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Conserved domains on  [gi|6680642|ref|NP_031429|]
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disintegrin and metalloproteinase domain-containing protein 8 isoform 1 precursor [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 ...
 196-395 1.08e-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: 1.08e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 6680642    353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 45-152 3.39e-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: 3.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680642    125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 412-486 1.72e-33

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: 123.18  E-value: 1.72e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680642     412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 6.59e-32

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 120.93  E-value: 6.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680642     556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 695-807 7.15e-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: 43.39  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    695 VAPKPISGLSNPLFYTRDSSLPAKNRPPDPS---ETVSTNQP--PRPIVKPKRPPPAPPGAV---SSSPLPVPVYAPKIP 766
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRrlTRPAVASLSESRESLPSPwdpADPPAAVLAPAAALP 2819

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 6680642    767 NQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGtGGTVPG 807
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPG 2859
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 196-395 1.08e-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: 1.08e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 6680642    353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 196-393 2.15e-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: 2.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 352
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6680642  353 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 45-152 3.39e-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: 3.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680642    125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 412-486 1.72e-33

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: 123.18  E-value: 1.72e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680642     412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
412-484 1.53e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.42  E-value: 1.53e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680642    412 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 484
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 6.59e-32

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 120.93  E-value: 6.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680642     556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 489-527 1.02e-12

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: 64.94  E-value: 1.02e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6680642    489 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 527
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
PHA03247 PHA03247
large tegument protein UL36; Provisional
 695-807 7.15e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    695 VAPKPISGLSNPLFYTRDSSLPAKNRPPDPS---ETVSTNQP--PRPIVKPKRPPPAPPGAV---SSSPLPVPVYAPKIP 766
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRrlTRPAVASLSESRESLPSPwdpADPPAAVLAPAAALP 2819

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 6680642    767 NQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGtGGTVPG 807
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPG 2859
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 196-395 1.08e-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: 1.08e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 6680642    353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 196-393 2.15e-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: 2.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 352
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6680642  353 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 196-391 1.83e-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: 1.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  196 RYVELYVVADSQEFQKLGsREAVRQRVLEVVNHVDKLYQELS----FRVVLVGLEIWNKDKF--YISRYANVTLENFLSW 269
Cdd:cd04273   1 RYVETLVVADSKMVEFHH-GEDLEHYILTLMNIVASLYKDPSlgnsINIVVVRLIVLEDEESglLISGNAQKSLKSFCRW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  270 --REQNLQGQHP--HDNVQLITGVDFIGS-----TVGLAKVSALCSRH-SGAVNQDhskNSIGVASTMAHELGHNLGMSH 339
Cdd:cd04273  80 qkKLNPPNDSDPehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSrSCSINED---TGLSSAFTIAHELGHVLGMPH 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6680642  340 DEDIPGCycpEPREGGGCIMTESIGSKF-PRIFSRCSKIDLESFVTKPQTGCL 391
Cdd:cd04273 157 DGDGNSC---GPEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 45-152 3.39e-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: 3.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562  17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680642    125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 196-377 1.76e-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: 1.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  196 RYVELYVVADSQEFQKL-GSREAVRQRVLEVVNHVDKLYQELSF----RVVLVGLEIWNKDKFY--ISRYANVTLENFLS 268
Cdd:cd04267   1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAppIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  269 WREQNLQGqhpHDNVQLITGVDFI-GSTVGLAKVSALC-SRHSGAVNQDHSKNSIgVASTMAHELGHNLGMSHDEDipGC 346
Cdd:cd04267  81 WRAEGPIR---HDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGG--DE 154

                       170       180       190
                ....*....|....*....|....*....|.
gi 6680642  347 YCPEPREGGGCIMTESIGSKFPRIFSRCSKI 377
Cdd:cd04267 155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSIG 185
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 412-486 1.72e-33

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: 123.18  E-value: 1.72e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680642     412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
412-484 1.53e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.42  E-value: 1.53e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680642    412 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 484
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 6.59e-32

