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Conserved domains on  [gi|215500424|gb|EEC09918|]
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metalloprotease, putative [Ixodes scapularis]

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 ...
 10-223 1.11e-53

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 cd04272:

Pssm-ID: 469599  Cd Length: 220  Bit Score: 171.77  E-value: 1.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  10 ITPEVHLLIDSALESKFNDTESIVKYYAIFAAFVNLKFKTLEEwLDVQLVMTKITIFTKRTETFIKKPPANESVIMTDSL 89
Cdd:cd04272    1 VYPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKS-PRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  90 EYLMNYTQNENEFKEDDIVVLLTGLNIASYNSTTKKvesEGILGYAYVGGACRSSKVGMVEDEANMFTGTHTFVHEVGHL 169
Cdd:cd04272   80 ENFNEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQ---TGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215500424 170 LGMSHDGDGPPESVTDSPGASYCNASDGYIMapSYHVNST--HIFSVCSADQLEAF 223
Cdd:cd04272  157 LGAPHDGSPPPSWVKGHPGSLDCPWDDGYIM--SYVVNGErqYRFSQCSQRQIRNV 210
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 10-223 1.11e-53

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 171.77  E-value: 1.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  10 ITPEVHLLIDSALESKFNDTESIVKYYAIFAAFVNLKFKTLEEwLDVQLVMTKITIFTKRTETFIKKPPANESVIMTDSL 89
Cdd:cd04272    1 VYPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKS-PRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  90 EYLMNYTQNENEFKEDDIVVLLTGLNIASYNSTTKKvesEGILGYAYVGGACRSSKVGMVEDEANMFTGTHTFVHEVGHL 169
Cdd:cd04272   80 ENFNEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQ---TGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215500424 170 LGMSHDGDGPPESVTDSPGASYCNASDGYIMapSYHVNST--HIFSVCSADQLEAF 223
Cdd:cd04272  157 LGAPHDGSPPPSWVKGHPGSLDCPWDDGYIM--SYVVNGErqYRFSQCSQRQIRNV 210
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
55-209 8.93e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 8.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424   55 DVQLVMTKITIFTkrtETFIKKPPANESVimtDSLEYLMNYT-QNENEFKE-DDIVVLLTGLNiasyNSTTkkvesegil 132
Cdd:pfam13688  44 NISLGLVNLTISD---STCPYTPPACSTG---DSSDRLSEFQdFSAWRGTQnDDLAYLFLMTN----CSGG--------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  133 GYAYVGGACRSSKVGMVEDEANM-------FTGTHTFVHEVGHLLGMSHDGDGPPESVTDSPGASYCNASDGYIMAPSYH 205
Cdd:pfam13688 105 GLAWLGQLCNSGSAGSVSTRVSGnnvvvstATEWQVFAHEIGHNFGAVHDCDSSTSSQCCPPSNSTCPAGGRYIMNPSSS 184


                  ....
gi 215500424  206 VNST 209
Cdd:pfam13688 185 PNST 188
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 10-223 1.11e-53

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 171.77  E-value: 1.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  10 ITPEVHLLIDSALESKFNDTESIVKYYAIFAAFVNLKFKTLEEwLDVQLVMTKITIFTKRTETFIKKPPANESVIMTDSL 89
Cdd:cd04272    1 VYPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKS-PRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  90 EYLMNYTQNENEFKEDDIVVLLTGLNIASYNSTTKKvesEGILGYAYVGGACRSSKVGMVEDEANMFTGTHTFVHEVGHL 169
Cdd:cd04272   80 ENFNEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQ---TGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215500424 170 LGMSHDGDGPPESVTDSPGASYCNASDGYIMapSYHVNST--HIFSVCSADQLEAF 223
Cdd:cd04272  157 LGAPHDGSPPPSWVKGHPGSLDCPWDDGYIM--SYVVNGErqYRFSQCSQRQIRNV 210
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 106-223 9.38e-19

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: 80.75  E-value: 9.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424 106 DIVVLLTGLNIASYNSTTkkveseGILGYAYVGGAC-RSSKVGMVEDeaNMFTGTHTFVHEVGHLLGMSHDGDGppesvt 184
Cdd:cd04273   95 DHAILLTRQDICRSNGNC------DTLGLAPVGGMCsPSRSCSINED--TGLSSAFTIAHELGHVLGMPHDGDG------ 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 215500424 185 dspgaSYC--NASDGYIMAP--SYHVNSTHiFSVCSADQLEAF 223
Cdd:cd04273  161 -----NSCgpEGKDGHIMSPtlGANTGPFT-WSKCSRRYLTSF 197
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 13-223 1.10e-18

