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Conserved domains on  [gi|117606341|ref|NP_031426|]
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disintegrin and metalloproteinase domain-containing protein 12 preproprotein [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 ...
 212-414 8.70e-103

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: 317.32  E-value: 8.70e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIK 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  292 LLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGCSCRmaa 371
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 117606341  372 EKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKGMGMCLFNLP 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
508-650 5.88e-56

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 189.11  E-value: 5.88e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   508 DGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSkSAFAKCELRDAKCGKIQCQGGA 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117606341   588 SRPVIGTNAVSIETNIpqqegGRILCRGTHVYLGDDmPDPGLVLAGTKCAEGKICLNRRCQNI 650
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-161 5.39e-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: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   64 DHPDVLTVQLQLESRDLILSLERNEGLIANGFTETHYLQDGTDVSLTRNHTDHCYYHGHVQGDAASVVSLSTCSGLRGLI 143
Cdd:pfam01562  22 TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFI 101

                          90
                  ....*....|....*...
gi 117606341  144 MFENKTYSLEPMKNTTDS 161
Cdd:pfam01562 102 RTENEEYLIEPLEKYSRE 119
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 437-505 1.35e-28

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: 109.32  E-value: 1.35e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117606341   437 DCGEPEECTNRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVY 505
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 796-897 5.29e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  796 ISRPLDARAVPQLQsPQRvllplhqtPRAPSGPARPLPASPAvrQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQ 875
Cdd:PHA03247 2891 VSRSTESFALPPDQ-PER--------PPQPQAPPPPQPQPQP--PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959

                          90       100
                  ....*....|....*....|....
gi 117606341  876 QEP--GHRPAPIRPAPKHQVPRPS 897
Cdd:PHA03247 2960 PQPwlGALVPGRVAVPRFRVPQPA 2983
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-414 8.70e-103

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: 317.32  E-value: 8.70e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIK 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  292 LLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGCSCRmaa 371
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 117606341  372 EKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKGMGMCLFNLP 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-412 5.85e-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: 304.54  E-value: 5.85e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIK 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 292 LLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTleRGCSCRMaa 371
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 117606341 372 ekGGCIMNPSTGFPfPMVFSSCSRKDLEASLEKGMGMCLFN 412
Cdd:cd04269  157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
508-650 5.88e-56

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 189.11  E-value: 5.88e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   508 DGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSkSAFAKCELRDAKCGKIQCQGGA 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117606341   588 SRPVIGTNAVSIETNIpqqegGRILCRGTHVYLGDDmPDPGLVLAGTKCAEGKICLNRRCQNI 650
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 508-618 9.37e-43

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: 150.84  E-value: 9.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  508 DGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSKSaFAKCELRDAKCGKIQCQGGA 587
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 117606341  588 SRPVIGTNAVSIETNIPQQeggriLCRGTHV 618
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGV-----TCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-161 5.39e-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: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   64 DHPDVLTVQLQLESRDLILSLERNEGLIANGFTETHYLQDGTDVSLTRNHTDHCYYHGHVQGDAASVVSLSTCSGLRGLI 143
Cdd:pfam01562  22 TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFI 101

                          90
                  ....*....|....*...
gi 117606341  144 MFENKTYSLEPMKNTTDS 161
Cdd:pfam01562 102 RTENEEYLIEPLEKYSRE 119
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 437-505 1.35e-28

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: 109.32  E-value: 1.35e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117606341   437 DCGEPEECTNRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVY 505
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
441-503 1.71e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 106.17  E-value: 1.71e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117606341  441 PEECT-NRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPAN 503
Cdd:pfam00200  11 LEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
 796-897 5.29e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  796 ISRPLDARAVPQLQsPQRvllplhqtPRAPSGPARPLPASPAvrQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQ 875
Cdd:PHA03247 2891 VSRSTESFALPPDQ-PER--------PPQPQAPPPPQPQPQP--PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959

