.41e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 28316229    1306 WRTGPWGQCSSSCSGGLQHRAVVCQDENGQ-SASYCDAASkpPELQQCGPGPCP 1358
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1078-1133 1.51e-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: 38.34  E-value: 1.51e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 28316229    1078 WQVGPWGPCTTTCGHGYQMRDVKCVNELASAvlEDTECHEASRpsDRQSCVLTPCS 1133
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN--GGGPCTGEDV--ETRACNEQPCP 53
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 389-445 1.64e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 40.80  E-value: 1.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 28316229     389 INEEKGLISAFTIAHELGHTLGVQHDDNP--RCKEMKVTKYHVMAPAlsFHMSPWSWSN 445
Cdd:smart00235   76 LSLGNGCINTGVAAHELGHALGLYHEQSRsdRDNYMYINYTNIDTRN--FDLSEDDSLG 132
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
343-435 1.83e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  343 LDDVHPSHHDTAVLITRYDICSskEKCN-MLGLSYLGTIC-----DPLQSCFI----NEEKGLISAFTIA-HELGHTLGV 411
Cdd:COG1913   60 LSRLKEEDGDKVLGVTDVDLYA--PGLNfVFGLAYLGGRVavvstARLRPEFYglppDEELFLERVLKEAvHELGHLFGL 137

                         90       100
                 ....*....|....*....|....
gi 28316229  412 QHDDNPRCkemkvtkyhVMAPALS 435
Cdd:COG1913  138 GHCPNPRC---------VMHFSNS 152
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1157-1180 1.93e-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: 37.95  E-value: 1.93e-03
                            10        20
                    ....*....|....*....|....
gi 28316229    1157 GSWTPCSVSCGRGTQARYVSCRDA 1180
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSP 28
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 401-419 5.09e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.01  E-value: 5.09e-03
                          10
                  ....*....|....*....
gi 28316229   401 IAHELGHTLGVQHDDNPRC 419
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRC 147
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
401-419 5.34e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 5.34e-03
                          10
                  ....*....|....*....
gi 28316229   401 IAHELGHTLGVQHDDNPRC 419
Cdd:NF033823  126 AVHELGHLLGLGHCPNPRC 144
 
Name Accession Description Interval E-value
GON pfam08685
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ...
 1710-1907 3.79e-102

GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.


Pssm-ID: 462559  Cd Length: 200  Bit Score: 325.72  E-value: 3.79e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1710 FTTCKEIQVKNHIRKDGDYYLNIKGRIIKIYCADMYLENPKEYLTLVQGE-ENFSEVYGFRLKNPYQCPFNGSRREDCEC 1788
Cdd:pfam08685    1 PRSCKEIQSRSGVRKDGEYTLNVRGRNVRIYCHGMNTSSPKEYLTLPSGPqENYSEVYGYRLKNPNECPFNGSRRDDCAC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229   1789 DNGHLA-AGYTVFSKIRIDLTSMQIKATDLLFSKTIFGNAVPFATAGDCYSAFRCPQGQFSINLSGTGMKISSTAKWLTQ 1867
Cdd:pfam08685   81 RQDYPAnAGTTTFSKVRLDLTSLRIITNDFTFARTIRGKPVPFGTAGDCYSAAKCPQGRFSINLTGTGLRVSPDTKWVSQ 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 28316229   1868 GSYTSVSIRRSQDGTRFFGKCGGYCGKCLPHMTTGLPIQV 1907
Cdd:pfam08685  161 GNYAVSKIHRSQDGTKVRGRCGGYCGKCTPSPGTGLLLDV 200
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 259-464 5.65e-97

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: 311.09  E-value: 5.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVV-SAHGSNLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINFDGATTLKNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVeFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  338 QTQNDLDDVHPSHHDTAVLITRYDICSSKEKCNMLGLSYLGTICDPLQSCFINEEKGLISAFTIAHELGHTLGVQHDDN- 416
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 28316229  417 PRCKEmKVTKYHVMAPALSFHMSPWSWSNCSRKYVTEFLETGYGECLL 464
Cdd:cd04273  161 NSCGP-EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 259-456 8.17e-44

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: 158.35  E-value: 8.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVVS---AHGSNLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINFDGATTLKNFCS 335
Cdd:cd04267    1 REIELVVVADHRMVSyfnSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  336 WQQTQndlddvhPSHHDTAVLITRYDICSSKEkcnmLGLSYLGTICDPLQSCFINEEKG--LISAFTIAHELGHTLGVQH 413
Cdd:cd04267   81 WRAEG-------PIRHDNAVLLTAQDFIEGDI----LGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEH 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 28316229  414 DDNPRCKEMKVT-KYHVMAPALSFhMSPWSWSNCSRKYVTEFLE 456
Cdd:cd04267  150 DGGDELAFECDGgGNYIMAPVDSG-LNSYRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-186 2.15e-35

