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Conserved domains on  [gi|1622964307|ref|XP_028681854|]
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phosphotriesterase-related protein isoform X5 [Macaca mulatta]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
22-295 1.94e-135

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member pfam02126:

Pssm-ID: 469705  Cd Length: 298  Bit Score: 385.38  E-value: 1.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  22 NQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEI 101
Cdd:pfam02126  34 SKEVAAIREELLYLKARGVGALVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 102 LHGADGTSIKCGVIGEIGCSWPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDr 181
Cdd:pfam02126 114 EHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 182 TILDKKELLEFAQLGCYLEYDLFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGY 261
Cdd:pfam02126 193 TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGY 262
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622964307 262 SH--ILTNVVPKMLLRGITENVLDKILIENPKQWLT 295
Cdd:pfam02126 263 SHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
22-295 1.94e-135

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 385.38  E-value: 1.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  22 NQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEI 101
Cdd:pfam02126  34 SKEVAAIREELLYLKARGVGALVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 102 LHGADGTSIKCGVIGEIGCSWPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDr 181
Cdd:pfam02126 114 EHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 182 TILDKKELLEFAQLGCYLEYDLFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGY 261
Cdd:pfam02126 193 TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGY 262
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622964307 262 SH--ILTNVVPKMLLRGITENVLDKILIENPKQWLT 295
Cdd:pfam02126 263 SHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
17-294 9.82e-130

Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active.


Pssm-ID: 238295  Cd Length: 293  Bit Score: 370.44  E-value: 9.82e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  17 ENLQLNQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDV 96
Cdd:cd00530    23 VDDFDLADVEAAKEELKRFRAHGGRTIVDATPPGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  97 LMNEILHGADGTSIKCGVIGEIGCSWPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVM 176
Cdd:cd00530   103 LIREIEEGIEGTGIKAGIIKEAGGSPAITPLEEKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 177 SHLDRTIlDKKELLEFAQLGCYLEYDLFGTELLHyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMK- 255
Cdd:cd00530   183 GHLDRND-DPDYLLKIAALGAYLEFDGIGKDKIF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKr 254
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622964307 256 YGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWL 294
Cdd:cd00530   255 YGGHGYDYILTRFIPRLRERGVTEEQLDTILVENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
15-296 8.57e-92

Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction only];


Pssm-ID: 441341  Cd Length: 305  Bit Score: 274.36  E-value: 8.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  15 HKENLQLNQEtEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLT 94
Cdd:COG1735    37 PADDDELDDV-EAAVEELERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  95 DVLMNEILHGADGTSIKCGVIgEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISK 173
Cdd:COG1735   116 ELLIREITEGIDGTGVRAGVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPER 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 174 TVMSHLDRTiLDKKELLEFAQLGCYLEYDLFGTELLHyqlcpdidmpDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRL 253
Cdd:COG1735   194 VVIGHMDRN-PDLDYHRELADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYL 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1622964307 254 MKYGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWLTF 296
Cdd:COG1735   263 KAYGGPGYDYILEVFLPRLRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
26-293 2.91e-36

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 131.49  E-value: 2.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  26 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 105
Cdd:PRK09875   34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 106 DGTSIKCGVIGEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 183
Cdd:PRK09875  114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 184 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH 263
Cdd:PRK09875  193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622964307 264 ILTNVVPKMLLRGITENVLDKILIENPKQW 293
Cdd:PRK09875  261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
22-295 1.94e-135

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 385.38  E-value: 1.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  22 NQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEI 101
Cdd:pfam02126  34 SKEVAAIREELLYLKARGVGALVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 102 LHGADGTSIKCGVIGEIGCSWPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDr 181
Cdd:pfam02126 114 EHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 182 TILDKKELLEFAQLGCYLEYDLFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGY 261
Cdd:pfam02126 193 TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGY 262
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622964307 262 SH--ILTNVVPKMLLRGITENVLDKILIENPKQWLT 295
Cdd:pfam02126 263 SHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
17-294 9.82e-130

Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active.