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: 80.16  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  13 EVHLLIDSALESKFNDTESIVKYY-AIFAAFVNLKFKTLEEWLDVQLVMTKITIFtkRTETFIKKPPANESVimtdsley 91
Cdd:cd04267    4 ELVVVADHRMVSYFNSDENILQAYiTELINIANSIYRSTNLRLGIRISLEGLQIL--KGEQFAPPIDSDASN-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  92 lmnyTQNENEFKE------DDIVVLLTGLNIasynsttkkvESEGILGYAYVGGACRS-SKVGMVEDEANMFTGTHTFVH 164
Cdd:cd04267   74 ----TLNSFSFWRaegpirHDNAVLLTAQDF----------IEGDILGLAYVGSMCNPySSVGVVEDTGFTLLTALTMAH 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215500424 165 EVGHLLGMSHDGDgpPESVTDspgasyCNASDGYIMAPSyhVNSTHI--FSVCSADQLEAF 223
Cdd:cd04267  140 ELGHNLGAEHDGG--DELAFE------CDGGGNYIMAPV--DSGLNSyrFSQCSIGSIREF 190
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 13-223 1.01e-14

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: 69.57  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  13 EVHLLIDSALESKFNDTESIVKYYAI-FAAFVNLKFKTLeewlDVQLVMTKITIFTKRtetfikkppaNESVIMTDS--- 88
Cdd:cd04269    4 ELVVVVDNSLYKKYGSNLSKVRQRVIeIVNIVDSIYRPL----NIRVVLVGLEIWTDK----------DKISVSGDAget 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  89 LEYLMNYTQNE-NEFKEDDIVVLLTGLNiasYNSTTkkvesegiLGYAYVGGAC-RSSKVGMVED-EANMFTGTHTFVHE 165
Cdd:cd04269   70 LNRFLDWKRSNlLPRKPHDNAQLLTGRD---FDGNT--------VGLAYVGGMCsPKYSGGVVQDhSRNLLLFAVTMAHE 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 215500424 166 VGHLLGMSHDGdgppesvtdspgaSYCN-ASDGYIMAPsYHVNSTHIFSVCSADQLEAF 223
Cdd:cd04269  139 LGHNLGMEHDD-------------GGCTcGRSTCIMAP-SPSSLTDAFSNCSYEDYQKF 183
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
55-209 8.93e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 8.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424   55 DVQLVMTKITIFTkrtETFIKKPPANESVimtDSLEYLMNYT-QNENEFKE-DDIVVLLTGLNiasyNSTTkkvesegil 132
Cdd:pfam13688  44 NISLGLVNLTISD---STCPYTPPACSTG---DSSDRLSEFQdFSAWRGTQnDDLAYLFLMTN----CSGG--------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  133 GYAYVGGACRSSKVGMVEDEANM-------FTGTHTFVHEVGHLLGMSHDGDGPPESVTDSPGASYCNASDGYIMAPSYH 205
Cdd:pfam13688 105 GLAWLGQLCNSGSAGSVSTRVSGnnvvvstATEWQVFAHEIGHNFGAVHDCDSSTSSQCCPPSNSTCPAGGRYIMNPSSS 184


                  ....
gi 215500424  206 VNST 209
Cdd:pfam13688 185 PNST 188
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 13-223 2.98e-12

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: 63.09  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424   13 EVHLLIDSALESKFNDTESIVKYYAI-FAAFVNLKFKTLeewlDVQLVMTKITIFTKRtetfikkppaNESVIMTDSLEY 91
Cdd:pfam01421   4 ELFIVVDKQLFQKMGSDTTVVRQRVFqVVNLVNSIYKEL----NIRVVLVGLEIWTDE----------DKIDVSGDANDT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424   92 LMNYTQNENEF----KEDDIVVLLTGLNIasYNSTTkkvesegilGYAYVGGAC-RSSKVGMVED-EANMFTGTHTFVHE 165
Cdd:pfam01421  70 LRNFLKWRQEYlkkrKPHDVAQLLSGVEF--GGTTV---------GAAYVGGMCsLEYSGGVNEDhSKNLESFAVTMAHE 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 215500424  166 VGHLLGMSHDgdgppesvtDSPGASYCNASDGYIMAPSYHVNSTHIFSVCSADQLEAF 223
Cdd:pfam01421 139 LGHNLGMQHD---------DFNGGCKCPPGGGCIMNPSAGSSFPRKFSNCSQEDFEQF 187
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 121-224 6.01e-11

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 59.56  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  121 STTKKVESEGILGYAYVGGAC------RSSKVGMV---EDEANMFTGTH--TFVHEVGHLLGMSHDGDG---PPESVTDS 186
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICqkgassPKTNTGLStttNYGSFNYPTQEwdVVAHEVGHNFGATHDCDGsqyASSGCERN 155

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 215500424  187 PGASYCNASDGYIMAPSYHVNSThIFSVCSADQLEAFQ 224
Cdd:pfam13574 156 AATSVCSANGSFIMNPASKSNND-LFSPCSISLICDVL 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 130-223 5.01e-09

