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Conserved domains on  [gi|767918205|ref|XP_011509509|]
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astacin-like metalloendopeptidase isoform X2 [Homo sapiens]

Protein Classification

zinc metalloprotease( domain architecture ID 1881)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 105-268 2.41e-76

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.


The actual alignment was detected with superfamily member cd04283:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 182  Bit Score: 235.23  E-value: 2.41e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYG------------------S 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGryafsingkptivpipdpN 159

                        170       180
                 ....*....|....*....|...
gi 767918205 246 VHIGQRWNLSASDITRVLKLYGC 268
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 255-410 6.72e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  255 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 330
Cdd:PHA03307   53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  331 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 410
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
 
Name Accession Description Interval E-value
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 105-268 2.41e-76

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 235.23  E-value: 2.41e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYG------------------S 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGryafsingkptivpipdpN 159

                        170       180
                 ....*....|....*....|...
gi 767918205 246 VHIGQRWNLSASDITRVLKLYGC 268
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-270 7.41e-60

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 192.88  E-value: 7.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205   97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGSVH---- 247
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAfskn 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767918205  248 ----------------IGQRWNLSASDITRVLKLYGCSP 270
Cdd:pfam01400 154 gslptivpkdndyqatIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 5.89e-37

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 131.32  E-value: 5.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205    96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918205   172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 255-410 6.72e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  255 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 330
Cdd:PHA03307   53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  331 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 410
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 277-408 2.04e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  277 GRGSHAHSTGRSPAPASLSLQrlleALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQPQTLASS 356
Cdd:pfam05109 447 GLPSSTHVPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767918205  357 PRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAgIQPVPVQGSPAlPGGCVP 408
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNA-TSPTPAVTTPT-PNATIP 572
 
Name Accession Description Interval E-value
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 105-268 2.41e-76

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 235.23  E-value: 2.41e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYG------------------S 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGryafsingkptivpipdpN 159

                        170       180
                 ....*....|....*....|...
gi 767918205 246 VHIGQRWNLSASDITRVLKLYGC 268
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 109-266 2.63e-69

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 217.05  E-value: 2.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 109 VPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKgrGIVLHE 188
Cdd:cd04280    4 VPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSL--GTIVHE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 189 LMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGSVH------------------ 247
Cdd:cd04280   82 LMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKyspDTVTTYGVPYDYGSVMHYGPTAfskngkptivpkdpgyqi 161

                        170
                 ....*....|....*....
gi 767918205 248 IGQRWNLSASDITRVLKLY 266
Cdd:cd04280  162 IGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-270 7.41e-60

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 192.88  E-value: 7.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205   97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGSVH---- 247
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAfskn 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767918205  248 ----------------IGQRWNLSASDITRVLKLYGCSP 270
Cdd:pfam01400 154 gslptivpkdndyqatIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 57-268 1.34e-44

Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells.


Pssm-ID: 239809 [Multi-domain]  Cd Length: 230  Bit Score: 154.55  E-value: 1.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  57 DKDIPAINQGLILEetpessfLIEGDI-IRPSPFRL-LSATSNKWPMggsgvvEVPFLLSSKYDEPSRQVILEALAEFER 134
Cdd:cd04282    9 DQDIFEINLGAGLD-------LFEGDIlLDEGQSRNgLIGDTYRWPF------PIPYILDDSLDLNAKGVILKAFEMYRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 135 STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNE 214
Cdd:cd04282   76 KSCVDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKA--TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767918205 215 ILPGFEINFIK---SQSSNMLTPYDYSSVMHYGSVH--------------------IGQRWNLSASDITRVLKLYGC 268
Cdd:cd04282  154 ILSGREHNFNKyddSFSTDLNTPYDYESVMHYSPFSfnkgaseptittkipefndiIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 93-268 3.08e-39

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 139.50  E-value: 3.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  93 SATSNKWPmggSGVVevPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISI-IPMYGCFSSVGRSG-GMQV 170
Cdd:cd04281    4 ARKERIWP---GGVI--PYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFtYRPCGCCSYVGRRGnGPQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 171 VSLAPTClqKGRGIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSS---NMLTPYDYSSVMHYG--- 244
Cdd:cd04281   79 ISIGKNC--DKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEevdSLGEPYDFDSIMHYArnt 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767918205 245 -----------------SVH--IGQRWNLSASDITRVLKLYGC 268
Cdd:cd04281  157 fsrgmfldtilpkrdpnGVRpeIGQRTRLSEGDIIQANKLYKC 199
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 5.89e-37

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 131.32  E-value: 5.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205    96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918205   172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-266 1.41e-19

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: 85.27  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 107 VEVPFLL--------SSKYDEPSRQVILEALAEFERSTCIRFV--TYQDQRDFIsIIPMY--------GCFSSVGRS--G 166
Cdd:cd00203    1 KVIPYVVvaddrdveEENLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADI-AILVTrqdfdggtGGWAYLGRVcdS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 167 GMQVVSLAPTCLQK--GRGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqSSNMLTPYDYSSVMHY- 243
Cdd:cd00203   80 LRGVGVLQDNQSGTkeGAQTIAHELGHALGFYHDHDRKDRDDYPTID----------------DTLNAEDDDYYSVMSYt 143

