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Conserved domains on  [gi|40806187|ref|NP_955387|]
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A disintegrin and metalloproteinase with thrombospondin motifs 18 isoform 1 preproprotein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 293-494 3.76e-111

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: 346.15  E-value: 3.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  293 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 372
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  373 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 449
Cdd:cd04273   81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 40806187  450 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 494
Cdd:cd04273  160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 750-861 1.34e-39

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: 142.72  E-value: 1.34e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    750 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 828
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40806187    829 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 861
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-203 7.36e-37

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: 135.13  E-value: 7.36e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187     64 VTPVEVDSAgsyishdilhngRKKRSAQNARSS---LHYRFSAFGQELHLELKPSAIL-SSHFIVQVLGKDGASETQKPE 139
Cdd:pfam01562    3 VIPVRLDPS------------RRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLlAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    140 VQ-QCFYQGFIRNDSSSSVAVSTCAGLSGLIRTRKNEFLISPLPqllaqehNYSSPAGHHPHVLY 203
Cdd:pfam01562   71 QTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE-------KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 511-578 1.37e-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: 1.37e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40806187    511 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 578
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 592-643 1.80e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.80e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 40806187     592 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 643
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 935-991 8.77e-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: 64.01  E-value: 8.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 40806187    935 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 991
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 648-748 1.23e-12

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


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    648 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 715
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 40806187    716 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 748
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1127-1173 4.66e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 4.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187   1127 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1173
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 995-1048 2.25e-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: 60.16  E-value: 2.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    995 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 1048
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1188-1218 1.65e-10

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.65e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 40806187   1188 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1218
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1056-1115 7.80e-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: 7.80e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187   1056 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 1115
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-931 9.22e-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: 38.59  E-value: 9.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 40806187    883 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 931
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 293-494 3.76e-111

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: 346.15  E-value: 3.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  293 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 372
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  373 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 449
Cdd:cd04273   81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 40806187  450 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 494
Cdd:cd04273  160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 750-861 1.34e-39

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: 142.72  E-value: 1.34e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    750 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 828
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40806187    829 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 861
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-203 7.36e-37

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: 135.13  E-value: 7.36e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187     64 VTPVEVDSAgsyishdilhngRKKRSAQNARSS---LHYRFSAFGQELHLELKPSAIL-SSHFIVQVLGKDGASETQKPE 139
Cdd:pfam01562    3 VIPVRLDPS------------RRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLlAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    140 VQ-QCFYQGFIRNDSSSSVAVSTCAGLSGLIRTRKNEFLISPLPqllaqehNYSSPAGHHPHVLY 203
Cdd:pfam01562   71 QTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE-------KYSREEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 295-498 4.10e-33

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: 127.03  E-value: 4.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    295 VETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKdgtiGSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQW 371
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeIWTDEDK--IDVSGDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    372 QSALIGKNgKRHDHAILLTGfdicswKNEPCDTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHDG 448
Cdd:pfam01421   77 RQEYLKKR-KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 40806187    449 EGNPCR--KAEGNIMSPTlTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEP 498
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 511-578 1.37e-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: 1.37e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40806187    511 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 578
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 592-643 1.80e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.80e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 40806187     592 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 643
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 935-991 8.77e-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: 64.01  E-value: 8.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 40806187    935 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 991
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 648-748 1.23e-12

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    648 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 715
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 40806187    716 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 748
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1127-1173 4.66e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 4.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187   1127 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1173
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 995-1048 2.25e-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: 60.16  E-value: 2.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    995 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 1048
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1188-1218 1.65e-10

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.65e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 40806187   1188 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1218
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
593-643 2.99e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.99e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187    593 SAWSKWSECSRTCGGGVKFQERHCNNPKPqyGGLFCPGSSRIYQLCNINPC 643
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1056-1115 7.80e-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: 7.80e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187   1056 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 1115
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 995-1049 4.58e-06

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: 44.89  E-value: 4.58e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187     995 WSLGPWSQCSKTCGRGVRKRELLCKgSAAETLPESQCTSlPRPELQEgCVLGRCP 1049
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG-EDVETRA-CNEQPCP 53
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 991-1049 9.03e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 9.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40806187   991 CPPqWSlgPWSQCSKTCGRGV--RKRELLCKGsaaetlpesqCTSlprpELQEGCVLGRCP 1049
Cdd:PTZ00441  240 CGP-WD--EWTPCSVTCGKGThsRSRPILHEG----------CTT----HMVEECEEEECP 283
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1059-1116 1.50e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.65  E-value: 1.50e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 40806187    1059 SSWSECSATCGLGVRKREMKCsekgfqgklITFPERRCRNIKKPNLDLEETCNRRACP 1116
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC---------CSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 938-992 2.22e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.26  E-value: 2.22e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187     938 GEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlhsLCPVSTPtQVQACNSHACP 992
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-----PCTGEDV-ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1131-1178 2.76e-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: 39.88  E-value: 2.76e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 40806187    1131 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSCLLHQKPPVLRACNTNFCP 1178
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-931 9.22e-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: 38.59  E-value: 9.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 40806187    883 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 931
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 293-494 3.76e-111