                          90       100
                  ....*....|....*....|....
gi 117606341  876 QEP--GHRPAPIRPAPKHQVPRPS 897
Cdd:PHA03247 2960 PQPwlGALVPGRVAVPRFRVPQPA 2983
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 751-902 1.98e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  751 HPSRTPSGPHLGQAHHTPgkgllmnraPHFNTPkdrHSLKCQNMDISRPldaravPQLQSPQRVLLPLHQTPRAPSGPAR 830
Cdd:pfam09770 214 PAPAPAQPPAAPPAQQAQ---------QQQQFP---PQIQQQQQPQQQP------QQPQQHPGQGHPVTILQRPQSPQPD 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117606341  831 PlPASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQQEPGHRPAPIRPAPKHQvPRPSHNAYI 902
Cdd:pfam09770 276 P-AQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQ-GSFGRQAPI 345
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 286-398 8.98e-05

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: 45.93  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 286 DWRKIKLLPRKSHDNAQLISGVYFQGTTIGMApimSMCTAEQSGGVVMDHSDSPlgAAVTLAHELGHNFGMNHDTLERG- 364
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 117606341 365 CScrmaaEKGGCIMNPSTGFPFPMVFSSCSRKDL 398
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-414 8.70e-103

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: 317.32  E-value: 8.70e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIK 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  292 LLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGCSCRmaa 371
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 117606341  372 EKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKGMGMCLFNLP 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-412 5.85e-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: 304.54  E-value: 5.85e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIK 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 292 LLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTleRGCSCRMaa 371
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 117606341 372 ekGGCIMNPSTGFPfPMVFSSCSRKDLEASLEKGMGMCLFN 412
Cdd:cd04269  157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
508-650 5.88e-56

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 189.11  E-value: 5.88e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   508 DGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSkSAFAKCELRDAKCGKIQCQGGA 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117606341   588 SRPVIGTNAVSIETNIpqqegGRILCRGTHVYLGDDmPDPGLVLAGTKCAEGKICLNRRCQNI 650
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 508-618 9.37e-43

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: 150.84  E-value: 9.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  508 DGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSKSaFAKCELRDAKCGKIQCQGGA 587
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 117606341  588 SRPVIGTNAVSIETNIPQQeggriLCRGTHV 618
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGV-----TCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 212-403 3.16e-36

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: 135.24  E-value: 3.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 212 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYR----PLNIRIVLVGVEVWN-DIDKCSISQDPFTSLHEFLD 286
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKgEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 287 WRKIKllpRKSHDNAQLISGVYF-QGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAaVTLAHELGHNFGMNHDTleRGC 365
Cdd:cd04267   81 WRAEG---PIRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTA-LTMAHELGHNLGAEHDG--GDE 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 117606341 366 SCRMAAEKGGCIMNPSTGFPFPMVFSSCSRKDLEASLE 403
Cdd:cd04267  155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 212-411 1.12e-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: 128.51  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 212 KYVELVIVADNREFQRQGKdlEKVKQRLIEIANHVDKFYR-PL---NIRIVLVGVEVWNDIDK-CSISQDPFTSLHEFLD 286
Cdd:cd04273    1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 287 WRKiKLLPR-----KSHDNAQLISGVYFQG-----TTIGMAPIMSMCTAEQSGGVVMDHsdsPLGAAVTLAHELGHNFGM 356
Cdd:cd04273   79 WQK-KLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLGM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 117606341 357 NHDTLERGCScrmAAEKGGCIMNPSTGFPF-PMVFSSCSRKDLEASLEKGMGMCLF 411
Cdd:cd04273  155 PHDGDGNSCG---PEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-161 5.39e-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: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341   64 DHPDVLTVQLQLESRDLILSLERNEGLIANGFTETHYLQDGTDVSLTRNHTDHCYYHGHVQGDAASVVSLSTCSGLRGLI 143
Cdd:pfam01562  22 TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFI 101

                          90
                  ....*....|....*...
gi 117606341  144 MFENKTYSLEPMKNTTDS 161
Cdd:pfam01562 102 RTENEEYLIEPLEKYSRE 119
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 437-505 1.35e-28

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: 109.32  E-value: 1.35e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117606341   437 DCGEPEECTNRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVY 505
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
441-503 1.71e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 106.17  E-value: 1.71e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117606341  441 PEECT-NRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPAN 503
Cdd:pfam00200  11 LEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-383 1.22e-19