                        170       180
                 ....*....|....*....|....
gi 767918205 244 -GSVHIGQRWNLSASDITRVLKLY 266
Cdd:cd00203  144 kGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-266 1.53e-15

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 73.68  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 108 EVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRD------FISIIPMY-GCFSSVGRSGGM--QVVSLAPTCL 178
Cdd:cd04268    3 PITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirysVIRWIPYNdGTWSYGPSQVDPltGEILLARVYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 179 QKG---------RGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqssnmLTPYDYSSVMHYGSVHI- 248
Cdd:cd04268   83 YSSfveysgarlRNTAEHELGHALGLRHNFAASDRDDNVDLL--------------------AEKGDTSSVMDYAPSNFs 142

                        170       180
                 ....*....|....*....|...
gi 767918205 249 -----GQRWNLSASDITRVLKLY 266
Cdd:cd04268  143 iqlgdGQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 98-266 2.78e-07

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 50.84  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  98 KWPMGGsgVVEVPFLLSSkyDEPSRQVILEALAEFER--STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGgMQVVSLAP 175
Cdd:cd04327    2 LWRNGT--VLRIAFLGGP--DAFLKDKVRAAAREWLPyaNLKFKFVTDADADIRISFTPGDGYWSYVGTDA-LLIGADAP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 176 T----------CLQKGRGIVLHELMHVLGFWHEHTRAD----------RDRYIR--VNWNEILPgfEINFIKSQSSNML- 232
Cdd:cd04327   77 TmnlgwftddtPDPEFSRVVLHEFGHALGFIHEHQSPAanipwdkeavYAYFSGppNWDRETVI--NHNVFAKLDDGDVa 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767918205 233 -TPYDYSSVMHY---GSVHIGQR---WN--LSASDITRVLKLY 266
Cdd:cd04327  155 ySPYDPDSIMHYpfpGSLTLDGEevpPNrtLSDKDKAFMRLLY 197
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 255-410 6.72e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  255 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 330
Cdd:PHA03307   53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  331 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 410
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 277-408 2.04e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  277 GRGSHAHSTGRSPAPASLSLQrlleALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQPQTLASS 356
Cdd:pfam05109 447 GLPSSTHVPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767918205  357 PRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAgIQPVPVQGSPAlPGGCVP 408
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNA-TSPTPAVTTPT-PNATIP 572
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 270-405 4.91e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 270 PSGPRPRG--RGSHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASA 347
Cdd:PRK07764 624 PAAPAPAGaaAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP 703

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767918205 348 RQPQTLASSPRSRPGAGAPGVAQEQSwlagvstkptvPSSEAGIQPVPVQGSPALPGG 405
Cdd:PRK07764 704 APAATPPAGQADDPAAQPPQAAQGAS-----------APSPAADDPVPLPPEPDDPPD 750
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 107-201 7.30e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 39.75  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 107 VEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTY--QDQRDFISI--------------IPMYG-CFSSVGRSGGMQ 169
Cdd:cd04279    8 IDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIffdrpppvggagggLARAGfPLISDGNRKLFN 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767918205 170 VVSLA--------PTCLQkgrGIVLHELMHVLGFWHEHTR 201
Cdd:cd04279   88 RTDINlgpgqprgAENLQ---AIALHELGHALGLWHHSDR 124
PHA03247 PHA03247
large tegument protein UL36; Provisional
 270-412 9.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  270 PSGPRPRGRGSHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSgSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQ 349
Cdd:PHA03247 2593 PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG 2671

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918205  350 PQTLASSP--RSRPGAGAPGVAQeqswLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRNHF 412
Cdd:PHA03247 2672 RAAQASSPpqRPRRRAARPTVGS----LTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 295-398 4.34e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 39.04  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 295 SLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAeasARQPQTLASSPrsRPGAGAPGVAqeqsw 374
Cdd:PRK13729 108 KLGQDNAALAEQVKALGANPVTATGEPVPQMPASPPGPEGEPQPGNTPV---SFPPQGSVAVP--PPTAFYPGNG----- 177

                         90       100
                 ....*....|....*....|....
gi 767918205 375 lagvstkpTVPSSEAGIQPVPVQG 398
Cdd:PRK13729 178 --------VTPPPQVTYQSVPVPN 193
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 267-369 7.33e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.45  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205 267 GCSPSgPRPRGRG-SHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWEspalkklSAEA 345
Cdd:PHA03264 272 GGSPA-PPGDDRPeAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRPEGWP-------SLEA 343

                         90       100
                 ....*....|....*....|....*.
gi 767918205 346 SARQPQTLAS--SPRSRPGAGAPGVA 369
Cdd:PHA03264 344 ITFPPPTPATpaVPRARPVIVGTGIA 369
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 269-405 7.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 38.61  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918205  269 SPSGPRPRGRGSHaHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASAR 348
Cdd:PHA03307  247 CGWGPENECPLPR-PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767918205  349 QPQTLASSPRSRPGAGAPGVAQEQSwlaGVSTKP----TVPSSEAGIQPVPVQGSPALPGG 405
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRS---PSPSRPpppaDPSSPRKRPRPSRAPSSPAASAG 383
 
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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