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Conserved domains on  [gi|389634681|ref|XP_003714993|]
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metalloprotease 1 [Pyricularia oryzae 70-15]

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 ...
 65-276 4.40e-113

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: 325.06  E-value: 4.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  65 LTIDTYVHVVATSTSASAGYLSDATIQQQLRVMNEDYAP------SGIQFVLKGTDRTVNANWA---RDSGETAMKTALR 135
Cdd:cd04275    2 IVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681 136 KGTYKDLNLYFLSSIPGGILGYCYFPASATTSTVRLDGCTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGG--C 213
Cdd:cd04275   82 KGGYKYLNIYVANFLGGGLLGYATFPDSLVSLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGGspC 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681 214 NGQGDLVDDTPAQASASSGCPIGRDSCPNQPGLDPIHNYMDYSDDSCYEEFTPGQNARMSSMF 276
Cdd:cd04275  162 CTTGDYVADTPAEASPSYGCPAGRDTCPGQPGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYL 224
 
Name Accession Description Interval E-value
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 65-276 4.40e-113

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: 325.06  E-value: 4.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  65 LTIDTYVHVVATSTSASAGYLSDATIQQQLRVMNEDYAP------SGIQFVLKGTDRTVNANWA---RDSGETAMKTALR 135
Cdd:cd04275    2 IVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681 136 KGTYKDLNLYFLSSIPGGILGYCYFPASATTSTVRLDGCTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGG--C 213
Cdd:cd04275   82 KGGYKYLNIYVANFLGGGLLGYATFPDSLVSLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGGspC 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681 214 NGQGDLVDDTPAQASASSGCPIGRDSCPNQPGLDPIHNYMDYSDDSCYEEFTPGQNARMSSMF 276
Cdd:cd04275  162 CTTGDYVADTPAEASPSYGCPAGRDTCPGQPGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYL 224
Peptidase_M43 pfam05572
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ...
 139-272 1.81e-13

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: 66.48  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  139 YKDLNLYFLSSIPGGIL---GYCYFPASATTS--TVRLdgctIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGC 213
Cdd:pfam05572  15 EKYMNVYIQNDLADGLTnnsGVAWYPDSGMSAdgTARV----VFNGAYLAADPTSTNFSSTLTHEFGHFLGLIHTFEGGC 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681  214 -NGQGDLVDDTPAQASA-SSGCPIGRDSCPNqpglDPIH--NYMDYSDdsCYEEFTPGQNARM 272
Cdd:pfam05572  91 eRGEGDKVPDTPSYTGGeVSLRNKDLFNCNG----EPINsqNQMDYNG--CYAMFTQDQVDRM 147
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 172-210 3.27e-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: 36.94  E-value: 3.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 389634681   172 DGCTIASGTVPGGSIsRFNLG------KTAVHEVGHWFGLYHTFQ 210
Cdd:smart00235  60 SGCTLSHAGRPGGDQ-HLSLGngcintGVAAHELGHALGLYHEQS 103
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
138-213 4.80e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 4.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389634681 138 TYKDLnlyflsSIPGG--ILGYCYFPAS-ATTSTVRLDgcTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGC 213
Cdd:COG1913   75 TDVDL------YAPGLnfVFGLAYLGGRvAVVSTARLR--PEFYGLPPDEELFLERVLKEAVHELGHLFGLGHCPNPRC 145
 
Name Accession Description Interval E-value
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 65-276 4.40e-113

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: 325.06  E-value: 4.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  65 LTIDTYVHVVATSTSASAGYLSDATIQQQLRVMNEDYAP------SGIQFVLKGTDRTVNANWA---RDSGETAMKTALR 135
Cdd:cd04275    2 IVIPVYFHVIYNNSAVSGGNISDAQITDQIDVLNDDYSGlnagvdLGIEFVLAGTTRTVNSAWPvfaGSGTEDAMKSALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681 136 KGTYKDLNLYFLSSIPGGILGYCYFPASATTSTVRLDGCTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGG--C 213
Cdd:cd04275   82 KGGYKYLNIYVANFLGGGLLGYATFPDSLVSLAFITDGVVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYHTFQGGspC 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681 214 NGQGDLVDDTPAQASASSGCPIGRDSCPNQPGLDPIHNYMDYSDDSCYEEFTPGQNARMSSMF 276
Cdd:cd04275  162 CTTGDYVADTPAEASPSYGCPAGRDTCPGQPGLDPIHNYMDYSDDSCMNEFTPGQVTRMRSYL 224
Peptidase_M43 pfam05572
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ...
 139-272 1.81e-13

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: 66.48  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  139 YKDLNLYFLSSIPGGIL---GYCYFPASATTS--TVRLdgctIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGC 213
Cdd:pfam05572  15 EKYMNVYIQNDLADGLTnnsGVAWYPDSGMSAdgTARV----VFNGAYLAADPTSTNFSSTLTHEFGHFLGLIHTFEGGC 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681  214 -NGQGDLVDDTPAQASA-SSGCPIGRDSCPNqpglDPIH--NYMDYSDdsCYEEFTPGQNARM 272
Cdd:pfam05572  91 eRGEGDKVPDTPSYTGGeVSLRNKDLFNCNG----EPINsqNQMDYNG--CYAMFTQDQVDRM 147
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 73-274 2.45e-06

