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Conserved domains on  [gi|1039776953|ref|XP_017177422|]
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disintegrin and metalloproteinase domain-containing protein 8 isoform X2 [Mus musculus]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 12023311)

disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-394 3.24e-101

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: 312.70  E-value: 3.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 272
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 273 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 351
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039776953 352 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 394
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-151 3.36e-36

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: 132.82  E-value: 3.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  44 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 123
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039776953 124 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 151
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 5.09e-34

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


:

Pssm-ID: 214490  Cd Length: 75  Bit Score: 124.73  E-value: 5.09e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776953  411 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
487-606 2.27e-32

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 122.47  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  487 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 554
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776953  555 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 606
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 637-856 4.87e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  637 APPNCVQRLADVSDEQAVSSFPVVTESAAVHSTTASGNWLGLNSGIVGLGLTTTTSSNPLLESQKSwsstslpvsVVVVL 716
Cdd:PHA03247  2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP---------GPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  717 VILVAAMVIVAGIVIYRKAPRQIQRRSVAPK--PISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPivkpkrppp 794
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP--------- 2919

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039776953  795 appgavSSSPLPVPVYAPKIPNQFRPDPPTKPLPELKPkQVKPTFAPPTPPVkpgtGGTVPG 856
Cdd:PHA03247  2920 ------QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL----GALVPG 2970
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-394 3.24e-101

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: 312.70  E-value: 3.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 272
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 273 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 351
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039776953 352 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 394
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 195-392 4.61e-79

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: 254.08  E-value: 4.61e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 272
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 273 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 351
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039776953 352 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 392
Cdd:cd04269   156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-151 3.36e-36

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: 132.82  E-value: 3.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  44 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 123
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039776953 124 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 151
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 5.09e-34

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 124.73  E-value: 5.09e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776953  411 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
411-483 4.83e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.96  E-value: 4.83e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776953 411 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 483
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
487-606 2.27e-32

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 122.47  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  487 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 554
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776953  555 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 606
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 488-526 7.08e-13

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 65.33  E-value: 7.08e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039776953 488 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 526
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
PHA03247 PHA03247
large tegument protein UL36; Provisional
 637-856 4.87e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  637 APPNCVQRLADVSDEQAVSSFPVVTESAAVHSTTASGNWLGLNSGIVGLGLTTTTSSNPLLESQKSwsstslpvsVVVVL 716
Cdd:PHA03247  2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP---------GPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  717 VILVAAMVIVAGIVIYRKAPRQIQRRSVAPK--PISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPivkpkrppp 794
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP--------- 2919

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039776953  795 appgavSSSPLPVPVYAPKIPNQFRPDPPTKPLPELKPkQVKPTFAPPTPPVkpgtGGTVPG 856
Cdd:PHA03247  2920 ------QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL----GALVPG 2970
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-394 3.24e-101

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: 312.70  E-value: 3.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 272
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 273 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 351
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039776953 352 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 394
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 195-392 4.61e-79

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: 254.08  E-value: 4.61e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 272
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 273 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 351
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039776953 352 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 392
Cdd:cd04269   156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 195-390 2.08e-38

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: 141.99  E-value: 2.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGsREAVRQRVLEVVNHVDKLYQELS----FRVVLVGLEIWNKDKF--YISRYANVTLENFLSW 268
Cdd:cd04273     1 RYVETLVVADSKMVEFHH-GEDLEHYILTLMNIVASLYKDPSlgnsINIVVVRLIVLEDEESglLISGNAQKSLKSFCRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 269 --REQNLQGQHP--HDNVQLITGVDFIGS-----TVGLAKVSALCSRH-SGAVNQDhskNSIGVASTMAHELGHNLGMSH 338
Cdd:cd04273    80 qkKLNPPNDSDPehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSrSCSINED---TGLSSAFTIAHELGHVLGMPH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039776953 339 DEDIPGCycpEPREGGGCIMTESIGSKF-PRIFSRCSKIDLESFVTKPQTGCL 390
Cdd:cd04273   157 DGDGNSC---GPEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-151 3.36e-36

