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Conserved domains on  [gi|56553642|pdb|1R55|A]
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Chain A, ADAM 33

Protein Classification

ZnMc_adamalysin_II_like domain-containing protein( domain architecture ID 10136384)

ZnMc_adamalysin_II_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 7-204 1.04e-89

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: 261.78  E-value: 1.04e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRG- 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       86 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGC-CveaaaE 164
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1R55_A      165 SGGCVMAAATGHPfPRVFSACSRRQLRAFFRKGGGACLSN 204
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 7-204 1.04e-89

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: 261.78  E-value: 1.04e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRG- 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       86 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGC-CveaaaE 164
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1R55_A      165 SGGCVMAAATGHPfPRVFSACSRRQLRAFFRKGGGACLSN 204
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 7-206 7.46e-89

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: 259.93  E-value: 7.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A          7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWR-RG 85
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         86 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPD--GCCVEaaa 163
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
1R55_A        164 ESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAP 206
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 136-155 2.83e-03

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: 36.56  E-value: 2.83e-03
                           10        20
                   ....*....|....*....|
1R55_A         136 AAATMAHEIGHSLGLSHDPD 155
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQS 103
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
140-171 5.17e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.47  E-value: 5.17e-03
                        10        20        30
                ....*....|....*....|....*....|..
1R55_A      140 MAHEIGHSLGLSHdpdgcCVEAaaesgGCVMA 171
Cdd:COG1913 127 AVHELGHLFGLGH-----CPNP-----RCVMH 148
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 7-204 1.04e-89

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: 261.78  E-value: 1.04e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRG- 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       86 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGC-CveaaaE 164
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1R55_A      165 SGGCVMAAATGHPfPRVFSACSRRQLRAFFRKGGGACLSN 204
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 7-206 7.46e-89

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: 259.93  E-value: 7.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A          7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWR-RG 85
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         86 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPD--GCCVEaaa 163
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
1R55_A        164 ESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAP 206
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 7-195 5.14e-38

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: 130.23  E-value: 5.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHTLFLTRHRNLQHTKQRLLEVANYVDQLLRTLD----IQVALTGLEVW-TERDRSRVTQDANATLWAFLQ 81
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       82 WRRGLWAQrpHDSAQLLTGRAF-QGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAaTMAHEIGHSLGLSHDPDGCCVE 160
Cdd:cd04267  81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTAL-TMAHELGHNLGAEHDGGDELAF 157

                       170       180       190
                ....*....|....*....|....*....|....*
1R55_A      161 AAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFR 195
Cdd:cd04267 158 ECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 7-202 9.66e-37

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 127.35  E-value: 9.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHTLFLTRHRnlQHTKQRLLEVANYVDQLLR--TL--DIQVALTGLEVWTERDR-SRVTQDANATLWAFLQ 81
Cdd:cd04273   1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       82 WRRGLWAQRP-----HDSAQLLTGRAFQGA-----TVGLAPVEGMCRAESSGGVSTDHselPIGAAATMAHEIGHSLGLS 151
Cdd:cd04273  79 WQKKLNPPNDsdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLGMP 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
1R55_A      152 HDPDG--CcveAAAESGGCVMA---AATGHPFPrvFSACSRRQLRAFFRKGGGACL 202
Cdd:cd04273 156 HDGDGnsC---GPEGKDGHIMSptlGANTGPFT--WSKCSRRYLTSFLDTGDGNCL 206
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 7-193 7.83e-17

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: 74.48  E-value: 7.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        7 KYLELYIVADHtlfltRHRNLQHTKQRLLEVANYVDQLLRT-LDIQVALTGLEVwterdrsrvtqdanatlwaflqwrrg 85
Cdd:cd00203   1 KVIPYVVVADD-----RDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       86 lwaqRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAES 165
Cdd:cd00203  50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1R55_A      166 ----------GGCVMAAATG---HPFPRVFSACSRRQLRAF 193
Cdd:cd00203 126 ddtlnaedddYYSVMSYTKGsfsDGQRKDFSQCDIDQINKL 166
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
11-176 3.19e-16