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 120.93  E-value: 6.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642     488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680642     556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 197-392 5.24e-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: 5.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  197 YVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLYQELS---FRVVLVGLEIwNKDKFYISRYAN---------VTLE 264
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIHPinygyidaaETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  265 NFlswREQNLQGQHP--HDNVQLITGVDF--------IGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVaSTMAHELGHN 334
Cdd:cd04272  81 NF---NEYVKKKRDYfnPDVVFLVTGLDMstysggslQTGTGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELAHL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680642  335 LGMSHDEDIPGCYCPEPREGGGC------IMteSIGSKFPRI--FSRCSKIDLESFVTKPQTGCLT 392
Cdd:cd04272 157 LGAPHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVNGERQyrFSQCSQRQIRNVFRRLGASCLH 220
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
195-365 4.21e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 83.24  E-value: 4.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    195 TRYVELYVVADsQEFQKLGSREAVRQRVLEVVNHVDKL-YQELSFRVVLVGLEIWNKDKFYISRYANV-----TLENFLS 268
Cdd:pfam13688   2 TRTVALLVAAD-CSYVAAFGGDAAQANIINMVNTASNVyERDFNISLGLVNLTISDSTCPYTPPACSTgdssdRLSEFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    269 WREQNlqGQHPHDNVQLITGVDFigSTVGLAKVSALCSRHS-GAVNQDHSKNSIGVAS-----TMAHELGHNLGMSHDED 342
Cdd:pfam13688  81 FSAWR--GTQNDDLAYLFLMTNC--SGGGLAWLGQLCNSGSaGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCD 156

                         170       180
                  ....*....|....*....|....*....
gi 6680642    343 I--PGCYCPEPRE----GGGCIMTESIGS 365
Cdd:pfam13688 157 SstSSQCCPPSNStcpaGGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 221-340 2.37e-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: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    221 RVLEVVNHVDKLYQ-ELSFRVVLVGLEIWNKDKF-YISRYANVTLENFLswreQNLQGQHPHDN---VQLITGVDFIGsT 295
Cdd:pfam13582   2 RIVSLVNRANTIYErDLGIRLQLAAIIITTSADTpYTSSDALEILDELQ----EVNDTRIGQYGydlGHLFTGRDGGG-G 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6680642    296 VGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD 340
Cdd:pfam13582  77 GGIAYVGGVCnSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 221-382 8.35e-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: 8.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  221 RVLEVVNHVDKLYQELSFR------VVLVGLEIWNKdkfyisrYANVTLenFLSwreqnLQGQHPHDNVQLITGVDFIGS 294
Cdd:cd00203   1 KVIPYVVVADDRDVEEENLsaqiqsLILIAMQIWRD-------YLNIRF--VLV-----GVEIDKADIAILVTRQDFDGG 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  295 TVGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD------EDIPGCYCPEPRE--GGGCIM-----T 360
Cdd:cd00203  67 TGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDDTLNAEddDYYSVMsytkgS 146

                       170       180
                ....*....|....*....|..
gi 6680642  361 ESIGSKFPriFSRCSKIDLESF 382
Cdd:cd00203 147 FSDGQRKD--FSQCDIDQINKL 166
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 200-376 1.74e-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: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  200 LYVVADSQEFQKLGS--REAVRQRVLEVVNHVDKLYQELSFRVVL---VGLEIW----NKD--------KFYISRYANVT 262
Cdd:cd04270   5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQIKririHTTpdevdpgnKFYNKSFPNWG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  263 LENFLswrEQNLQGQHPHDN--VQLITGVDFIGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVAS--------------- 325
Cdd:cd04270  85 VEKFL---VKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkr 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680642  326 --------TMAHELGHNLGMSHDEDIPGCyCPEPREGGGCIMTESIGS---KFPRIFSRCSK 376
Cdd:cd04270 162 vptkesdlVTAHELGHNFGSPHDPDIAEC-APGESQGGNYIMYARATSgdkENNKKFSPCSK 222
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 489-527 1.02e-12