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: 132.82  E-value: 3.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  44 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 123
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039776953 124 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 151
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 195-376 1.90e-34

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: 130.23  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKL-GSREAVRQRVLEVVNHVDKLYQELSF----RVVLVGLEIWNKDKFY--ISRYANVTLENFLS 267
Cdd:cd04267     1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAppIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 268 WREQNLQGqhpHDNVQLITGVDFI-GSTVGLAKVSALC-SRHSGAVNQDHSKNSIgVASTMAHELGHNLGMSHDEDipGC 345
Cdd:cd04267    81 WRAEGPIR---HDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGG--DE 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039776953 346 YCPEPREGGGCIMTESIGSKFPRIFSRCSKI 376
Cdd:cd04267   155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSIG 185
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 5.09e-34

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 124.73  E-value: 5.09e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776953  411 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
411-483 4.83e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.96  E-value: 4.83e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776953 411 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 483
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
487-606 2.27e-32

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 122.47  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  487 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 554
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776953  555 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 606
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 196-391 5.62e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 86.64  E-value: 5.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 196 YVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLYQELS---FRVVLVGLEIwNKDKFYISRYAN---------VTLE 263
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIHPinygyidaaETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 264 NFlswREQNLQGQHP--HDNVQLITGVDF--------IGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVaSTMAHELGHN 333
Cdd:cd04272    81 NF---NEYVKKKRDYfnPDVVFLVTGLDMstysggslQTGTGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELAHL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039776953 334 LGMSHDEDIPGCYCPEPREGGGC------IMteSIGSKFPRI--FSRCSKIDLESFVTKPQTGCLT 391
Cdd:cd04272   157 LGAPHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVNGERQyrFSQCSQRQIRNVFRRLGASCLH 220
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
194-364 4.63e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 83.24  E-value: 4.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 194 TRYVELYVVADsQEFQKLGSREAVRQRVLEVVNHVDKL-YQELSFRVVLVGLEIWNKDKFYISRYANV-----TLENFLS 267
Cdd:pfam13688   2 TRTVALLVAAD-CSYVAAFGGDAAQANIINMVNTASNVyERDFNISLGLVNLTISDSTCPYTPPACSTgdssdRLSEFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 268 WREQNlqGQHPHDNVQLITGVDFigSTVGLAKVSALCSRHS-GAVNQDHSKNSIGVAS-----TMAHELGHNLGMSHDED 341
Cdd:pfam13688  81 FSAWR--GTQNDDLAYLFLMTNC--SGGGLAWLGQLCNSGSaGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCD 156

                         170       180
                  ....*....|....*....|....*....
gi 1039776953 342 I--PGCYCPEPRE----GGGCIMTESIGS 364
Cdd:pfam13688 157 SstSSQCCPPSNStcpaGGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 220-339 2.52e-14

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: 70.09  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 220 RVLEVVNHVDKLYQ-ELSFRVVLVGLEIWNKDKF-YISRYANVTLENFLswreQNLQGQHPHDN---VQLITGVDFIGsT 294
Cdd:pfam13582   2 RIVSLVNRANTIYErDLGIRLQLAAIIITTSADTpYTSSDALEILDELQ----EVNDTRIGQYGydlGHLFTGRDGGG-G 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039776953 295 VGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD 339
Cdd:pfam13582  77 GGIAYVGGVCnSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 220-381 8.92e-14

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: 69.86  E-value: 8.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 220 RVLEVVNHVDKLYQELSFR------VVLVGLEIWNKdkfyisrYANVTLenFLSwreqnLQGQHPHDNVQLITGVDFIGS 293
Cdd:cd00203     1 KVIPYVVVADDRDVEEENLsaqiqsLILIAMQIWRD-------YLNIRF--VLV-----GVEIDKADIAILVTRQDFDGG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 294 TVGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD------EDIPGCYCPEPRE--GGGCIM-----T 359
Cdd:cd00203    67 TGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDDTLNAEddDYYSVMsytkgS 146

