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Conserved domains on  [gi|73747885|ref|NP_003465|]
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disintegrin and metalloproteinase domain-containing protein 12 isoform 1 preproprotein [Homo sapiens]

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 ...
 214-416 1.72e-105

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: 324.64  E-value: 1.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 373
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 73747885   374 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
510-652 1.22e-54

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 185.64  E-value: 1.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747885    590 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 652
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-159 4.65e-31

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: 118.19  E-value: 4.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTvilGHCYYHGHVRGYSDSAVSLSTCS 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT---DHCYYQGHVEGHPDSSVALSTCS 95

                          90       100
                  ....*....|....*....|
gi 73747885   140 GLRGLIVFENESYVLEPMKS 159
Cdd:pfam01562  96 GLRGFIRTENEEYLIEPLEK 115
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-507 2.24e-29

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: 111.63  E-value: 2.24e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747885    439 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 507
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 754-905 7.78e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   754 PSRPPRGFQPCQAHLGHLGKG--LMRKPPdSYPPKDNPRRLLQCQNVDISRPlnglnVPQPQSTQRVLPPLHRA-PRAPS 830
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGgdVRRRPP-SRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPErPPQPQ 2912

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   831 VPARPLPAKPALRQAQGTckPNPPQKPLPADPLARTTRLTHAL------------ARTPGQWETGLRLAPlRPAPQYPHQ 898
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQ--PPPPPPPRPQPPLAPTTDPAGAGepsgavpqpwlgALVPGRVAVPRFRVP-QPAPSREAP 2989


                  ....*..
gi 73747885   899 VPrSTHT 905
Cdd:PHA03247 2990 AS-STPP 2995
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 214-416 1.72e-105

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: 324.64  E-value: 1.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 373
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 73747885   374 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 214-414 4.62e-98

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: 304.92  E-value: 4.62e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 373
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 73747885 374 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 414
Cdd:cd04269 157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
510-652 1.22e-54

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 185.64  E-value: 1.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747885    590 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 652
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 510-620 1.37e-41

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: 147.38  E-value: 1.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 73747885   590 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 620
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-159 4.65e-31

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: 118.19  E-value: 4.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTvilGHCYYHGHVRGYSDSAVSLSTCS 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT---DHCYYQGHVEGHPDSSVALSTCS 95

                          90       100
                  ....*....|....*....|
gi 73747885   140 GLRGLIVFENESYVLEPMKS 159
Cdd:pfam01562  96 GLRGFIRTENEEYLIEPLEK 115
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-507 2.24e-29

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: 111.63  E-value: 2.24e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747885    439 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 507
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
443-505 5.20e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 107.71  E-value: 5.20e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747885   443 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 505
Cdd:pfam00200  11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
 754-905 7.78e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   754 PSRPPRGFQPCQAHLGHLGKG--LMRKPPdSYPPKDNPRRLLQCQNVDISRPlnglnVPQPQSTQRVLPPLHRA-PRAPS 830
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGgdVRRRPP-SRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPErPPQPQ 2912

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   831 VPARPLPAKPALRQAQGTckPNPPQKPLPADPLARTTRLTHAL------------ARTPGQWETGLRLAPlRPAPQYPHQ 898
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQ--PPPPPPPRPQPPLAPTTDPAGAGepsgavpqpwlgALVPGRVAVPRFRVP-QPAPSREAP 2989


                  ....*..
gi 73747885   899 VPrSTHT 905
Cdd:PHA03247 2990 AS-STPP 2995
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 288-400 3.07e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 44.00  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885  288 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 366
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 73747885  367 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 400
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 779-871 2.15e-03

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 38.91  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   779 PPDSYPPKDNPrrllqcqNVDISRPLnGLNVPQPQSTQRVLPPLHrAPRAPSVPARPLPAKPALRQAQGTckPNPPQKPL 858
Cdd:pfam12526  31 PPESAHPDPPP-------PVGDPRPP-VVDTPPPVSAVWVLPPPS-EPAAPEPDLVPPVTGPAGPPSPLA--PPAPAQKP 99