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: 346.15  E-value: 3.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  293 LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 372
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  373 SALIGKNGK---RHDHAILLTGFDICSWkNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGE 449
Cdd:cd04273   81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 40806187  450 GNPCRK--AEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCL 494
Cdd:cd04273  160 GNSCGPegKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 750-861 1.34e-39

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: 142.72  E-value: 1.34e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    750 FYKGLYlNQHKANEYYPVVLIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSID-WPGEFPFAGTTFEYQRSFNRP 828
Cdd:pfam05986    1 TVSGSF-TEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40806187    829 ERLYAPGPTNETLVFEILMQ---GKNPGIAWKYALP 861
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 295-487 2.34e-38

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 141.79  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  295 VETLVVADKKMVEK-HGKGNVTT-YILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQ 372
Cdd:cd04267    3 IELVVVADHRMVSYfNSDENILQaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  373 SaligKNGKRHDHAILLTGFDICSwknepCDTLGFAPISGMCSKYRSCTINEDTGLGL--AFTIAHESGHNFGMIHDGEG 450
Cdd:cd04267   83 A----EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGD 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 40806187  451 ---NPCRKAEGNIMSPTLTGNNGVFsWSSCSRQYLKKFLS 487
Cdd:cd04267  154 elaFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-203 7.36e-37

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: 135.13  E-value: 7.36e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187     64 VTPVEVDSAgsyishdilhngRKKRSAQNARSS---LHYRFSAFGQELHLELKPSAIL-SSHFIVQVLGKDGASETQKPE 139
Cdd:pfam01562    3 VIPVRLDPS------------RRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLlAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    140 VQ-QCFYQGFIRNDSSSSVAVSTCAGLSGLIRTRKNEFLISPLPqllaqehNYSSPAGHHPHVLY 203
Cdd:pfam01562   71 QTdHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE-------KYSREEGGHPHVVY 128
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 294-494 4.76e-35

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 132.35  E-value: 4.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  294 NVETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKDgtigSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQ 370
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLeIWTDKDK--ISVSGDAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  371 WQSALIGKnGKRHDHAILLTGFDICSwknepcDTLGFAPISGMCSKYRSCTINEDTG---LGLAFTIAHESGHNFGMIHD 447
Cdd:cd04269   76 WKRSNLLP-RKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHD 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 40806187  448 GEGNPCRkAEGNIMSPTLTgnNGVFSWSSCSRQYLKKFLSTPQAGCL 494
Cdd:cd04269  149 DGGCTCG-RSTCIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 295-498 4.10e-33

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: 127.03  E-value: 4.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    295 VETLVVADKKMVEKHGK--GNVTTYILTVMNMVSGLFKdgtiGSDINVVVVSL-ILLEQEPggLLINHHADQSLNSFCQW 371
Cdd:pfam01421    3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLeIWTDEDK--IDVSGDANDTLRNFLKW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    372 QSALIGKNgKRHDHAILLTGfdicswKNEPCDTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHDG 448
Cdd:pfam01421   77 RQEYLKKR-KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 40806187    449 EGNPCR--KAEGNIMSPTlTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEP 498
Cdd:pfam01421  150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 511-578 1.37e-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: 1.37e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40806187    511 PGQIYDADTQCKWQFGAKAKLCSlGFVKDICKSLWCHRV-GHRCETKFMPAAEGTVCGLSMWCRQGQCV 578
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCP-NGDEDVCSKLWCSNPgGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 592-643 1.80e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.80e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 40806187     592 WSAWSKWSECSRTCGGGVKFQERHCNNPKPQYGGLFCPGSSRIYQLCNINPC 643
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 293-494 6.43e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.08  E-value: 6.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  293 LNVETLVVADKKmVEKHGKGN--VTTYILTVMNMVSGLFKDgTIGSDINVVVVSLILLEQEPGGLLINHHAD------QS 364
Cdd:cd04272    1 VYPELFVVVDYD-HQSEFFSNeqLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYgyidaaET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  365 LNSFCQWqsaligKNGKRH----DHAILLTGFDICSWKNEPCDT--LGFAPISGMCSKYRsCTINEDTG--LGLAFTIAH 436
Cdd:cd04272   79 LENFNEY------VKKKRDyfnpDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENR-VAMGEDTPgsYYGVYTMTH 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40806187  437 ESGHNFGMIHDGEGNP-----------CRKAEGNIMSptlTGNNGV--FSWSSCSRQYLKKFLSTPQAGCL 494
Cdd:cd04272  152 ELAHLLGAPHDGSPPPswvkghpgsldCPWDDGYIMS---YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 361-486 7.95e-15