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 131.67  E-value: 2.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229     41 EVVIPERVNEFgevfpqshhfsRQKRSSEALEPMPFRTHYRFTAYGQLFQLNLTADASFLAAGYTEVHLGTPERGaWESD 120
Cdd:pfam01562    1 EVVIPVRLDPS-----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG-VESP 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28316229    121 AGPSDlrHCFYRGQVNSQEDYKAVVSLCGGLVGTFKGQNGEYFLEPIMKadgnEYEDGHNKPHLIY 186
Cdd:pfam01562   69 PVQTD--HCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEK----YSREEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 259-465 3.86e-33

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: 127.73  E-value: 3.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVVSAHGSNL---QNYILTLMSIVATIYKdpSIGnlIHIVVVKLVMIHREEEGPVINfDGATTLKNFCS 335
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYR--PLN--IRVVLVGLEIWTDKDKISVSG-DAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  336 WQQTqnDLDDVHPshHDTAVLITRYDICSskekcNMLGLSYLGTICDPLQSCFINEEKG---LISAFTIAHELGHTLGVQ 412
Cdd:cd04269   76 WKRS--NLLPRKP--HDNAQLLTGRDFDG-----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 28316229  413 HDDN------PRCkemkvtkyhVMAPALSFHmsPWSWSNCSRKYVTEFLETGYGECLLD 465
Cdd:cd04269  147 HDDGgctcgrSTC---------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 722-838 3.64e-30

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: 116.14  E-value: 3.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    722 TITGVFNSSH-YGYNVVVKIPAGATNVDIRQYSYSGqpddSYLALSDAEGNFLFNGNFLLSTSKKEINVQGTVIEYSGSN 800
Cdd:pfam05986    1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRKPSF----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRSL 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 28316229    801 NAVERINSTNRQEKEILIEVLCV-GNLYNPDVHYSFNIP 838
Cdd:pfam05986   77 PALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 259-467 4.07e-27

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: 110.47  E-value: 4.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    259 RYIEIMVTADAKVVSAHGSNL---QNYILTLMSIVATIYKDPSIgnliHIVVVKLvMIHREEEGPVINFDGATTLKNFCS 335
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNI----RVVLVGL-EIWTDEDKIDVSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    336 WQQTQNdlddVHPSHHDTAVLITRYDICSSKEkcnmlGLSYLGTICDPLQSCFINE---EKGLISAFTIAHELGHTLGVQ 412
Cdd:pfam01421   76 WRQEYL----KKRKPHDVAQLLSGVEFGGTTV-----GAAYVGGMCSLEYSGGVNEdhsKNLESFAVTMAHELGHNLGMQ 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28316229    413 HDDNPR---CKEMKVTkyhVMAPALSfHMSPWSWSNCSRKYVTEFLETGYGECLLDKP 467
Cdd:pfam01421  147 HDDFNGgckCPPGGGC---IMNPSAG-SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 479-546 2.03e-18

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: 80.85  E-value: 2.03e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    479 PGSRYDGNKQCELAFGPGSQMCPHI--NICMHLWCTSTEKlhKGCFTQHVPPADGTDCGPGMHCRHGLCV 546
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 259-455 2.68e-16

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: 78.33  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  259 RYIEIMVTADAKVVsaHGSNLQNYILTLMSIVATIYKDPsigNLIHIVVVKLVmihreeegpvinfdgattlknfcswqq 338
Cdd:cd00203    1 KVIPYVVVADDRDV--EEENLSAQIQSLILIAMQIWRDY---LNIRFVLVGVE--------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  339 tqndlddvhPSHHDTAVLITRYDIcsskeKCNMLGLSYLGTICDPLQSCFINEEKGLIS---AFTIAHELGHTLGVQHDD 415
Cdd:cd00203   49 ---------IDKADIAILVTRQDF-----DGGTGGWAYLGRVCDSLRGVGVLQDNQSGTkegAQTIAHELGHALGFYHDH 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28316229  416 NPRCKEMKVT-----------KYHVMAPALSF--HMSPWSWSNCSRKYVTEFL 455
Cdd:cd00203  115 DRKDRDDYPTiddtlnaedddYYSVMSYTKGSfsDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1360-1413 2.48e-14

