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Conserved domains on  [gi|47933341|ref|NP_001001484|]
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phosphotriesterase-related protein isoform 1 [Homo sapiens]

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 ...
15-347 4.30e-140

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: 399.24  E-value: 4.30e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAISKEpivmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   175 PLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   255 LFGTELlhyqlgpdidMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 47933341   333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 4.30e-140

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 399.24  E-value: 4.30e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAISKEpivmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   175 PLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   255 LFGTELlhyqlgpdidMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 47933341   333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 5.57e-131

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: 375.83  E-value: 5.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  21 GRTLTHEHLAMTFDCCycppppcqeaiskepivmknlywiqKNAYSHkENLQLNQETEAIKEELLYFKANGGGALVENTT 100
Cdd:cd00530   1 GVTLTHEHLIIDSSGF-------------------------VRDPPE-VDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 101 TGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSWPLTESE 180
Cdd:cd00530  55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 181 RKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTIlDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530 135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 261 LHyqlgpdiDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMK-YGGHGYSHILTNVVPKMLLRGITENVLDKILI 339
Cdd:cd00530 214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                ....*..
gi 47933341 340 ENPKQWL 346
Cdd:cd00530 287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 7.30e-100

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 297.08  E-value: 7.30e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   5 SGKVQTVLGLVEPSKLGRTLTHEHLamTFDCCycppppcqeaiskepivmknlyWIQKNAYshKENLQLNQEtEAIKEEL 84
Cdd:COG1735   1 MGFVRTVLGPIPPEELGVTLMHEHL--FVDLP----------------------GVRQDPP--ADDDELDDV-EAAVEEL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  85 LYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKC 164
Cdd:COG1735  54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 165 GIIgEIGCS-WPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISKTVMSHLDRTiLDKKELLE 243
Cdd:COG1735 134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 244 FAQLGCYLEYDLFGTELLHyqlgpdidmpDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735 211 LADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                       330       340
                ....*....|....*....|....*
gi 47933341 324 MLLRGITENVLDKILIENPKQWLTF 348
Cdd:COG1735 281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
78-345 2.89e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 130.33  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   78 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 157
Cdd:PRK09875  34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  158 DGTSIKCGIIGEIGCS-WPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 235
Cdd:PRK09875 114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  236 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlgpdiDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSH 315
Cdd:PRK09875 193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                        250       260       270
                 ....*....|....*....|....*....|
gi 47933341  316 ILTNVVPKMLLRGITENVLDKILIENPKQW 345
Cdd:PRK09875 261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 4.30e-140

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 399.24  E-value: 4.30e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAISKEpivmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   175 PLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   255 LFGTELlhyqlgpdidMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 47933341   333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 5.57e-131

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: 375.83  E-value: 5.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  21 GRTLTHEHLAMTFDCCycppppcqeaiskepivmknlywiqKNAYSHkENLQLNQETEAIKEELLYFKANGGGALVENTT 100
Cdd:cd00530   1 GVTLTHEHLIIDSSGF-------------------------VRDPPE-VDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 101 TGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSWPLTESE 180
Cdd:cd00530  55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 181 RKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTIlDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530 135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 261 LHyqlgpdiDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMK-YGGHGYSHILTNVVPKMLLRGITENVLDKILI 339
Cdd:cd00530 214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                ....*..
gi 47933341 340 ENPKQWL 346
Cdd:cd00530 287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 7.30e-100

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 297.08  E-value: 7.30e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   5 SGKVQTVLGLVEPSKLGRTLTHEHLamTFDCCycppppcqeaiskepivmknlyWIQKNAYshKENLQLNQEtEAIKEEL 84
Cdd:COG1735   1 MGFVRTVLGPIPPEELGVTLMHEHL--FVDLP----------------------GVRQDPP--ADDDELDDV-EAAVEEL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  85 LYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKC 164
Cdd:COG1735  54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 165 GIIgEIGCS-WPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISKTVMSHLDRTiLDKKELLE 243
Cdd:COG1735 134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341 244 FAQLGCYLEYDLFGTELLHyqlgpdidmpDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735 211 LADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                       330       340
                ....*....|....*....|....*
gi 47933341 324 MLLRGITENVLDKILIENPKQWLTF 348
Cdd:COG1735 281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
78-345 2.89e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 130.33  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   78 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 157
Cdd:PRK09875  34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  158 DGTSIKCGIIGEIGCS-WPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 235
Cdd:PRK09875 114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341  236 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlgpdiDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSH 315
Cdd:PRK09875 193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                        250       260       270
                 ....*....|....*....|....*....|
gi 47933341  316 ILTNVVPKMLLRGITENVLDKILIENPKQW 345
Cdd:PRK09875 261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
67-346 5.17e-07

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: 50.34  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341    67 HKENLQLNQETEAIKEEllyFKANGGGALVENTTTgiSRDTQTLKRLAEETGVHIISGAGFyvdatHSSEtramsVEQLT 146
Cdd:pfam01026   6 HLDFKDFDEDRDEVIER---AREAGVTGVVVVGTD--LEDFLRVLELAEKYPDRVYAAVGV-----HPHE-----ADEAS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   147 DVLMNEILHGADGTSIKCgiIGEIGC-SWPLTESER----KVLQATAHAQAQLGCPVIIHpGRSSRApfQIIRILQEAGA 221
Cdd:pfam01026  71 EDDLEALEKLAEHPKVVA--IGEIGLdYYYVDESPKeaqeEVFRRQLELAKELGLPVVIH-TRDAEE--DLLEILKEAGA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47933341   222 DISKTVMSHLDrtiLDKKELLEFAQLGCYleydlFGtellhyqLGPDIdMPDDNKRIRRVRLLVEegcEDRILV---AHD 298
Cdd:pfam01026 146 PGARGVLHCFT---GSVEEARKFLDLGFY-----IS-------ISGIV-TFKNAKKLREVAAAIP---LDRLLVetdAPY 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 47933341   299 IHTKTRLMKYGGHGYshiLTNVVPKML-LRGITENVLDKILIENPKQWL 346
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.
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