                         170       180
                  ....*....|....*....|..
gi 1039776953 360 ESIGSKFPriFSRCSKIDLESF 381
Cdd:cd00203   147 FSDGQRKD--FSQCDIDQINKL 166
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 199-375 1.90e-13

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: 70.87  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 199 LYVVADSQEFQKLGS--REAVRQRVLEVVNHVDKLYQELSFRVVL---VGLEIW----NKD--------KFYISRYANVT 261
Cdd:cd04270     5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQIKririHTTpdevdpgnKFYNKSFPNWG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 262 LENFLswrEQNLQGQHPHDN--VQLITGVDFIGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVAS--------------- 324
Cdd:cd04270    85 VEKFL---VKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkr 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039776953 325 --------TMAHELGHNLGMSHDEDIPGCyCPEPREGGGCIMTESIGS---KFPRIFSRCSK 375
Cdd:cd04270   162 vptkesdlVTAHELGHNFGSPHDPDIAEC-APGESQGGNYIMYARATSgdkENNKKFSPCSK 222
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 488-526 7.08e-13

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 65.33  E-value: 7.08e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039776953 488 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 526
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 216-375 1.64e-10

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: 61.11  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 216 AVRQRVLEVVNHVDKLY--QELSFRVVLVG---LEI-------WNKDKFyiSRYANVTLENFLSwreqNLQGQHPHDNVQ 283
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYepDDININGGLVNpgeIPAttsasdsGNNYCN--SPTTIVRRLNFLS----QWRGEQDYCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 284 LITGVDFIGSTVGLAKVSALCSRHSGAVnqdhsKNSIGVAST---------------MAHELGHNLGMSHDEDI-----P 343
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGsqyasS 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039776953 344 GCYCPEPR----EGGGCIMTESIGSKfPRIFSRCSK 375
Cdd:pfam13574 151 GCERNAATsvcsANGSFIMNPASKSN-NDLFSPCSI 185
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 201-391 4.86e-10

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: 60.51  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 201 VVADSQEFQKLGSREAVRQRVLEVVNHVDKLYqELSFRVVL--VGLEI--------------WN---KDKFYISRyanvT 261
Cdd:cd04271     7 VAADCSYTKSFGSVEEARRNILNNVNSASQLY-ESSFNISLglRNLTIsdascpstavdsapWNlpcNSRIDIDD----R 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 262 LENFLSWReqnlqGQHPHDNV---QLITGVDfIGSTVGLAKVSALC-SRHSGAVNQDH-SKNSIGVAST----MAHELGH 332
Cdd:cd04271    82 LSIFSQWR-----GQQPDDGNafwTLMTACP-SGSEVGVAWLGQLCrTGASDQGNETVaGTNVVVRTSNewqvFAHEIGH 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776953 333 NLGMSHDEDIPGCY---------CPEPRE----GGGCIMTESIGSKFPRiFSRCSKIDLESFVTK--PQTGCLT 391
Cdd:cd04271   156 TFGAVHDCTSGTCSdgsvgsqqcCPLSTStcdaNGQYIMNPSSSSGITE-FSPCTIGNICSLLGRnpVRTSCLS 228
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 195-345 6.60e-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: 404471  Cd Length: 203  Bit Score: 48.00  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 195 RYVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLY-QELSFRVVLVG----------LEIWNKDKFyISRYANVTLE 263
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCS-GGDLGNWRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 264 NFLSWReqnlqGQHPHDNVQLITGVDFIGSTVGLAKVSALCSrhsgAVNQDHSKNsiGVA------STMAHELGHNLGMS 337
Cdd:pfam13583  82 TLTSWR-----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCS----SARQNAKAS--GVArsrdewDIFAHEIGHTFGAV 150


