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Conserved domains on  [gi|303321089|ref|XP_003070539|]
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metalloprotease 1 precursor [Coccidioides posadasii C735 delta SOWgp]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 57-270 2.07e-111

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: 320.44  E-value: 2.07e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  57 PIEVETYFHVVASSRSERDGYISDQMLSDQIRVMNEDYAP------HGVHFNLRETTRTINPSWA---SDGNEIAMKRSL 127
Cdd:cd04275    1 SIVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089 128 RKGGYAALNVYFLKDL-GGALGYCYFPTNAApgSTTFIRDGCSVLSSSVPGGSGAPYDLGKTATHEVGHWMGLFHTFQGG 206
Cdd:cd04275   81 RKGGYKYLNIYVANFLgGGLLGYATFPDSLV--SLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303321089 207 --CSGQGDYVSDTPPQRSPSSGCPVGRDSCPGG-GVDPIHNYMDYSVDSCMNQFTRGQGTRMSSMWR 270
Cdd:cd04275  159 spCCTTGDYVADTPAEASPSYGCPAGRDTCPGQpGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYLD 225
 
Name Accession Description Interval E-value
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 57-270 2.07e-111

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: 320.44  E-value: 2.07e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  57 PIEVETYFHVVASSRSERDGYISDQMLSDQIRVMNEDYAP------HGVHFNLRETTRTINPSWA---SDGNEIAMKRSL 127
Cdd:cd04275    1 SIVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089 128 RKGGYAALNVYFLKDL-GGALGYCYFPTNAApgSTTFIRDGCSVLSSSVPGGSGAPYDLGKTATHEVGHWMGLFHTFQGG 206
Cdd:cd04275   81 RKGGYKYLNIYVANFLgGGLLGYATFPDSLV--SLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303321089 207 --CSGQGDYVSDTPPQRSPSSGCPVGRDSCPGG-GVDPIHNYMDYSVDSCMNQFTRGQGTRMSSMWR 270
Cdd:cd04275  159 spCCTTGDYVADTPAEASPSYGCPAGRDTCPGQpGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYLD 225
Peptidase_M43 pfam05572
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ...
 188-265 2.34e-14

Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system.


Pssm-ID: 368506  Cd Length: 152  Bit Score: 68.79  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  188 TATHEVGHWMGLFHTFQGGCS-GQGDYVSDTPPQRS-PSSGCPVGRDSCPGggvDPIH--NYMDYSvdSCMNQFTRGQGT 263
Cdd:pfam05572  71 TLTHEFGHFLGLIHTFEGGCErGEGDKVPDTPSYTGgEVSLRNKDLFNCNG---EPINsqNQMDYN--GCYAMFTQDQVD 145


                  ..
gi 303321089  264 RM 265
Cdd:pfam05572 146 RM 147
 
Name Accession Description Interval E-value
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 57-270 2.07e-111

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: 320.44  E-value: 2.07e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  57 PIEVETYFHVVASSRSERDGYISDQMLSDQIRVMNEDYAP------HGVHFNLRETTRTINPSWA---SDGNEIAMKRSL 127
Cdd:cd04275    1 SIVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089 128 RKGGYAALNVYFLKDL-GGALGYCYFPTNAApgSTTFIRDGCSVLSSSVPGGSGAPYDLGKTATHEVGHWMGLFHTFQGG 206
Cdd:cd04275   81 RKGGYKYLNIYVANFLgGGLLGYATFPDSLV--SLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303321089 207 --CSGQGDYVSDTPPQRSPSSGCPVGRDSCPGG-GVDPIHNYMDYSVDSCMNQFTRGQGTRMSSMWR 270
Cdd:cd04275  159 spCCTTGDYVADTPAEASPSYGCPAGRDTCPGQpGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYLD 225
Peptidase_M43 pfam05572
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ...
 188-265 2.34e-14

Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system.