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 87.86  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  211 TKYVELVIVADNrEFqRQGKDLEKVKQRLIEIANHVD-KFYRPLNIRIVLVGVEVWN----DIDKCSISQDPFTSLHEFL 285
Cdd:pfam13688   2 TRTVALLVAADC-SY-VAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDstcpYTPPACSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  286 D---WRKikllpRKSHDNAQLISGVYFQGTtiGMAPIMSMCTAEQSGGVVMDHSD-----SPLGAAVTLAHELGHNFGMN 357
Cdd:pfam13688  80 DfsaWRG-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGnnvvvSTATEWQVFAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 117606341  358 HD----TLERGCSCRMAAEKGG--CIMNPSTG 383
Cdd:pfam13688 153 HDcdssTSSQCCPPSNSTCPAGgrYIMNPSSS 184
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 212-396 2.96e-16

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 77.18  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 212 KYVELVIVADNREFqrqgkDLEKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwndidkcsisqdpftslhefldwrki 290
Cdd:cd00203    1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 291 kllprKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGC----- 365
Cdd:cd00203   50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRddypt 124

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 117606341 366 -SCRMAAE--KGGCIMNPsTGFPFPMV----FSSCSRK 396
Cdd:cd00203  125 iDDTLNAEddDYYSVMSY-TKGSFSDGqrkdFSQCDID 161
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 239-359 3.50e-12

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: 63.93  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  239 LIEIANHVdkFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIkllpRKSHDNA---QLISGVYFQGTTiG 315
Cdd:pfam13582   6 LVNRANTI--YERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-G 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 117606341  316 MAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHD 359
Cdd:pfam13582  79 IAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 213-397 2.11e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 61.60  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 213 YVELVIVADnREFQRQGKDLEKVKQRLIEIANHVDKFYRPLN---IRIVLVGVEVWNDiDKCSISQDPFT--------SL 281
Cdd:cd04272    2 YPELFVVVD-YDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKD-PDFEPYIHPINygyidaaeTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 282 HEFLDWRKIKLLPRKShDNAQLISG----VYFQGT----TIGMAPIMSMCTaEQSGGVVMDHSDSPLGAaVTLAHELGHN 353
Cdd:cd04272   80 ENFNEYVKKKRDYFNP-DVVFLVTGldmsTYSGGSlqtgTGGYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMTHELAHL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 117606341 354 FGMNHDTLERGCSCRMAAEKGGC------IMNPSTGFPFPMVFSSCSRKD 397
Cdd:cd04272  157 LGAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQ 206
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 216-409 3.01e-09

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: 58.54  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 216 LVIVADNREFQRQGKDLEK-VKQRLIEIANHVDKFYRPLNirivlvgvevWND---------IDKCSISQDP-------F 278
Cdd:cd04270    5 LLLVADHRFYKYMGRGEEEtTINYLISHIDRVDDIYRNTD----------WDGggfkgigfqIKRIRIHTTPdevdpgnK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 279 TSLHEFLDWRKIKLLPRKSHDN-------AQLISGVYFQGTTIGMAPIMSMcTAEQSGGVVMDHSDSPLG---------- 341
Cdd:cd04270   75 FYNKSFPNWGVEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGSP-RDNSAGGICEKAYYYSNGkkkylntglt 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 342 -------------AAVTLAHELGHNFGMNHDTleRGCSCRMAAEKGG-CIMNPS--TGF-PFPMVFSSCSRKDLEASLEK 404
Cdd:cd04270  154 ttvnygkrvptkeSDLVTAHELGHNFGSPHDP--DIAECAPGESQGGnYIMYARatSGDkENNKKFSPCSKKSISKVLEV 231


