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Conserved domains on  [gi|2462573404|ref|XP_054198100|]
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astacin-like metalloendopeptidase isoform X1 [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 ...
 105-286 1.17e-88

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: 267.21  E-value: 1.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283     2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPS 263
Cdd:cd04283    80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDPN 159

                         170       180
                  ....*....|....*....|...
gi 2462573404 264 VHIGQRWNLSASDITRVLKLYGC 286
Cdd:cd04283   160 VPIGQRQGMSNLDILRINKLYNC 182
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 273-428 9.97e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 9.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  273 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 348
Cdd:PHA03307    53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  349 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 428
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 ...
 105-286 1.17e-88

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: 267.21  E-value: 1.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283     2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPS 263
Cdd:cd04283    80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDPN 159

                         170       180
                  ....*....|....*....|...
gi 2462573404 264 VHIGQRWNLSASDITRVLKLYGC 286
Cdd:cd04283   160 VPIGQRQGMSNLDILRINKLYNC 182
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-288 2.90e-68

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: 215.22  E-value: 2.90e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGRLAFSRR 251
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAFSKN 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462573404 252 G-LPTITPL-WAPSVHIGQRWNLSASDITRVLKLYGCSP 288
Cdd:pfam01400 154 GsLPTIVPKdNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 8.05e-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: 8.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404   96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462573404  172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 273-428 9.97e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 9.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  273 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 348
Cdd:PHA03307    53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  349 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 428
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 295-426 2.27e-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: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 295 GRGSHAHSTGRSPAPASLSLQrlleALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQPQTLASS 374
Cdd:pfam05109 447 GLPSSTHVPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462573404 375 PRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAgIQPVPVQGSPAlPGGCVP 426
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 ...
 105-286 1.17e-88

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: 267.21  E-value: 1.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283     2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPS 263
Cdd:cd04283    80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDPN 159

                         170       180
                  ....*....|....*....|...
gi 2462573404 264 VHIGQRWNLSASDITRVLKLYGC 286
Cdd:cd04283   160 VPIGQRQGMSNLDILRINKLYNC 182
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 109-284 7.12e-80

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: 244.79  E-value: 7.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 109 VPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKgrGIVLHE 188
Cdd:cd04280     4 VPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSL--GTIVHE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 189 LMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVH 265
Cdd:cd04280    82 LMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKyspDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGYQI 161

                         170
                  ....*....|....*....
gi 2462573404 266 IGQRWNLSASDITRVLKLY 284
Cdd:cd04280   162 IGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-288 2.90e-68

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: 215.22  E-value: 2.90e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGRLAFSRR 251
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAFSKN 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462573404 252 G-LPTITPL-WAPSVHIGQRWNLSASDITRVLKLYGCSP 288
Cdd:pfam01400 154 GsLPTIVPKdNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 57-286 7.02e-49

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: 166.49  E-value: 7.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  57 DKDIPAINQGLILEetpessfLIEGDI-IRPSPFRL-LSATSNKWPMggsgvvEVPFLLSSKYDEPSRQVILEALAEFER 134
Cdd:cd04282     9 DQDIFEINLGAGLD-------LFEGDIlLDEGQSRNgLIGDTYRWPF------PIPYILDDSLDLNAKGVILKAFEMYRL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 135 STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNE 214
Cdd:cd04282    76 KSCVDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKA--TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462573404 215 ILPGFEINFIK---SQSSNMLTPYDYSSVMHYGRLAFSR-RGLPTITPLwAPSVH--IGQRWNLSASDITRVLKLYGC 286
Cdd:cd04282   154 ILSGREHNFNKyddSFSTDLNTPYDYESVMHYSPFSFNKgASEPTITTK-IPEFNdiIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 93-286 1.22e-45

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: 156.83  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  93 SATSNKWPmggSGVVevPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISI-IPMYGCFSSVGRSG-GMQV 170
Cdd:cd04281     4 ARKERIWP---GGVI--PYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFtYRPCGCCSYVGRRGnGPQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 171 VSLAPTClqKGRGIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSS---NMLTPYDYSSVMHYGRLA 247
Cdd:cd04281    79 ISIGKNC--DKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEevdSLGEPYDFDSIMHYARNT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462573404 248 FSRRG-LPTITPLWAPS---VHIGQRWNLSASDITRVLKLYGC 286
Cdd:cd04281   157 FSRGMfLDTILPKRDPNgvrPEIGQRTRLSEGDIIQANKLYKC 199
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 8.05e-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: 8.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404   96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462573404  172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-284 2.22e-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: 82.18  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 107 VEVPFLL--------SSKYDEPSRQVILEALAEFERSTCIRFV--TYQDQRDFIsIIPMY--------GCFSSVGRS--G 166
Cdd:cd00203     1 KVIPYVVvaddrdveEENLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADI-AILVTrqdfdggtGGWAYLGRVcdS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 167 GMQVVSLAPTCLQK--GRGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqSSNMLTPYDYSSVMHYg 244
Cdd:cd00203    80 LRGVGVLQDNQSGTkeGAQTIAHELGHALGFYHDHDRKDRDDYPTID----------------DTLNAEDDDYYSVMSY- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462573404 245 rlafsrrglptitplWAPSVHIGQRWNLSASDITRVLKLY 284
Cdd:cd00203   143 ---------------TKGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-284 2.30e-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: 73.30  E-value: 2.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 108 EVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRD------FISIIPMY-GCFSSVGRSGGM--QVVSLAPTCL 178
Cdd:cd04268     3 PITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirysVIRWIPYNdGTWSYGPSQVDPltGEILLARVYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 179 QKG---------RGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqssnmLTPYDYSSVMHYGRLAFS 249
Cdd:cd04268    83 YSSfveysgarlRNTAEHELGHALGLRHNFAASDRDDNVDLL--------------------AEKGDTSSVMDYAPSNFS 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462573404 250 RRGLPTITPlwapsvhigqrwNLSASDITRVLKLY 284
Cdd:cd04268   143 IQLGDGQKY------------TIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 98-284 2.77e-06