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 73.61  E-value: 3.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         11 LYIVADHTLFLTRHRNLqhTKQRLLEVANYVDQLL-RTLDIQVALTGLEVWTERDRS----RVTQDANATLWAFlQWRRG 85
Cdd:pfam13688   7 LLVAADCSYVAAFGGDA--AQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         86 LWAQRPHDSAQLLTGRAFQgaTVGLAPVEGMCRAESSGGVSTDHSELPIGAAA-----TMAHEIGHSLGLSHDPD----- 155
Cdd:pfam13688  84 WRGTQNDDLAYLFLMTNCS--GGGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDsstss 161

                         170       180
                  ....*....|....*....|....
1R55_A        156 GCC---VEAAAESGGCVMAAATGH 176
Cdd:pfam13688 162 QCCppsNSTCPAGGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 39-153 1.84e-14

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 67.01  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         39 NYVDQLLRT-LDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGaTVGLAPVEGMC 117
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGG-GGGIAYVGGVC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
1R55_A        118 RAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHD 153
Cdd:pfam13582  87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 11-201 4.16e-13

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: 65.86  E-value: 4.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       11 LYIVADHTLF-LTRHRNLQHTKQRLLEVANYVDQLLRTLDIQV-ALTGLEVWTER-----DRSRVTQDANATLWAFLQWR 83
Cdd:cd04270   5 LLLVADHRFYkYMGRGEEETTINYLISHIDRVDDIYRNTDWDGgGFKGIGFQIKRirihtTPDEVDPGNKFYNKSFPNWG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       84 RGLW----AQRPHDS----AQLLTGRAFQGATVGLAPVeGMCRAESSGGVSTDHSELPIGAAA----------------- 138
Cdd:cd04270  85 VEKFlvklLLEQFSDdvclAHLFTYRDFDMGTLGLAYV-GSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkrvp 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1R55_A      139 ------TMAHEIGHSLGLSHDPDGC-CVEAAAESGGCVM--AAATG-HPFPRVFSACSRRQLRAFFRKGGGAC 201
Cdd:cd04270 164 tkesdlVTAHELGHNFGSPHDPDIAeCAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 8-202 3.21e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 63.14  E-value: 3.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A        8 YLELYIVADHTLfltrHRNLQHTKQRLLEVANYVDQL-LRTLD-----IQVALTGLEVWTERDRSRV-------TQDANA 74
Cdd:cd04272   2 YPELFVVVDYDH----QSEFFSNEQLIRYLAVMVNAAnLRYRDlksprIRLLLVGITISKDPDFEPYihpinygYIDAAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       75 TLWAFLQWRRGLWAQRPHDSAQLLTGR--------AFQGATVGLAPVEGMCrAESSGGVSTDHSELPIGAAaTMAHEIGH 146
Cdd:cd04272  78 TLENFNEYVKKKRDYFNPDVVFLVTGLdmstysggSLQTGTGGYAYVGGAC-TENRVAMGEDTPGSYYGVY-TMTHELAH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1R55_A      147 SLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRV--------FSACSRRQLRAFFRKGGGACL 202
Cdd:cd04272 156 LLGAPHDGSPPPSWVKGHPGSLDCPWDDGYIMSYVvngerqyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 28-192 6.22e-10

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: 56.48  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         28 QHTKQRLLEVANYVDQLLRTLDIQVALtGL-------------EVWTERDRSRVTQDANATLwaFLQWRrglwAQRPHDS 94
Cdd:pfam13574   1 GNVTENLVNVVNRVNQIYEPDDINING-GLvnpgeipattsasDSGNNYCNSPTTIVRRLNF--LSQWR----GEQDYCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         95 AQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATM---------AHEIGHSLGLSHDPDG------CCV 159
Cdd:pfam13574  74 AHLVTMGTFSGGELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNyptqewdvvAHEVGHNFGATHDCDGsqyassGCE 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
1R55_A        160 EAAA-----ESGGCVMAAATGHpFPRVFSACSRRQLRA 192
Cdd:pfam13574 154 RNAAtsvcsANGSFIMNPASKS-NNDLFSPCSISLICD 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 13-203 3.16e-09