                 ....*
gi 117606341 405 GMGMC 409
Cdd:cd04270  232 KSNSC 236
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 235-403 2.61e-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: 372637  Cd Length: 193  Bit Score: 54.94  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  235 VKQRLIEIANHVDKFYRP--LNIRIVLVGVEVWNDIDKCSISQDPFTS--------LHEFLDWRKikllpRKSHDNAQLI 304
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPddININGGLVNPGEIPATTSASDSGNNYCNspttivrrLNFLSQWRG-----EQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  305 SGVYFQGTTIGMAPIMSMC-TAEQSGGVVMDHSDS--------PLGAAVTLAHELGHNFGMNHD----TLERGCSCRMAA 371
Cdd:pfam13574  78 TMGTFSGGELGLAYVGQICqKGASSPKTNTGLSTTtnygsfnyPTQEWDVVAHEVGHNFGATHDcdgsQYASSGCERNAA 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 117606341  372 -----EKGGCIMNPSTGfPFPMVFSSCSRKDLEASLE 403
Cdd:pfam13574 158 tsvcsANGSFIMNPASK-SNNDLFSPCSISLICDVLG 193
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 211-380 2.65e-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: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  211 TKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFY-RPLNIRIVLVGVEVWNDIDKcsiSQDPFTSL---HEFLD 286
Cdd:pfam13583   1 TRRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRDVIYTDS---STDSFNADcsgGDLGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  287 WRKIKL---LPRKSHDNAQLISGVYFQGTTIGMAPIMSMC-TAEQS--GGVVMDHSDSPlgaaVTLAHELGHNFGMNHDT 360
Cdd:pfam13583  78 WRLATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakASGVARSRDEW----DIFAHEIGHTFGAVHDC 153

                         170       180
                  ....*....|....*....|..
gi 117606341  361 LERGCSCRMAAE--KGGCIMNP 380
Cdd:pfam13583 154 SSQGEGLSSSTEdgSGQTIMSY 175
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 310-394 1.57e-06

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: 50.11  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 310 QGTTIGMAPIMSMCTAEQSGGVVMDHSdSPLGAAVT------LAHELGHNFGMNHDTLERGCSCRMAAEKGGC------- 376
Cdd:cd04271  108 SGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCplststc 186

                         90       100
                 ....*....|....*....|....
gi 117606341 377 ------IMNPSTGFPFpMVFSSCS 394
Cdd:cd04271  187 dangqyIMNPSSSSGI-TEFSPCT 209
PHA03247 PHA03247
large tegument protein UL36; Provisional
 796-897 5.29e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  796 ISRPLDARAVPQLQsPQRvllplhqtPRAPSGPARPLPASPAvrQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQ 875
Cdd:PHA03247 2891 VSRSTESFALPPDQ-PER--------PPQPQAPPPPQPQPQP--PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959

                          90       100
                  ....*....|....*....|....
gi 117606341  876 QEP--GHRPAPIRPAPKHQVPRPS 897
Cdd:PHA03247 2960 PQPwlGALVPGRVAVPRFRVPQPA 2983
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 751-902 1.98e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.49  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  751 HPSRTPSGPHLGQAHHTPgkgllmnraPHFNTPkdrHSLKCQNMDISRPldaravPQLQSPQRVLLPLHQTPRAPSGPAR 830
Cdd:pfam09770 214 PAPAPAQPPAAPPAQQAQ---------QQQQFP---PQIQQQQQPQQQP------QQPQQHPGQGHPVTILQRPQSPQPD 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117606341  831 PlPASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQQEPGHRPAPIRPAPKHQvPRPSHNAYI 902
Cdd:pfam09770 276 P-AQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQ-GSFGRQAPI 345
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 286-398 8.98e-05

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: 45.93  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 286 DWRKIKLLPRKSHDNAQLISGVYFQGTTIGMApimSMCTAEQSGGVVMDHSDSPlgAAVTLAHELGHNFGMNHDTLERG- 364
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 117606341 365 CScrmaaEKGGCIMNPSTGFPFPMVFSSCSRKDL 398
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
 776-889 1.22e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  776 RAPHFNTPKDRHSLKCQNMDisRPLDARAVPQLQSPQRVLLPlHQTPRAPSGPARPLPasPAVRQAQG-----IRKPSPP 850
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPE--RPRDDPAPGRVSRPRRARRL-GRAAQASSPPQRPRR--RAARPTVGsltslADPPPPP 2705

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 117606341  851 QKPLPADPlsrtsRLTSALVRTPGQQEPGHR--PAPIRPAP 889
Cdd:PHA03247 2706 PTPEPAPH-----ALVSATPLPPGPAAARQAspALPAAPAP 2741
PHA03379 PHA03379
EBNA-3A; Provisional
 817-897 1.67e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.43  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 817 PLHQTPRAPSGPARPLPASPAVRQAQGIRKPSPPQK--------PLPADPLSRTsrLTSALVRTPGQQEPGHRPAPIRPA 888
Cdd:PHA03379 455 PLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDgrpacapvPAPAGPIVRP--WEASLSQVPGVAFAPVMPQPMPVE 532