Pssm-ID: 238295  Cd Length: 293  Bit Score: 370.44  E-value: 9.82e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  17 ENLQLNQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDV 96
Cdd:cd00530    23 VDDFDLADVEAAKEELKRFRAHGGRTIVDATPPGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  97 LMNEILHGADGTSIKCGVIGEIGCSWPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVM 176
Cdd:cd00530   103 LIREIEEGIEGTGIKAGIIKEAGGSPAITPLEEKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 177 SHLDRTIlDKKELLEFAQLGCYLEYDLFGTELLHyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMK- 255
Cdd:cd00530   183 GHLDRND-DPDYLLKIAALGAYLEFDGIGKDKIF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKr 254
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622964307 256 YGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWL 294
Cdd:cd00530   255 YGGHGYDYILTRFIPRLRERGVTEEQLDTILVENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
15-296 8.57e-92

Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction only];


Pssm-ID: 441341  Cd Length: 305  Bit Score: 274.36  E-value: 8.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  15 HKENLQLNQEtEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLT 94
Cdd:COG1735    37 PADDDELDDV-EAAVEELERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  95 DVLMNEILHGADGTSIKCGVIgEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISK 173
Cdd:COG1735   116 ELLIREITEGIDGTGVRAGVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPER 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 174 TVMSHLDRTiLDKKELLEFAQLGCYLEYDLFGTELLHyqlcpdidmpDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRL 253
Cdd:COG1735   194 VVIGHMDRN-PDLDYHRELADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYL 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1622964307 254 MKYGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWLTF 296
Cdd:COG1735   263 KAYGGPGYDYILEVFLPRLRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
26-293 2.91e-36

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 131.49  E-value: 2.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  26 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 105
Cdd:PRK09875   34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 106 DGTSIKCGVIGEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 183
Cdd:PRK09875  114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 184 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH 263
Cdd:PRK09875  193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622964307 264 ILTNVVPKMLLRGITENVLDKILIENPKQW 293
Cdd:PRK09875  261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
15-294 1.18e-06

TatD related DNase; This family of proteins are related to a large superfamily of metalloenzymes. TatD, a member of this family has been shown experimentally to be a DNase enzyme.


Pssm-ID: 425997 [Multi-domain]  Cd Length: 253  Bit Score: 48.80  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  15 HKENLQLNQETEAIKEEllyFKANGGGALVENTTTgiSRDTQTLKRLAEETGVHIISGAGFyvdatHSSEtramsVEQLT 94
Cdd:pfam01026   6 HLDFKDFDEDRDEVIER---AREAGVTGVVVVGTD--LEDFLRVLELAEKYPDRVYAAVGV-----HPHE-----ADEAS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307  95 DVLMNEILHGADGTSIKCgvIGEIGC-SWPLTESEK----KVLQATAHAQAQLGCPVIIHpGRSSRApfQIIRILQEAGA 169
Cdd:pfam01026  71 EDDLEALEKLAEHPKVVA--IGEIGLdYYYVDESPKeaqeEVFRRQLELAKELGLPVVIH-TRDAEE--DLLEILKEAGA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964307 170 DISKTVMSHLDrtiLDKKELLEFAQLGCYleydlFGtellhyqlCPDIDMPDDNKRIRRVRLLVEegyEDRILV---AHD 246
Cdd:pfam01026 146 PGARGVLHCFT---GSVEEARKFLDLGFY-----IS--------ISGIVTFKNAKKLREVAAAIP---LDRLLVetdAPY 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622964307 247 IHTKTRLMKYGGHGYshiLTNVVPKML-LRGITENVLDKILIENPKQWL 294
Cdd:pfam01026 207 LAPVPYRGKRNEPAY---VPYVVEKLAeLKGISPEEVAEITTENAERLF 252
 
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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