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: 69.02  E-value: 2.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1360 WNYGNWGECSQTCGGGIKSRLVICQFPNGQILE-DHNCEIVNKPPSVIQCHMHAC 1413
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1078-1132 1.67e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.71  E-value: 1.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1078 WQVGPWGPCTTTCGHGYQMRDVKCVNELASAVLEDTECHEASRPSDRQSCVLTPC 1132
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1306-1357 2.25e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 66.32  E-value: 2.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1306 WRTGPWGQCSSSCSGGLQHRAVVCQDENGQSA---SYCDAASKPPELQQCGPGPC 1357
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvpdSECSAQKKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 559-611 2.50e-12

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: 63.37  E-value: 2.50e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 28316229     559 WGPWEPYSSCSRTCGGGIESATRRCNRPEPRNGGNYCVGRRMKFRSCNTDSCP 611
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 260-463 2.89e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 68.15  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  260 YIEIMVTADAKVVSAHGSNLQ--NYILTLMSIVATIYKDPSIGNlIHIVVVKLVMIHREEEGPVI------NFDGATTLK 331
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYRDLKSPR-IRLLLVGITISKDPDFEPYIhpinygYIDAAETLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  332 NFCSWQQTQNdlddvHPSHHDTAVLITRYDICS---SKEKCNMLGLSYLGTICDPLQSCFINEEKGLIS-AFTIAHELGH 407
Cdd:cd04272   81 NFNEYVKKKR-----DYFNPDVVFLVTGLDMSTysgGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYgVYTMTHELAH 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28316229  408 TLGVQHDDNPRCKEMKVTKYHVMAPA-LSFHMS-------PWSWSNCSRKYVTEFLETGYGECL 463
Cdd:cd04272  156 LLGAPHDGSPPPSWVKGHPGSLDCPWdDGYIMSyvvngerQYRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1419-1472 9.45e-11

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 58.62  E-value: 9.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1419 WHQEPWTSCSASCGKGRKYREVFCIDQFQRKLE-DTNCSQVQKPPTHKACRSVRC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1528 2.28e-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: 57.85  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1475 WKANSWNECSVTCGSGVQQRDVYCRLKGVGQVV-EEMCDQSTRPCSQRRCWSQDC 1528
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1209-1261 9.05e-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: 55.92  E-value: 9.05e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1209 WQAGDWSPCSASCGHGKTTRQVLCMNYH--QPIDENYCDPEVRPLMEQECSLAAC 1261
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1154-1206 6.60e-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: 6.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1154 WRHGSWTPCSVSCGRGTQARYVSCRDALDRIA-DESYCAHLPRPAEIWDCFT-PC 1206
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKPPETQSCNLkPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1023-1075 1.03e-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: 52.84  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1023 WAASEWSECLVTCGKGTKQRQVWCQLNVDHL--SDGFCNSSTKPESLSPCELHTC 1075
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 616-720 1.11e-08

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: 55.10  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    616 DFREKQCSDFNGKHLDIS-GIPSNVRWLPRYSGVGTKDRCKLYCQVAGTNYFYLLKDMVEDGTPCGTE------THDICV 688
Cdd:pfam19236    4 EFMSQQCARTDGQPLRSSpGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCV 83

                           90       100       110
                   ....*....|....*....|....*....|..
gi 28316229    689 QGQCMAAGCDHVLNSSAKIDKCGVCGGDNSSC 720
Cdd:pfam19236   84 LGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
257-416 1.39e-08

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.66  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    257 YPRYIEIMVTADAKVVSAHGSN-LQNYILTLMSIVATIYKDPSigNlIHIVVVKLVMIHREEE---GPVINFDGATTLKN 332
Cdd:pfam13688    1 STRTVALLVAADCSYVAAFGGDaAQANIINMVNTASNVYERDF--N-ISLGLVNLTISDSTCPytpPACSTGDSSDRLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    333 FC---SWQQTQNDlddvhpshhDTAVLITRYDicsskekCNMLGLSYLGTICDPLQSCFINE----EKGLISA----FTI 401
Cdd:pfam13688   78 FQdfsAWRGTQND---------DLAYLFLMTN-------CSGGGLAWLGQLCNSGSAGSVSTrvsgNNVVVSTatewQVF 141