Pssm-ID: 368506  Cd Length: 152  Bit Score: 68.79  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  188 TATHEVGHWMGLFHTFQGGCS-GQGDYVSDTPPQRS-PSSGCPVGRDSCPGggvDPIH--NYMDYSvdSCMNQFTRGQGT 263
Cdd:pfam05572  71 TLTHEFGHFLGLIHTFEGGCErGEGDKVPDTPSYTGgEVSLRNKDLFNCNG---EPINsqNQMDYN--GCYAMFTQDQVD 145


                  ..
gi 303321089  264 RM 265
Cdd:pfam05572 146 RM 147
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 65-201 1.03e-07

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: 50.88  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  65 HVVASSR----SERDGYISDQMLSDQIRVMNEDY----APHGVHFNLRETTRT--------INPSWASDGNEIAMKRS-- 126
Cdd:cd04267    6 VVVADHRmvsyFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILkgeqfappIDSDASNTLNSFSFWRAeg 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303321089 127 LRKGGYAALNVYFLKDLGGALGYCYFPTNaapgsttfirdGCSVLSSSVPGGSGAPYDLGKTATHEVGHWMGLFH 201
Cdd:cd04267   86 PIRHDNAVLLTAQDFIEGDILGLAYVGSM-----------CNPYSSVGVVEDTGFTLLTALTMAHELGHNLGAEH 149
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
88-257 1.86e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 47.41  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089   88 RVMNEDYAPHGVHFNLRETTR-----TINPSWASDGN------EIAMKRSLRKGGYAALNVYFL--KDLGGALGYCYFPT 154
Cdd:pfam13688  34 TASNVYERDFNISLGLVNLTIsdstcPYTPPACSTGDssdrlsEFQDFSAWRGTQNDDLAYLFLmtNCSGGGLAWLGQLC 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  155 NAAPGSttfirdGCSVLSSSVPGGSGAPYDLgKTATHEVGHWMGLFHTFQGGCSGQgdyvsdtppqrspssGCPVGRDSC 234
Cdd:pfam13688 114 NSGSAG------SVSTRVSGNNVVVSTATEW-QVFAHEIGHNFGAVHDCDSSTSSQ---------------CCPPSNSTC 171

                         170       180
                  ....*....|....*....|....
gi 303321089  235 PGGGvdpihNY-MDYSVDSCMNQF 257
Cdd:pfam13688 172 PAGG-----RYiMNPSSSPNSTDF 190
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 64-267 1.16e-04

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: 41.74  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089  64 FHVVASSRSERDGYISDQMLSdQIRVMNEDYA-PHGVHFNLRETTRtinpswASDGNEIAMKRSLRKGGyaalnvyflkd 142
Cdd:cd00203    5 YVVVADDRDVEEENLSAQIQS-LILIAMQIWRdYLNIRFVLVGVEI------DKADIAILVTRQDFDGG----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089 143 lggALGYCYFPTNAAPGSttfirdGCSVLSSSVPGgsgaPYDLGKTATHEVGHWMGLFHTFQGGC-SGQGDYVSDTPPqr 221
Cdd:cd00203   67 ---TGGWAYLGRVCDSLR------GVGVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDrDDYPTIDDTLNA-- 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 303321089 222 spssgcpvgrdsCPGGGvdpiHNYMDYSVDScmnqFTRGQGTRMSS 267
Cdd:cd00203  132 ------------EDDDY----YSVMSYTKGS----FSDGQRKDFSQ 157
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-206 1.20e-04

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: 42.02  E-value: 1.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303321089 132 YAALNVYFLKD-LGGALGYCYFPTNaapgSTTFIRDGCSVLSSSVPGGSGAPYDLGK-TATHEVGHWMGLFHTFQGG 206
Cdd:cd04277   62 GADIRFGNSSDpDGNTAGYAYYPGS----GSGTAYGGDIWFNSSYDTNSDSPGSYGYqTIIHEIGHALGLEHPGDYN 134
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 133-203 2.35e-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: 40.52  E-value: 2.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303321089 133 AALNVYFLKDLGGALGYCYFPTNAAPGSTTFIRDGCSVLS-SSVPGGSGAPYDLGKTATHEVGHWMGLFHTF 203
Cdd:cd04279   51 ADIVIFFDRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDiNLGPGQPRGAENLQAIALHELGHALGLWHHS 122
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 97-202 7.54e-04

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: 38.51  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303321089   97 HGVHFNL---RETTRTINPSWASDGNEIAMK----RSLRKGGYAA-LNVYFLK-DLGGALGYCYFPTNAAPGSttfirdg 167
Cdd:pfam13582  18 LGIRLQLaaiIITTSADTPYTSSDALEILDElqevNDTRIGQYGYdLGHLFTGrDGGGGGGIAYVGGVCNSGS------- 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 303321089  168 csvlSSSVPGGSGAPYDLG-KTATHEVGHWMGLFHT 202
Cdd:pfam13582  91 ----KFGVNSGSGPVGDTGaDTFAHEIGHNFGLNHT 122
 
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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