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: 47.76  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  98 KWPMGGsgVVEVPFLLSSkyDEPSRQVILEALAEFER--STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGgMQVVSLAP 175
Cdd:cd04327     2 LWRNGT--VLRIAFLGGP--DAFLKDKVRAAAREWLPyaNLKFKFVTDADADIRISFTPGDGYWSYVGTDA-LLIGADAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 176 T----------CLQKGRGIVLHELMHVLGFWHEHTRAD----------RDRYIR--VNWNEILPgfEINFIKSQSSNML- 232
Cdd:cd04327    77 TmnlgwftddtPDPEFSRVVLHEFGHALGFIHEHQSPAanipwdkeavYAYFSGppNWDRETVI--NHNVFAKLDDGDVa 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462573404 233 -TPYDYSSVMHYG-RLAFSRRGLPTITPLwapsvhigqrwNLSASDITRVLKLY 284
Cdd:cd04327   155 ySPYDPDSIMHYPfPGSLTLDGEEVPPNR-----------TLSDKDKAFMRLLY 197
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 273-428 9.97e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 9.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  273 SASDITRVLKLYGCSPSGPRPRGRgsHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQP----VPAGPGESP 348
Cdd:PHA03307    53 VTVVAGAAACDRFEPPTGPPPGPG--TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPpptpPPASPPPSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  349 HGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRN 428
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 295-426 2.27e-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: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 295 GRGSHAHSTGRSPAPASLSLQrlleALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQPQTLASS 374
Cdd:pfam05109 447 GLPSSTHVPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462573404 375 PRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAgIQPVPVQGSPAlPGGCVP 426
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNA-TSPTPAVTTPT-PNATIP 572
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 288-423 6.30e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 288 PSGPRPRG--RGSHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASA 365
Cdd:PRK07764  624 PAAPAPAGaaAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP 703

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462573404 366 RQPQTLASSPRSRPGAGAPGVAQEQSwlagvstkptvPSSEAGIQPVPVQGSPALPGG 423
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 9.48e-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: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 107 VEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTY--QDQRDFISI--------------IPMYG-CFSSVGRSGGMQ 169
Cdd:cd04279     8 IDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIffdrpppvggagggLARAGfPLISDGNRKLFN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462573404 170 VVSLA--------PTCLQkgrGIVLHELMHVLGFWHEHTR 201
Cdd:cd04279    88 RTDINlgpgqprgAENLQ---AIALHELGHALGLWHHSDR 124
PHA03247 PHA03247
large tegument protein UL36; Provisional
 288-430 1.32e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  288 PSGPRPRGRGSHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSgSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQ 367
Cdd:PHA03247  2593 PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG 2671

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462573404  368 PQTLASSP--RSRPGAGAPGVAQeqswLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRNHF 430
Cdd:PHA03247  2672 RAAQASSPpqRPRRRAARPTVGS----LTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 258-420 3.36e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  258 PLWAPSVHIGQRWNLSASDITRVLKLYGCSPSGPRPRGRG---SHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSS 334
Cdd:PHA03307   258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSpspSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404  335 AGGQPVPAGPGESP-----HGWESPALKKlSAEASARQPQTLASSP------RSRPGAGAPGVAQEQSWLAGVSTKPTVP 403
Cdd:PHA03307   338 GAAVSPGPSPSRSPspsrpPPPADPSSPR-KRPRPSRAPSSPAASAgrptrrRARAAVAGRARRRDATGRFPAGRPRPSP 416

                          170
                   ....*....|....*..
gi 2462573404  404 SSEAGIQPVPVQGSPAL 420
Cdd:PHA03307   417 LDAGAASGAFYARYPLL 433
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 313-416 4.27e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 39.42  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573404 313 SLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAeasARQPQTLASSPrsRPGAGAPGVAqeqsw 392
Cdd:PRK13729  108 KLGQDNAALAEQVKALGANPVTATGEPVPQMPASPPGPEGEPQPGNTPV---SFPPQGSVAVP--PPTAFYPGNG----- 177

                          90       100
                  ....*....|....*....|....
gi 2462573404 393 lagvstkpTVPSSEAGIQPVPVQG 416
Cdd:PRK13729  178 --------VTPPPQVTYQSVPVPN 193
 
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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