                 ....*....
gi 117606341 889 PkhqVPRPS 897
Cdd:PHA03379 533 P---VPVPT 538
PHA03247 PHA03247
large tegument protein UL36; Provisional
 755-897 4.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  755 TPSGPHLGQAHHTPGKGllmnrAPHFNTPKDRHSLKCQNMDISRPLDARAVPQLQSPQRVLLPLHQTPrapsgpARPLPA 834
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAG-----PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP------AGPLPP 2830

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  835 SPAVRQAQGIRKPSPPQKPL-------PADPLSRtsrltsalvRTPGQQEPGHRPAPIRPaPKHQVPRPS 897
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPPPSLplggsvaPGGDVRR---------RPPSRSPAAKPAAPARP-PVRRLARPA 2890
PHA03247 PHA03247
large tegument protein UL36; Provisional
 823-896 4.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117606341  823 RAPSGPARPLPASPAVRQAQGIRKPSPPQK----PLPADPLSRTsrltsalvRTPGQQEPGHRPAPIRPAPKHQVPRP 896
Cdd:PHA03247 2865 RPPSRSPAAKPAAPARPPVRRLARPAVSRStesfALPPDQPERP--------PQPQAPPPPQPQPQPPPPPQPQPPPP 2934
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-897 7.72e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341  752 PSRTPSGPHLGQAHHTPGKGLLMNR---APHFNTPKDRHSLKCQNMDISRPLDA---RAVPQLQSPQRVLLPLHQTPRAP 825
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRddpAPGRVSRPRRARRLGRAAQASSPPQRprrRAARPTVGSLTSLADPPPPPPTP 2708

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117606341  826 SGPARPL-PASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQ-QEPGHRPAPIRPA-----PKHQVPRPS 897
Cdd:PHA03247 2709 EPAPHALvSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARpPTTAGPPAPAPPAapaagPPRRLTRPA 2787
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 804-878 1.03e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 42.13  E-value: 1.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117606341 804 AVPQLQSPQRVLlPLHQTPRAPSGPARPLPASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALV----RTPGQQEP 878
Cdd:PLN02983 140 ALPQPPPPAPVV-MMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKSSHPPLKSPMAgtfyRSPAPGEP 217
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
801-900 1.74e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117606341 801 DARAVPQLQSPQRVLLPLHQTPRAPsgPARPLPASPAVRQAQGIRKPSPPQKPLPADPLS------RTSRLTSALVRTP- 873
Cdd:PRK12323 382 VAQPAPAAAAPAAAAPAPAAPPAAP--AAAPAAAAAARAVAAAPARRSPAPEALAAARQAsargpgGAPAPAPAPAAAPa 459

                         90       100
                 ....*....|....*....|....*..
gi 117606341 874 GQQEPGHRPAPIRPAPKHQVPRPSHNA 900
Cdd:PRK12323 460 AAARPAAAGPRPVAAAAAAAPARAAPA 486
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 822-897 4.72e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117606341 822 PRAPSGPARPLPASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQQEPGHRPAPIRPAPKHQVPRPS 897
Cdd:PRK07764 406 PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 342-383 7.91e-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: 38.43  E-value: 7.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 117606341 342 AAVTLAHELGHNFGMNHdtlergcsCRMAAekggCIMNPSTG 383
Cdd:cd11375  123 LLKEAVHELGHLFGLDH--------CPYYA----CVMNFSNS 152
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 298-367 9.68e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 38.47  E-value: 9.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117606341 298 HDNAQLISGV-YFQGTTIGMAPIMsmctaeqsGGVVMDH------SDSPLGAAVTLAHELGHNFGMNHdTLERGCSC 367
Cdd:cd04275   94 NFLGGGLLGYaTFPDSLVSLAFIT--------DGVVINPsslpggSAAPYNLGDTATHEVGHWLGLYH-TFQGGSPC 161
 
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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