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: 64.94  E-value: 1.02e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6680642    489 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 527
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 217-376 8.43e-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: 61.88  E-value: 8.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    217 AVRQRVLEVVNHVDKLY--QELSFRVVLVGL-EI---------WNKDKFyiSRYANVTLENFLSwreqNLQGQHPHDNVQ 284
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYepDDININGGLVNPgEIpattsasdsGNNYCN--SPTTIVRRLNFLS----QWRGEQDYCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    285 LITGVDFIGSTVGLAKVSALCSRHSGAVnqdhsKNSIGVAST---------------MAHELGHNLGMSHDEDI-----P 344
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGsqyasS 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6680642    345 GCYCPEPR----EGGGCIMTESIGSKfPRIFSRCSK 376
Cdd:pfam13574 151 GCERNAATsvcsANGSFIMNPASKSN-NDLFSPCSI 185
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 202-392 2.42e-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: 61.28  E-value: 2.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  202 VVADSQEFQKLGSREAVRQRVLEVVNHVDKLYqELSFRVVL--VGLEI--------------WN---KDKFYISRyanvT 262
Cdd:cd04271   7 VAADCSYTKSFGSVEEARRNILNNVNSASQLY-ESSFNISLglRNLTIsdascpstavdsapWNlpcNSRIDIDD----R 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642  263 LENFLSWReqnlqGQHPHDNV---QLITGVDfIGSTVGLAKVSALC-SRHSGAVNQDH-SKNSIGVAST----MAHELGH 333
Cdd:cd04271  82 LSIFSQWR-----GQQPDDGNafwTLMTACP-SGSEVGVAWLGQLCrTGASDQGNETVaGTNVVVRTSNewqvFAHEIGH 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680642  334 NLGMSHDEDIPGCY---------CPEPRE----GGGCIMTESIGSKFPRiFSRCSKIDLESFVTK--PQTGCLT 392
Cdd:cd04271 156 TFGAVHDCTSGTCSdgsvgsqqcCPLSTStcdaNGQYIMNPSSSSGITE-FSPCTIGNICSLLGRnpVRTSCLS 228
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 196-346 6.17e-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: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    196 RYVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLY-QELSFRVVLVG----------LEIWNKDKFyISRYANVTLE 264
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCS-GGDLGNWRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    265 NFLSWReqnlqGQHPHDNVQLITGVDFIGSTVGLAKVSALCSrhsgAVNQDHSKNsiGVA------STMAHELGHNLGMS 338
Cdd:pfam13583  82 TLTSWR-----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCS----SARQNAKAS--GVArsrdewDIFAHEIGHTFGAV 150


                  ....*...
gi 6680642    339 HDEDIPGC 346
Cdd:pfam13583 151 HDCSSQGE 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 695-807 7.15e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    695 VAPKPISGLSNPLFYTRDSSLPAKNRPPDPS---ETVSTNQP--PRPIVKPKRPPPAPPGAV---SSSPLPVPVYAPKIP 766
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRrlTRPAVASLSESRESLPSPwdpADPPAAVLAPAAALP 2819

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 6680642    767 NQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGtGGTVPG 807
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPG 2859
PHA03247 PHA03247
large tegument protein UL36; Provisional
 675-807 1.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    675 VIVAGIVIYRKAPRQIQRRSVAPK--PISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPivkpkrpppappgavS 752
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP---------------Q 2920

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6680642    753 SSPLPVPVYAPKIPNQFRPDPPTKPLPELKPkQVKPTFAPPTPPVkpgtGGTVPG 807
Cdd:PHA03247 2921 PQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL----GALVPG 2970
PHA03247 PHA03247
large tegument protein UL36; Provisional
 715-815 1.86e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    715 LPAKNRPPDPSETVSTNQP-PRPIVKPKRPPPAPPGAvsssplPVPVYAPKIPNQFRPDPPTKPLPELKPKQvkpTFAPP 793
Cdd:PHA03247 2555 LPPAAPPAAPDRSVPPPRPaPRPSEPAVTSRARRPDA------PPQSARPRAPVDDRGDPRGPAPPSPLPPD---THAPD 2625

                          90       100
                  ....*....|....*....|..
gi 6680642    794 TPPVKPGTGGTVPGATQGAGEP 815
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVP 2647
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 685-799 5.23e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642   685 KAPRQIQRRSVAPKPISGL----SNPLFYTRDSSLPAKNRPP-DPSETVStnqPPRPIVKPKRPPPAPPGAVSSSPLPVP 759
Cdd:PTZ00449 547 GKPGETKEGEVGKKPGPAKehkpSKIPTLSKKPEFPKDPKHPkDPEEPKK---PKRPRSAQRPTRPKSPKLPELLDIPKS 623

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6680642   760 VYAPKIPNQ-FRPDPPTKPL----PElKPKQVKPTFAP--PTPPVKP 799
Cdd:PTZ00449 624 PKRPESPKSpKRPPPPQRPSsperPE-GPKIIKSPKPPksPKPPFDP 669
PHA03247 PHA03247
large tegument protein UL36; Provisional
 697-807 5.44e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642    697 PKPISGLSNPLfyTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRPPPAPPGAVSSSPLPVPVYAPKIPNQFRPDPPTk 776
Cdd:PHA03247 2552 PPPLPPAAPPA--APDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP- 2628

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6680642    777 PLPELKPKQVKPTFAPPTPPVKPGTGGTVPG 807
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 694-796 7.02e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.79  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680642   694 SVAPKPISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRpppappgavSSSPLPVPVYAPKIPNQfRPDP 773
Cdd:PRK14950 359 LLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETA---------TPPPVPPRPVAPPVPHT-PESA 428

                         90       100
                 ....*....|....*....|...
gi 6680642   774 PTKPlPELKPKQVKPTFAPPTPP 796
Cdd:PRK14950 429 PKLT-RAAIPVDEKPKYTPPAPP 450
 
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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