                          170
                   ....*....|....*
gi 28316229    402 AHELGHTLGVQHDDN 416
Cdd:pfam13688  142 AHEIGHNFGAVHDCD 156
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1656-1707 2.14e-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: 52.07  E-value: 2.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229   1656 WKVGKWSKCSVTCGIGIMKRQVKCITKHGLS---SDLCLNHLKPGAQKKCYANDC 1707
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 848-899 3.73e-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: 51.30  E-value: 3.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    848 WDpYGPWEGCTKMC-QGLQRRNITCIHKSDHSVVSDKECDHLPLPSfVTQSCN 899
Cdd:pfam19030    1 WV-AGPWGECSVTCgGGVQTRLVQCVQKGGGSIVPDSECSAQKKPP-ETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 968-1020 6.21e-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: 50.91  E-value: 6.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229    968 WHYSEWSQCSRSCGGGERSRESYCMNNFGHRL-ADNECQELSR-VTRENCNEFSC 1020
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIvPDSECSAQKKpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1206-1262 1.24e-07

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: 49.89  E-value: 1.24e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 28316229    1206 CGEWqaGDWSPCSASCGHGKTTRQVLCMNYHQPIDENYCDPEVRplMEQECSLAACP 1262
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 968-1021 9.23e-07

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: 47.58  E-value: 9.23e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 28316229     968 WHYSEWSQCSRSCGGGERSRESYCmNNFGHRLADNECQELSRVTREnCNEFSCP 1021
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTGEDVETRA-CNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
560-610 8.20e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 8.20e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28316229    560 GPWEPYSSCSRTCGGGIESATRRCNRPEPrnGGNYCVGRRMKFRSCNTDSC 610
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 557-610 2.93e-05

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 43.04  E-value: 2.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 28316229    557 GEWGPWepySSCSRTCGGGIESATRRCNRPePRNGGNYCvGRRMKFRSCNTDSC 610
Cdd:pfam19028    4 SEWSEW---SECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 282-414 4.65e-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: 44.67  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    282 YILTLMSIVATIY-KDPSIG-NLIHIVVVKLvmihreEEGPVINFDGATTLKNFCSWQQTQNDLDDVhpshhDTAVLITR 359
Cdd:pfam13582    2 RIVSLVNRANTIYeRDLGIRlQLAAIIITTS------ADTPYTSSDALEILDELQEVNDTRIGQYGY-----DLGHLFTG 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28316229    360 YDICSSkekcnmLGLSYLGTICDPLQSCFINEEK---GLISAFTIAHELGHTLGVQHD 414
Cdd:pfam13582   71 RDGGGG------GGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 278-456 7.69e-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: 372637  Cd Length: 193  Bit Score: 45.70  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    278 NLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINF-DGATT----LKNFCSWQQTQNDlddvhpshhD 352
Cdd:pfam13574    2 NVTENLVNVVNRVNQIYEPDDININGGLVNPGEIPATTSASDSGNNYcNSPTTivrrLNFLSQWRGEQDY---------C 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    353 TAVLITRYDiCSSKEkcnmLGLSYLGTICDPlQSCFINEEKGLISAFT-------------IAHELGHTLGVQHDDN--- 416
Cdd:pfam13574   73 LAHLVTMGT-FSGGE----LGLAYVGQICQK-GASSPKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDgsq 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 28316229    417 ---PRCKEMKVTK------YHVMAPA---LSFHMSPwswsnCSRKYVTEFLE 456
Cdd:pfam13574  147 yasSGCERNAATSvcsangSFIMNPAsksNNDLFSP-----CSISLICDVLG 193
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 249-427 4.25e-04

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 44.95  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    249 SRKKRLISYPRYIEIMVTADAKvvsahGSNLQNYILTLMSIVATIYKDPsigNLIHIVVVKLVMihrEEEGPVINFDGAT 328
Cdd:TIGR03935  206 SQSRAVPSEPKTLYVILIREKG-----STGYPHEVTAQMQDAANSLKRL---VNNHFVLVEYTT---EYSCPSGGADESK 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229    329 TLKNFCSWQQTqndlDDVHPSHHDTAVLITRYDICSSkekcNMLGLSYLGTICDPLQScfiNEEKGLISA------FTIA 402
Cdd:TIGR03935  275 GLDGFTASLKS----NPKAKGYDKQIYILIRWGTWDN----NILGIGWLNSYNVNTAS---NFEASGMSTtqlmypGTLA 343