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: 53.68  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424 130 GILGYAYVGGACRSSKVGMVEDEANMFT--GTHTFVHEVGHLLGMSHDGDG--PPESVTDSPGASYCNASDGYIMAPSY- 204
Cdd:cd00203   66 GTGGWAYLGRVCDSLRGVGVLQDNQSGTkeGAQTIAHELGHALGFYHDHDRkdRDDYPTIDDTLNAEDDDYYSVMSYTKg 145

                         90       100
                 ....*....|....*....|..
gi 215500424 205 ---HVNSTHiFSVCSADQLEAF 223
Cdd:cd00203  146 sfsDGQRKD-FSQCDIDQINKL 166
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 54-175 6.54e-09

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: 52.37  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424   54 LDVQLVMTKITIFTKRTETFIKKPPaneSVIMTDSLEYLMNYTQNENEfkedDIVVLLTGLNiasynsttkkveSEGILG 133
Cdd:pfam13582  18 LGIRLQLAAIIITTSADTPYTSSDA---LEILDELQEVNDTRIGQYGY----DLGHLFTGRD------------GGGGGG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 215500424  134 YAYVGGAC-RSSKVGMVEDE-ANMFTGTHTFVHEVGHLLGMSHD 175
Cdd:pfam13582  79 IAYVGGVCnSGSKFGVNSGSgPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 103-218 2.24e-06

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 46.84  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  103 KEDDIVVLltglniasynsTTKKVESEGILGYAYVGGACRSSKVGMvedEANMFT----GTHTFVHEVGHLLGMSHD--G 176
Cdd:pfam13583  90 LNYDLAYL-----------TLMTGPSGQNVGVAWVGALCSSARQNA---KASGVArsrdEWDIFAHEIGHTFGAVHDcsS 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 215500424  177 DGPPESVtdspgaSYCNASDGYIMAPSyHVNSTHIFSVCSAD 218
Cdd:pfam13583 156 QGEGLSS------STEDGSGQTIMSYA-STASQTAFSPCTIR 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 128-220 1.92e-05

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 44.33  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424 128 SEGILGYAYVGGACRSskvGMVEDEANMFTGT----HT------FVHEVGHLLGMSHD------GDGPPESVTDSP-GAS 190
Cdd:cd04271  108 SGSEVGVAWLGQLCRT---GASDQGNETVAGTnvvvRTsnewqvFAHEIGHTFGAVHDctsgtcSDGSVGSQQCCPlSTS 184

                         90       100       110
                 ....*....|....*....|....*....|..
gi 215500424 191 YCNASDGYIMAPSyhvNSTHI--FSVCSADQL 220
Cdd:cd04271  185 TCDANGQYIMNPS---SSSGIteFSPCTIGNI 213
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 128-216 5.28e-05

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: 43.13  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424 128 SEGILGYAYV--------GGACRSSKVGMVEDEANMFTGTHTFV----------------HEVGHLLGMSHDGDGPPESV 183
Cdd:cd04270  113 DMGTLGLAYVgsprdnsaGGICEKAYYYSNGKKKYLNTGLTTTVnygkrvptkesdlvtaHELGHNFGSPHDPDIAECAP 192

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 215500424 184 TDSPGASycnasdgYIMAPS----YHVNSTHiFSVCS 216
Cdd:cd04270  193 GESQGGN-------YIMYARatsgDKENNKK-FSPCS 221
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 99-196 4.03e-04

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: 40.40  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215500424  99 ENEFKEDDIVVLLTGLNIASYNSTtkkveSEGILGYAYV------------GGACRSSKVGMveDEANMFTGTHTFVHEV 166
Cdd:cd04275   73 EDAMKSALRKGGYKYLNIYVANFL-----GGGLLGYATFpdslvslafitdGVVINPSSLPG--GSAAPYNLGDTATHEV 145

                         90       100       110
                 ....*....|....*....|....*....|
gi 215500424 167 GHLLGMSHdgdgppesvTDSPGASYCNASD 196
Cdd:cd04275  146 GHWLGLYH---------TFQGGSPCCTTGD 166
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 163-213 2.58e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 37.21  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 215500424  163 VHEVGHLLGMSHdgdgppesvTDSPGAsycnasdgyIMAPSYHVNSTHIFS 213
Cdd:pfam00413 113 AHEIGHALGLGH---------SSDPGA---------IMYPTYSPLDSKKFR 145
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 158-189 4.49e-03

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 37.01  E-value: 4.49e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 215500424 158 GTHTFVHEVGHLLGMSHDGDGPPESVTDSPGA 189
Cdd:cd04277  113 GYQTIIHEIGHALGLEHPGDYNGGDPVPPTYA 144
 
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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