                          90
                  ....*....|...
gi 73747885   859 PADPLARTTRLTH 871
Cdd:pfam12526 100 PLPPPRPQRRLLH 112
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 214-416 1.72e-105

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: 324.64  E-value: 1.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 373
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 73747885   374 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 214-414 4.62e-98

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: 304.92  E-value: 4.62e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 373
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 73747885 374 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 414
Cdd:cd04269 157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
510-652 1.22e-54

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 185.64  E-value: 1.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747885    590 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 652
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 510-620 1.37e-41

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: 147.38  E-value: 1.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 73747885   590 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 620
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 214-405 3.84e-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: 129.46  E-value: 3.84e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYR----PLNIRIVLVGVEVWN--DMDKcSVSQDPFTSLHEFL 287
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKgeQFAP-PIDSDASNTLNSFS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 288 DWRKMKllpRKSHDNAQLVSGVYF-QGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAaVTLAHELGHNFGMNHDtlDRG 366
Cdd:cd04267  80 FWRAEG---PIRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTA-LTMAHELGHNLGAEHD--GGD 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 73747885 367 CSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLE 405
Cdd:cd04267 154 ELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 214-413 3.53e-33

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: 127.35  E-value: 3.53e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 214 KYVELVIVADNREFQRQGKdlEKVKQRLIEIANHVDKFYR-PL---NIRIVLVGVEVWNDMDK-CSVSQDPFTSLHEFLD 288
Cdd:cd04273   1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 289 WRKmKLLPR-----KSHDNAQLVSGVYFQG-----TTIGMAPIMSMCTADQSGGIVmdhSDNPLGAAVTLAHELGHNFGM 358
Cdd:cd04273  79 WQK-KLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELGHVLGM 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 73747885 359 NHDTLDRGCScqmAVEKGGCIMNASTGYPF-PMVFSSCSRKDLETSLEKGMGVCLF 413
Cdd:cd04273 155 PHDGDGNSCG---PEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-159 4.65e-31

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: 118.19  E-value: 4.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885    60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTvilGHCYYHGHVRGYSDSAVSLSTCS 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT---DHCYYQGHVEGHPDSSVALSTCS 95

                          90       100
                  ....*....|....*....|
gi 73747885   140 GLRGLIVFENESYVLEPMKS 159
Cdd:pfam01562  96 GLRGFIRTENEEYLIEPLEK 115
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-507 2.24e-29

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: 111.63  E-value: 2.24e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747885    439 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 507
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
443-505 5.20e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 107.71  E-value: 5.20e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747885   443 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 505
Cdd:pfam00200  11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-385 3.59e-19

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 86.32  E-value: 3.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   212 ATKYVELVIVADNrEFqRQGKDLEKVKQRLIEIANHVD-KFYRPLNIRIVLVGVEVWNDMD----KCSVSQDPFTSLHEF 286
Cdd:pfam13688   1 STRTVALLVAADC-SY-VAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   287 LD---WRKmkllpRKSHDNAQLVSGVYFQGTtiGMAPIMSMCTADQSGGIVMDHSDN-----PLGAAVTLAHELGHNFGM 358
Cdd:pfam13688  79 QDfsaWRG-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNnvvvsTATEWQVFAHEIGHNFGA 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 73747885   359 NHD----TLDRGCSCQMAVEKGG--CIMNASTG 385
Cdd:pfam13688 152 VHDcdssTSSQCCPPSNSTCPAGgrYIMNPSSS 184
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 214-398 8.87e-18

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: 81.80  E-value: 8.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 214 KYVELVIVADNREFqrqgkDLEKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwndmdkcsvsqdpftslhefldwrkm 292
Cdd:cd00203   1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 293 kllprKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMA 372
Cdd:cd00203  50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDH-DRKDRDDYP 123