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: 73.71  E-value: 7.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  361 ADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDIcswknePCDTLGFAPISGMCSKYRSCTINEDTGLG---LAFTIAHE 437
Cdd:cd00203   30 AMQIWRDYLNIRFVLVGVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHE 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40806187  438 SGHNFGMIHDG-------------EGNPCRKAEGNIMSPTLTGNNGVFS--WSSCSRQYLKKFL 486
Cdd:cd00203  104 LGHALGFYHDHdrkdrddyptiddTLNAEDDDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 935-991 8.77e-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: 64.01  E-value: 8.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 40806187    935 WMPGEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlHSLCPVST-PTQVQACNSHAC 991
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVP---DSECSAQKkPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 648-748 1.23e-12

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 65.50  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    648 LDFRAQQCAEYNSKPFR-----GWFYQWKPYTKVEEEDR-CKLYCKAENFEFFFAMSGKVKDGTPCSPN--KND----VC 715
Cdd:pfam19236    3 LEFMSQQCARTDGQPLRsspggASFYHWGAAVPHSQGDAlCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpREDgtlsLC 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 40806187    716 IDGVCELVGCDHELGSKAVSDACGVCKGDNSTC 748
Cdd:pfam19236   83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1127-1173 4.66e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 4.66e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187   1127 WYSLPWQQCTVTCGGGVQTRSVHCVQQG----RPSSSCLLHQKPPVLRACN 1173
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsiVPDSECSAQKKPPETQSCN 51
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
298-473 1.11e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 65.13  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    298 LVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGtigSDINVVVVSLILLEQE-----PGGLLINhhADQSLNSFcQWQ 372
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERD---FNISLGLVNLTISDSTcpytpPACSTGD--SSDRLSEF-QDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    373 SALIGKngKRHDHAILLTGFDicswknepCDTLGFAPISGMCSKYRSCTINEDTG--------LGLAFTIAHESGHNFGM 444
Cdd:pfam13688   82 SAWRGT--QNDDLAYLFLMTN--------CSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGA 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 40806187    445 IHDGE----------GNPCRKAEGN-IMSPTLTGNNGVFS 473
Cdd:pfam13688  152 VHDCDsstssqccppSNSTCPAGGRyIMNPSSSPNSTDFS 191
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 995-1048 2.25e-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: 60.16  E-value: 2.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187    995 WSLGPWSQCSKTCGRGVRKRELLCKGSA-AETLPESQCTSLPRPELQEGCVLGRC 1048
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKPPETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 312-479 7.16e-11

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: 62.65  E-value: 7.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    312 GNVTTYILTVMNMVSGLFKDGTIGSDINVVvvslilleqEPGGLLINHHADQSLNSFCQ---WQ-------SALIGKNGK 381
Cdd:pfam13574    1 GNVTENLVNVVNRVNQIYEPDDININGGLV---------NPGEIPATTSASDSGNNYCNsptTIvrrlnflSQWRGEQDY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    382 RHDHAILLTGFdicswkNEPcdTLGFAPISGMCSKYRSCtINEDTGLGLAFT-------------IAHESGHNFGMIHD- 447
Cdd:pfam13574   72 CLAHLVTMGTF------SGG--ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDc 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 40806187    448 -GEGNPCRKAEGN------------IMSPTLTGNNGVFswSSCSR 479
Cdd:pfam13574  143 dGSQYASSGCERNaatsvcsangsfIMNPASKSNNDLF--SPCSI 185
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 1188-1218 1.65e-10

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 56.78  E-value: 1.65e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 40806187   1188 CVDFFNWCHLVPQHGVCNHKFYGKQCCKSCT 1218
Cdd:pfam08686    1 CKDKFANCSLVVQARLCSHKYYRQFCCRSCS 31
TSP_1 pfam00090
Thrombospondin type 1 domain;
593-643 2.99e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.99e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187    593 SAWSKWSECSRTCGGGVKFQERHCNNPKPqyGGLFCPGSSRIYQLCNINPC 643
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1056-1115 7.80e-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: 7.80e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187   1056 WVASSWSECSATCGLGVRKREMKCSEKGFQgklITFPERRCRNIKKPNldLEETCNRRAC 1115
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGG---SIVPDSECSAQKKPP--ETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 593-643 1.88e-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: 46.12  E-value: 1.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187    593 SAWSKWSECSRTCGGGVKFQERHCNNPkPQYGGLFCPGSSRIyQLCNINPC 643
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 433-501 2.54e-06