                  ....*...
gi 1039776953 338 HDEDIPGC 345
Cdd:pfam13583 151 HDCSSQGE 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 637-856 4.87e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  637 APPNCVQRLADVSDEQAVSSFPVVTESAAVHSTTASGNWLGLNSGIVGLGLTTTTSSNPLLESQKSwsstslpvsVVVVL 716
Cdd:PHA03247  2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP---------GPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  717 VILVAAMVIVAGIVIYRKAPRQIQRRSVAPK--PISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPivkpkrppp 794
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP--------- 2919

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039776953  795 appgavSSSPLPVPVYAPKIPNQFRPDPPTKPLPELKPkQVKPTFAPPTPPVkpgtGGTVPG 856
Cdd:PHA03247  2920 ------QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL----GALVPG 2970
PHA03247 PHA03247
large tegument protein UL36; Provisional
 744-856 6.17e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  744 VAPKPISGLSNPLFYTRDSSLPAKNRPPDPS---ETVSTNQP--PRPIVKPKRPPPAPPGAV---SSSPLPVPVYAPKIP 815
Cdd:PHA03247  2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRrlTRPAVASLSESRESLPSPwdpADPPAAVLAPAAALP 2819

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039776953  816 NQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGtGGTVPG 856
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPG 2859
PHA03247 PHA03247
large tegument protein UL36; Provisional
 764-864 1.69e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  764 LPAKNRPPDPSETVSTNQP-PRPIVKPKRPPPAPPGAvsssplPVPVYAPKIPNQFRPDPPTKPLPELKPKQvkpTFAPP 842
Cdd:PHA03247  2555 LPPAAPPAAPDRSVPPPRPaPRPSEPAVTSRARRPDA------PPQSARPRAPVDDRGDPRGPAPPSPLPPD---THAPD 2625

                           90       100
                   ....*....|....*....|..
gi 1039776953  843 TPPVKPGTGGTVPGATQGAGEP 864
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVP 2647
PHA03247 PHA03247
large tegument protein UL36; Provisional
 746-856 5.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953  746 PKPISGLSNPLfyTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRPPPAPPGAVSSSPLPVPVYAPKIPNQFRPDPPTk 825
Cdd:PHA03247  2552 PPPLPPAAPPA--APDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP- 2628

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1039776953  826 PLPELKPKQVKPTFAPPTPPVKPGTGGTVPG 856
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 734-848 5.65e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 734 KAPRQIQRRSVAPKPISGL----SNPLFYTRDSSLPAKNRPP-DPSETVStnqPPRPIVKPKRPPPAPPGAVSSSPLPVP 808
Cdd:PTZ00449  547 GKPGETKEGEVGKKPGPAKehkpSKIPTLSKKPEFPKDPKHPkDPEEPKK---PKRPRSAQRPTRPKSPKLPELLDIPKS 623

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039776953 809 VYAPKIPNQ-FRPDPPTKPL----PElKPKQVKPTFAP--PTPPVKP 848
Cdd:PTZ00449  624 PKRPESPKSpKRPPPPQRPSsperPE-GPKIIKSPKPPksPKPPFDP 669
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 743-845 7.40e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.79  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776953 743 SVAPKPISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRpppappgavSSSPLPVPVYAPKIPNQfRPDP 822
Cdd:PRK14950  359 LLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETA---------TPPPVPPRPVAPPVPHT-PESA 428

                          90       100
                  ....*....|....*....|...
gi 1039776953 823 PTKPlPELKPKQVKPTFAPPTPP 845
Cdd:PRK14950  429 PKLT-RAAIPVDEKPKYTPPAPP 450
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 322-358 9.46e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.05  E-value: 9.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1039776953 322 VASTMAHELGHNLGMSHdedipgcyCPEPRegggCIM 358
Cdd:cd11375   123 LLKEAVHELGHLFGLDH--------CPYYA----CVM 147
 
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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