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 73747885 373 VEK---------GGCIMNA-----STGYPFPmvFSSCSRK 398
Cdd:cd00203 124 TIDdtlnaedddYYSVMSYtkgsfSDGQRKD--FSQCDID 161
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 241-361 2.24e-13

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: 67.40  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   241 LIEIANHVdkFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMkllpRKSHDNA---QLVSGVYFQGTTiG 317
Cdd:pfam13582   6 LVNRANTI--YERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-G 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 73747885   318 MAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHD 361
Cdd:pfam13582  79 IAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 218-411 1.92e-10

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: 62.01  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 218 LVIVADNREFQRQGKDLEK-VKQRLIEIANHVDKFYRPL--------NIRIVLVGVEVwNDMDKCSVSQDPFTSlHEFLD 288
Cdd:cd04270   5 LLLVADHRFYKYMGRGEEEtTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRI-HTTPDEVDPGNKFYN-KSFPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 289 WRKMKLLPRKSHDN-------AQLVSGVYFQGTTIGMAPIMSMcTADQSGGIVMDHSDNPLG------------------ 343
Cdd:cd04270  83 WGVEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGSP-RDNSAGGICEKAYYYSNGkkkylntgltttvnygkr 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73747885 344 -----AAVTLAHELGHNFGMNHDTldRGCSCQMAVEKGG-CIMNAS--TGY-PFPMVFSSCSRKDLETSLEKGMGVC 411
Cdd:cd04270 162 vptkeSDLVTAHELGHNFGSPHDP--DIAECAPGESQGGnYIMYARatSGDkENNKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 215-399 3.47e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 60.83  E-value: 3.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 215 YVELVIVADnREFQRQGKDLEKVKQRLIEIANHVDKFYRPLN---IRIVLVGVEVWNDMDKCSVSQ-------DPFTSLH 284
Cdd:cd04272   2 YPELFVVVD-YDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHpinygyiDAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 285 EFLDWRKMKLLPRKShDNAQLVSG----VYFQGT----TIGMAPIMSMCTADqsgGIVMDHsDNP--LGAAVTLAHELGH 354
Cdd:cd04272  81 NFNEYVKKKRDYFNP-DVVFLVTGldmsTYSGGSlqtgTGGYAYVGGACTEN---RVAMGE-DTPgsYYGVYTMTHELAH 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 73747885 355 NFGMNHDTLDRGCSCQMAVEKGGC------IMNASTGYPFPMVFSSCSRKD 399
Cdd:cd04272 156 LLGAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQ 206
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 213-396 2.82e-08

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: 54.93  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   213 TKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFY-RPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRK 291
Cdd:pfam13583   1 TRRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   292 MKL---LPRKSHDNAQLVSGVYFQGTTIGMAPIMSMC-TADQS--GGIVMDHSDNPlgaaVTLAHELGHNFGMNHDTLDR 365
Cdd:pfam13583  81 ATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakASGVARSRDEW----DIFAHEIGHTFGAVHDCSSQ 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 73747885   366 GCSCQMAVE--KGGCIMNASTGYPFPMvFSSCS 396
Cdd:pfam13583 157 GEGLSSSTEdgSGQTIMSYASTASQTA-FSPCT 188
PHA03247 PHA03247
large tegument protein UL36; Provisional
 754-905 7.78e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   754 PSRPPRGFQPCQAHLGHLGKG--LMRKPPdSYPPKDNPRRLLQCQNVDISRPlnglnVPQPQSTQRVLPPLHRA-PRAPS 830
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGgdVRRRPP-SRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPErPPQPQ 2912

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   831 VPARPLPAKPALRQAQGTckPNPPQKPLPADPLARTTRLTHAL------------ARTPGQWETGLRLAPlRPAPQYPHQ 898
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQ--PPPPPPPRPQPPLAPTTDPAGAGepsgavpqpwlgALVPGRVAVPRFRVP-QPAPSREAP 2989