                          170       180
                   ....*....|....*....|....*
gi 28316229    403 HELGHTLGVQHDDNPrcKEMKVTKY 427
Cdd:TIGR03935  344 HELGHILGAEHTDNE--KDLMYTWY 366
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1026-1075 5.70e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 5.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 28316229    1026 SEWSECLVTCGKGTKQRQVWCQLNVDHLSDGFCnSSTKPESlSPCELHTC 1075
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPC-TGEDVET-RACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1360-1414 5.70e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 5.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 28316229    1360 WNYGNWGECSQTCGGGIKSRLVICQFPNGQiLEDHNCEIVNkpPSVIQCHMHACP 1414
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1479-1523 6.87e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.49  E-value: 6.87e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 28316229    1479 SWNECSVTCGSGVQQRDVYCrLKGVGQVVEEMC---DQSTRPCSQRRC 1523
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCtgeDVETRACNEQPC 52
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1206-1275 7.12e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.57  E-value: 7.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28316229  1206 CGEWQagDWSPCSASCGHGKTTRQvlcmnyhQPIDENYCDPEvrplMEQECSLAACPPAHSHFP-SSPVQP 1275
Cdd:PTZ00441  240 CGPWD--EWTPCSVTCGKGTHSRS-------RPILHEGCTTH----MVEECEEEECPVEPEPLPvPAPVPP 297
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 908-959 9.19e-04

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: 38.97  E-value: 9.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28316229    908 VIGK-SECSSQCGQGYRTLDIHCMKYSIHEGqtvqVDDHYCGDQLKPPTQELC 959
Cdd:pfam19030    2 VAGPwGECSVTCGGGVQTRLVQCVQKGGGSI----VPDSECSAQKKPPETQSC 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
1480-1523 1.22e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.55  E-value: 1.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 28316229   1480 WNECSVTCGSGVQQRDVYCRLKGVGQVVEEMCDQSTRPCSQRRC 1523
Cdd:pfam00090    6 WSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1306-1358 1.41e-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: 38.34  E-value: 1.41e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 28316229    1306 WRTGPWGQCSSSCSGGLQHRAVVCQDENGQ-SASYCDAASkpPELQQCGPGPCP 1358
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGED--VETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 963-987 1.47e-03

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 38.41  E-value: 1.47e-03
                           10        20
                   ....*....|....*....|....*
gi 28316229    963 CVFTRWhySEWSQCSRSCGGGERSR 987
Cdd:pfam19028    1 CVVSEW--SEWSECSVTCGGGVQTR 23
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1078-1133 1.51e-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: 38.34  E-value: 1.51e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 28316229    1078 WQVGPWGPCTTTCGHGYQMRDVKCVNELASAvlEDTECHEASRpsDRQSCVLTPCS 1133
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN--GGGPCTGEDV--ETRACNEQPCP 53
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 389-445 1.64e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 40.80  E-value: 1.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 28316229     389 INEEKGLISAFTIAHELGHTLGVQHDDNP--RCKEMKVTKYHVMAPAlsFHMSPWSWSN 445
Cdd:smart00235   76 LSLGNGCINTGVAAHELGHALGLYHEQSRsdRDNYMYINYTNIDTRN--FDLSEDDSLG 132
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
343-435 1.83e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28316229  343 LDDVHPSHHDTAVLITRYDICSskEKCN-MLGLSYLGTIC-----DPLQSCFI----NEEKGLISAFTIA-HELGHTLGV 411
Cdd:COG1913   60 LSRLKEEDGDKVLGVTDVDLYA--PGLNfVFGLAYLGGRVavvstARLRPEFYglppDEELFLERVLKEAvHELGHLFGL 137

                         90       100
                 ....*....|....*....|....
gi 28316229  412 QHDDNPRCkemkvtkyhVMAPALS 435
Cdd:COG1913  138 GHCPNPRC---------VMHFSNS 152
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1157-1180 1.93e-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: 37.95  E-value: 1.93e-03
                            10        20
                    ....*....|....*....|....
gi 28316229    1157 GSWTPCSVSCGRGTQARYVSCRDA 1180
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSP 28
TSP_1 pfam00090
Thrombospondin type 1 domain;
1026-1075 2.19e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.78  E-value: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 28316229   1026 SEWSECLVTCGKGTKQRQVWCqlnvDHLSDGFCNSSTKPESLSPCELHTC 1075
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTC----KSPFPGGEPCTGDDIETQACKMDKC 49
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 401-419 5.09e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.01  E-value: 5.09e-03
                          10
                  ....*....|....*....
gi 28316229   401 IAHELGHTLGVQHDDNPRC 419
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRC 147
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
401-419 5.34e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 5.34e-03
                          10
                  ....*....|....*....
gi 28316229   401 IAHELGHTLGVQHDDNPRC 419
Cdd:NF033823  126 AVHELGHLLGLGHCPNPRC 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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