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: 54.73  E-value: 3.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       13 IVADHTlFLTRHRNLQHTKQRLLEVANYVDQLLR-TLDIQVALTGLEVWTERDRSRVTQDA------------NATLWAF 79
Cdd:cd04271   7 VAADCS-YTKSFGSVEEARRNILNNVNSASQLYEsSFNISLGLRNLTISDASCPSTAVDSApwnlpcnsridiDDRLSIF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A       80 LQWRrglwAQRPHDSA---QLLTGRAfQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAAT-----MAHEIGHSLGLS 151
Cdd:cd04271  86 SQWR----GQQPDDGNafwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAV 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1R55_A      152 HDPD-GCCVEAAAESGGC--------------VMAAATGHPFPRvFSACSRRQLRAFFRKGG--GACLS 203
Cdd:cd04271 161 HDCTsGTCSDGSVGSQQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGRNPvrTSCLS 228
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 117-158 1.71e-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: 41.17  E-value: 1.71e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
1R55_A      117 CRAESSGGVSTDhselPIGAAATMAHEIGHSLGLSH---DPDGCC 158
Cdd:cd04275 122 INPSSLPGGSAA----PYNLGDTATHEVGHWLGLYHtfqGGSPCC 162
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 138-155 1.00e-03

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 38.34  E-value: 1.00e-03
                        10
                ....*....|....*...
1R55_A      138 ATMAHEIGHSLGLSHDPD 155
Cdd:cd04278 109 SVAAHEIGHALGLGHSSD 126
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 138-152 1.22e-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: 38.55  E-value: 1.22e-03
                        10
                ....*....|....*
1R55_A      138 ATMAHEIGHSLGLSH 152
Cdd:cd04277 115 QTIIHEIGHALGLEH 129
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 139-170 1.66e-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: 37.66  E-value: 1.66e-03
                        10        20        30
                ....*....|....*....|....*....|..
1R55_A      139 TMAHEIGHSLGLSHdpdgcCVEAAaesggCVM 170
Cdd:cd11375 126 EAVHELGHLFGLDH-----CPYYA-----CVM 147
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 141-155 1.88e-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: 37.60  E-value: 1.88e-03
                          10
                  ....*....|....*
1R55_A        141 AHEIGHSLGLSHDPD 155
Cdd:pfam00413 113 AHEIGHALGLGHSSD 127
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 136-155 2.83e-03

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: 36.56  E-value: 2.83e-03
                           10        20
                   ....*....|....*....|
1R55_A         136 AAATMAHEIGHSLGLSHDPD 155
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQS 103
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 93-173 3.69e-03

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: 37.21  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R55_A         93 DSAQLLTGRAFQGATVGLAPVEGMCRAES----SGGVSTDHSELPIgaaatMAHEIGHSLGLSHD-PDGCC---VEAAAE 164
Cdd:pfam13583  93 DLAYLTLMTGPSGQNVGVAWVGALCSSARqnakASGVARSRDEWDI-----FAHEIGHTFGAVHDcSSQGEglsSSTEDG 167


                  ....*....
1R55_A        165 SGGCVMAAA 173
Cdd:pfam13583 168 SGQTIMSYA 176
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
140-171 5.17e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.47  E-value: 5.17e-03
                        10        20        30
                ....*....|....*....|....*....|..
1R55_A      140 MAHEIGHSLGLSHdpdgcCVEAaaesgGCVMA 171
Cdd:COG1913 127 AVHELGHLFGLGH-----CPNP-----RCVMH 148
 
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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