                  ....*..
gi 73747885   899 VPrSTHT 905
Cdd:PHA03247 2990 AS-STPP 2995
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-405 7.94e-07

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: 50.32  E-value: 7.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   237 VKQRLIEIANHVDKFYRP--LNIRIVLVGV----------EVWNDmdKCSVSQDPFTSLHEFLDWRKmkllpRKSHDNAQ 304
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPddININGGLVNPgeipattsasDSGNN--YCNSPTTIVRRLNFLSQWRG-----EQDYCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   305 LVSGVYFQGTTIGMAPIMSMCTADQS---------GGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMAVEK 375
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASspktntglsTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDC-DGSQYASSGCER 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 73747885   376 GGCIMNASTGYPFPM---------VFSSCSRKDLETSLE 405
Cdd:pfam13574 155 NAATSVCSANGSFIMnpasksnndLFSPCSISLICDVLG 193
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-892 2.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   750 RCVRPSRPPRGFQP--CQAHLGHLgKGLMRKPPDSYPPKDNPRRLLQcqnvdiSRPLNglnvPQPQSTQRVLPPLHRAPR 827
Cdd:PHA03247 2672 RAAQASSPPQRPRRraARPTVGSL-TSLADPPPPPPTPEPAPHALVS------ATPLP----PGPAAARQASPALPAAPA 2740

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73747885   828 APSVPARPL----PAKPALRQA-QGTCKPNPPQKPlPADPLARTTR-----LTHALARTPGQWETGLRLAPLRPA 892
Cdd:PHA03247 2741 PPAVPAGPAtpggPARPARPPTtAGPPAPAPPAAP-AAGPPRRLTRpavasLSESRESLPSPWDPADPPAAVLAP 2814
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 235-412 1.54e-05

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: 47.03  E-value: 1.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 235 EKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwNDMDKCS--VSQDPFTS-----------LHEFLDWRKmkllPRKSH 300
Cdd:cd04271  21 EEARRNILNNVNSASQLYEsSFNISLGLRNLTI-SDASCPStaVDSAPWNLpcnsrididdrLSIFSQWRG----QQPDD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885 301 DNA--QLVSGVYfQGTTIGMAPIMSMCTADQSGGIVMDHSdNPLGAAVT------LAHELGHNFGMNHDTlDRGCSCQMA 372
Cdd:cd04271  96 GNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDC-TSGTCSDGS 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 73747885 373 VEKGGC--------------IMNASTGYPFpMVFSSCSRKDLETSLEKG--MGVCL 412
Cdd:cd04271 173 VGSQQCcplststcdangqyIMNPSSSSGI-TEFSPCTIGNICSLLGRNpvRTSCL 227
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 288-400 3.07e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 44.00  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885  288 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 366
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 73747885  367 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 400
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-893 4.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   750 RCVRPSRPPRGFQPcQAHLGHLGKGLMRKPPDSYPPKDNPRR------------LLQCQNVDISRPLNGLNVPQPQ--ST 815
Cdd:PHA03247 2585 RARRPDAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPDppppspspaanePDPHPPPTVPPPERPRDDPAPGrvSR 2663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   816 QRVLPPLHRAPRAPSVPARPLPakPALRQAQGTCK-----PNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLR 890
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP 2741


                  ...
gi 73747885   891 PAP 893
Cdd:PHA03247 2742 PAV 2744
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 779-871 2.15e-03

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 38.91  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747885   779 PPDSYPPKDNPrrllqcqNVDISRPLnGLNVPQPQSTQRVLPPLHrAPRAPSVPARPLPAKPALRQAQGTckPNPPQKPL 858
Cdd:pfam12526  31 PPESAHPDPPP-------PVGDPRPP-VVDTPPPVSAVWVLPPPS-EPAAPEPDLVPPVTGPAGPPSPLA--PPAPAQKP 99

                          90
                  ....*....|...
gi 73747885   859 PADPLARTTRLTH 871
Cdd:pfam12526 100 PLPPPRPQRRLLH 112
 
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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