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


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 50.06  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40806187  433 TIAHESGHNFGMIHDGEGNPCRKAE---GN-IMSPTLTG----NNGVFswSSCSRQYLKKFLSTPQAGCLVdEPKQA 501
Cdd:cd04270  170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYARATSgdkeNNKKF--SPCSKKSISKVLEVKSNSCFV-ERSQS 243
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 995-1049 4.58e-06

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: 44.89  E-value: 4.58e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187     995 WSLGPWSQCSKTCGRGVRKRELLCKgSAAETLPESQCTSlPRPELQEgCVLGRCP 1049
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG-EDVETRA-CNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 316-447 8.98e-06

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: 46.21  E-value: 8.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187    316 TYILTVMNMVSGLFKdgtIGSDINVVVVSLILLE-QEPGGLLINhhADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDI 394
Cdd:pfam13582    1 ARIVSLVNRANTIYE---RDLGIRLQLAAIIITTsADTPYTSSD--ALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGG 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 40806187    395 cswknepcdTLGFAPISGMCSKYRSCTINED---TGLGLAFTIAHESGHNFGMIHD 447
Cdd:pfam13582   76 ---------GGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 597-643 7.88e-05

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: 41.67  E-value: 7.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40806187    597 KWSECSRTCGGGVKFQERHCNNPKPQ--YGGLFCPGSSR--IYQLCNINPC 643
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 991-1049 9.03e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 9.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40806187   991 CPPqWSlgPWSQCSKTCGRGV--RKRELLCKGsaaetlpesqCTSlprpELQEGCVLGRCP 1049
Cdd:PTZ00441  240 CGP-WD--EWTPCSVTCGKGThsRSRPILHEG----------CTT----HMVEECEEEECP 283
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1059-1116 1.50e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.65  E-value: 1.50e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 40806187    1059 SSWSECSATCGLGVRKREMKCsekgfqgklITFPERRCRNIKKPNLDLEETCNRRACP 1116
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSC---------CSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 938-992 2.22e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 40.26  E-value: 2.22e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 40806187     938 GEWSTCSKACAGGQQSRKIQCVQKKPFQKEEavlhsLCPVSTPtQVQACNSHACP 992
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-----PCTGEDV-ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1131-1178 2.76e-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: 39.88  E-value: 2.76e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 40806187    1131 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSCLLHQKPPVLRACNTNFCP 1178
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-931 9.22e-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: 38.59  E-value: 9.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 40806187    883 SECSVSCGGGYINVKAICLR-DQNTQVNSSFCSAKTKPvTEPKICNAFSC 931
Cdd:pfam19030    7 GECSVTCGGGVQTRLVQCVQkGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1059-1115 1.20e-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: 38.03  E-value: 1.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187   1059 SSWSECSATCGLGVRKREMkcsekgfqgKLITFPE---RRCrnikkPNLDLEETCNRRAC 1115
Cdd:pfam19028    7 SEWSECSVTCGGGVQTRTR---------TVIVEPQnggRPC-----PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
998-1020 1.82e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.40  E-value: 1.82e-03
                           10        20
                   ....*....|....*....|...
gi 40806187    998 GPWSQCSKTCGRGVRKRELLCKG 1020
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTCKS 26
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 995-1014 2.82e-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: 36.87  E-value: 2.82e-03
                           10        20
                   ....*....|....*....|
gi 40806187    995 WSlgPWSQCSKTCGRGVRKR 1014
Cdd:pfam19028    6 WS--EWSECSVTCGGGVQTR 23
TSP_1 pfam00090
Thrombospondin type 1 domain;
1131-1160 3.01e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.01  E-value: 3.01e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 40806187   1131 PWQQCTVTCGGGVQTRSVHCVQQGRPSSSC 1160
Cdd:pfam00090    5 PWSPCSVTCGKGIQVRQRTCKSPFPGGEPC 34
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 318-447 7.15e-03

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 39.33  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806187  318 ILTVMNMVSGLFKDGTigsDINVVVVSLILLEQE---------PGGLLINHHAD--QSLNSFCQWQSaligknGKRHDHA 386
Cdd:cd04271   27 ILNNVNSASQLYESSF---NISLGLRNLTISDAScpstavdsaPWNLPCNSRIDidDRLSIFSQWRG------QQPDDGN 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40806187  387 ILLTGFDICswKNEPcdTLGFAPISGMCSKYRSCTINEDTG--LGLAFT------IAHESGHNFGMIHD 447
Cdd:cd04271   98 AFWTLMTAC--PSGS--EVGVAWLGQLCRTGASDQGNETVAgtNVVVRTsnewqvFAHEIGHTFGAVHD 162
TSP_1 pfam00090
Thrombospondin type 1 domain;
1059-1079 8.48e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 8.48e-03
                           10        20
                   ....*....|....*....|.
gi 40806187   1059 SSWSECSATCGLGVRKREMKC 1079
Cdd:pfam00090    4 SPWSPCSVTCGKGIQVRQRTC 24
 
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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