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: 46.75  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  73 VVATSTSASAGYLSDATIQQQLRVMNEDYA-PSGIQFVLkgtdrtvnanwardsgetamktalRKGTYKDLNLYFL---S 148
Cdd:cd00203    6 VVVADDRDVEEENLSAQIQSLILIAMQIWRdYLNIRFVL------------------------VGVEIDKADIAILvtrQ 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681 149 SIPGGILGYCYFPasattstvrlDGCTIASGTvpgGSISRFNLGK-----TAVHEVGHWFGLYHTFQGGC-NGQGDLVDD 222
Cdd:cd00203   62 DFDGGTGGWAYLG----------RVCDSLRGV---GVLQDNQSGTkegaqTIAHELGHALGFYHDHDRKDrDDYPTIDDT 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 389634681 223 TPAqasassgcpigrdsCPNQPGldpihNYMDYSDDScyeeFTPGQNARMSS 274
Cdd:cd00203  129 LNA--------------EDDDYY-----SVMSYTKGS----FSDGQRKDFSQ 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 151-208 8.37e-06

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: 44.92  E-value: 8.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389634681  151 PGGILGYCYFPASATTSTVRLDGC---TIASGtVPGGsisrFNLGKTAVHEVGHWFGLYHT 208
Cdd:pfam00413  70 PGGVLAHAFFPGPGLGGDIHFDDDetwTVGSD-PPHG----INLFLVAAHEIGHALGLGHS 125
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
71-242 1.05e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.10  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681   71 VHVVATStSASAGYLSDAT----IQQQLRVMNEDYAPSGIQFVLKG------TDRTVNANWARDSGETAMK-----TALR 135
Cdd:pfam13688   7 LLVAADC-SYVAAFGGDAAqaniINMVNTASNVYERDFNISLGLVNltisdsTCPYTPPACSTGDSSDRLSefqdfSAWR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  136 kGTYKDLNLYFLS--SIPGGILGYcyfPASATTSTVRLDGCTiaSGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGC 213
Cdd:pfam13688  86 -GTQNDDLAYLFLmtNCSGGGLAW---LGQLCNSGSAGSVST--RVSGNNVVVSTATEWQVFAHEIGHNFGAVHDCDSST 159

                         170       180
                  ....*....|....*....|....*....
gi 389634681  214 NGQgdlvddtpaqasassGCPIGRDSCPN 242
Cdd:pfam13688 160 SSQ---------------CCPPSNSTCPA 173
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 141-212 4.62e-05

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: 43.17  E-value: 4.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389634681 141 DLNLYFLSSIPGGILGYCYFPAsaTTSTVRLDGCTIASGTVPGGSISRFNLGK-TAVHEVGHWFGLYHTFQGG 212
Cdd:cd04277   64 DIRFGNSSDPDGNTAGYAYYPG--SGSGTAYGGDIWFNSSYDTNSDSPGSYGYqTIIHEIGHALGLEHPGDYN 134
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 152-209 8.46e-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: 38.98  E-value: 8.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389634681 152 GGILGYCYFPASATTSTVRLDGCTIASGTVPGGSisRFNLGKTAVHEVGHWFGLYHTF 209
Cdd:cd04279   67 GGGLARAGFPLISDGNRKLFNRTDINLGPGQPRG--AENLQAIALHELGHALGLWHHS 122
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 73-208 1.86e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 37.35  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681   73 VVATSTSASAGYLSDATIQQQLRvmnedyapsGIQFVLKGTDRTVNANWARDSGETAMKTALRKGTYK-DLNLYFLSSIP 151
Cdd:pfam13582   3 IVSLVNRANTIYERDLGIRLQLA---------AIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGyDLGHLFTGRDG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 389634681  152 GGILGYCYFPASATTStvrldgctIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHT 208
Cdd:pfam13582  74 GGGGGIAYVGGVCNSG--------SKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 71-207 2.27e-03

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: 38.17  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681  71 VHVVA----TSTSASAGYLSDATIQQQLRVMNEDY----APSGIQFVLKGTDRTVNANWARDSGEtamKTALRKGTYK-- 140
Cdd:cd04267    5 LVVVAdhrmVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDS---DASNTLNSFSfw 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389634681 141 --------DLNLYFLSS--IPGGILGYCYFPASATTStvrlDGCTIASGTVPGGSISRfnlgkTAVHEVGHWFGLYH 207
Cdd:cd04267   82 raegpirhDNAVLLTAQdfIEGDILGLAYVGSMCNPY----SSVGVVEDTGFTLLTAL-----TMAHELGHNLGAEH 149
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 172-210 3.27e-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: 36.94  E-value: 3.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 389634681   172 DGCTIASGTVPGGSIsRFNLG------KTAVHEVGHWFGLYHTFQ 210
Cdd:smart00235  60 SGCTLSHAGRPGGDQ-HLSLGngcintGVAAHELGHALGLYHEQS 103
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
138-213 4.80e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 4.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389634681 138 TYKDLnlyflsSIPGG--ILGYCYFPAS-ATTSTVRLDgcTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGC 213
Cdd:COG1913   75 TDVDL------YAPGLnfVFGLAYLGGRvAVVSTARLR--PEFYGLPPDEELFLERVLKEAVHELGHLFGLGHCPNPRC 145
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 194-274 6.79e-03

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: 36.71  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389634681 194 TAVHEVGHWFGLYHTFQGGCNGQGDLVDDTPAQASASsgcpigrdscpnqpgldpihnyMDYSDDSCYEEFTPGQNARMS 273
Cdd:cd04268   97 TAEHELGHALGLRHNFAASDRDDNVDLLAEKGDTSSV----------------------MDYAPSNFSIQLGDGQKYTIG 154


                 .
gi 389634681 274 S 274
Cdd:cd04268  155 P 155
 
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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