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Conserved domains on  [gi|61889077|ref|NP_071560|]
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phosphotriesterase-related protein [Rattus norvegicus]

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

 Zoom to residue level

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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 1.55e-161

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: 453.56  E-value: 1.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    15 VEPSQLGRTLTHEHLTMAFDSFYCPPPPCQEAASREpimmknlfwiqknpyshqenlqlnqeVEAVREELLYFKAKGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    95 VVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   175 PLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPFQIIRVLQEAGADISKTVMSHLDrSIFDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   255 LFGTELlnyqlspdidMPDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNVVPKMLLRGLTER 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 61889077   333 VLDKILRENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 1.55e-161

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 453.56  E-value: 1.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    15 VEPSQLGRTLTHEHLTMAFDSFYCPPPPCQEAASREpimmknlfwiqknpyshqenlqlnqeVEAVREELLYFKAKGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    95 VVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   175 PLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPFQIIRVLQEAGADISKTVMSHLDrSIFDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   255 LFGTELlnyqlspdidMPDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNVVPKMLLRGLTER 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 61889077   333 VLDKILRENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 5.76e-142

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: 403.57  E-value: 5.76e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  21 GRTLTHEHLTMAFDSFYCPPPPcqeaasrepimmknlfwiqknpyshqENLQLNQEVEAVREELLYFKAKGGGAVVENTT 100
Cdd:cd00530   1 GVTLTHEHLIIDSSGFVRDPPE--------------------------VDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 101 TGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKCGVIGEIGCSWPLTDSE 180
Cdd:cd00530  55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 181 RKVLQATAHAQAQLGCPVIIHPGRNPGAPFQIIRVLQEAGADISKTVMSHLDRSIfDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530 135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 261 LNyqlspdiDMPDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMK-YGGHGYSHILTNVVPKMLLRGLTERVLDKILR 339
Cdd:cd00530 214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                ....*..
gi 61889077 340 ENPKQWL 346
Cdd:cd00530 287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 7.71e-104

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 307.10  E-value: 7.71e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   5 SGKVQTVLGPVEPSQLGRTLTHEHLtmafdsFYCPPPPcqeaasrepimmknlfwiQKNPYSHqeNLQLNqEVEAVREEL 84
Cdd:COG1735   1 MGFVRTVLGPIPPEELGVTLMHEHL------FVDLPGV------------------RQDPPAD--DDELD-DVEAAVEEL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  85 LYFKAKGGGAVVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKC 164
Cdd:COG1735  54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 165 GVIgEIGCS-WPLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPfQIIRVLQEAGADISKTVMSHLDRSiFDKKELLE 243
Cdd:COG1735 134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 244 FAQLGCYLEYDLFGteLLNYQlspdidmpDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735 211 LADRGAYLEFDGIG--RDKYY--------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                       330       340
                ....*....|....*....|....*
gi 61889077 324 MLLRGLTERVLDKILRENPKQWLTF 348
Cdd:COG1735 281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
82-345 2.47e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 130.33  E-value: 2.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   82 EELLYFKAKGGGAVVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTS 161
Cdd:PRK09875  38 QEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  162 IKCGVIGEIGCS-WPLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPFQiIRVLQEAGADISKTVMSHLD-RSIFDKk 239
Cdd:PRK09875 118 LKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDNLDN- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  240 eLLEFAQLGCYLEYDLFGTEllNYqlspdidMPDDnKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTN 319
Cdd:PRK09875 196 -ILKMIDLGAYVQFDTIGKN--SY-------YPDE-KRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTT 264
                        250       260
                 ....*....|....*....|....*.
gi 61889077  320 VVPKMLLRGLTERVLDKILRENPKQW 345
Cdd:PRK09875 265 FIPQLRQSGFSQADVDVMLRENPSQF 290
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 1.55e-161

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 453.56  E-value: 1.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    15 VEPSQLGRTLTHEHLTMAFDSFYCPPPPCQEAASREpimmknlfwiqknpyshqenlqlnqeVEAVREELLYFKAKGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    95 VVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   175 PLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPFQIIRVLQEAGADISKTVMSHLDrSIFDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   255 LFGTELlnyqlspdidMPDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNVVPKMLLRGLTER 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 61889077   333 VLDKILRENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 5.76e-142

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: 403.57  E-value: 5.76e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  21 GRTLTHEHLTMAFDSFYCPPPPcqeaasrepimmknlfwiqknpyshqENLQLNQEVEAVREELLYFKAKGGGAVVENTT 100
Cdd:cd00530   1 GVTLTHEHLIIDSSGFVRDPPE--------------------------VDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 101 TGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKCGVIGEIGCSWPLTDSE 180
Cdd:cd00530  55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 181 RKVLQATAHAQAQLGCPVIIHPGRNPGAPFQIIRVLQEAGADISKTVMSHLDRSIfDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530 135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 261 LNyqlspdiDMPDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMK-YGGHGYSHILTNVVPKMLLRGLTERVLDKILR 339
Cdd:cd00530 214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                ....*..
gi 61889077 340 ENPKQWL 346
Cdd:cd00530 287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 7.71e-104

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 307.10  E-value: 7.71e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   5 SGKVQTVLGPVEPSQLGRTLTHEHLtmafdsFYCPPPPcqeaasrepimmknlfwiQKNPYSHqeNLQLNqEVEAVREEL 84
Cdd:COG1735   1 MGFVRTVLGPIPPEELGVTLMHEHL------FVDLPGV------------------RQDPPAD--DDELD-DVEAAVEEL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  85 LYFKAKGGGAVVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTSIKC 164
Cdd:COG1735  54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 165 GVIgEIGCS-WPLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPfQIIRVLQEAGADISKTVMSHLDRSiFDKKELLE 243
Cdd:COG1735 134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077 244 FAQLGCYLEYDLFGteLLNYQlspdidmpDDNKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735 211 LADRGAYLEFDGIG--RDKYY--------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                       330       340
                ....*....|....*....|....*
gi 61889077 324 MLLRGLTERVLDKILRENPKQWLTF 348
Cdd:COG1735 281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
82-345 2.47e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 130.33  E-value: 2.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   82 EELLYFKAKGGGAVVENTTTGLSRDVRTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLISEILHGADGTS 161
Cdd:PRK09875  38 QEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  162 IKCGVIGEIGCS-WPLTDSERKVLQATAHAQAQLGCPVIIHPGRNPGAPFQiIRVLQEAGADISKTVMSHLD-RSIFDKk 239
Cdd:PRK09875 118 LKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDNLDN- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077  240 eLLEFAQLGCYLEYDLFGTEllNYqlspdidMPDDnKRIRRVRFLVNEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTN 319
Cdd:PRK09875 196 -ILKMIDLGAYVQFDTIGKN--SY-------YPDE-KRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTT 264
                        250       260
                 ....*....|....*....|....*.
gi 61889077  320 VVPKMLLRGLTERVLDKILRENPKQW 345
Cdd:PRK09875 265 FIPQLRQSGFSQADVDVMLRENPSQF 290
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
67-251 2.33e-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: 48.41  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077    67 HQENLQLNQEVEAVREEllyFKAKGGGAVVeNTTTGLSRDVRTLkWLAEQTGVHIIAGAGFYVDathsaatramSVEQLT 146
Cdd:pfam01026   6 HLDFKDFDEDRDEVIER---AREAGVTGVV-VVGTDLEDFLRVL-ELAEKYPDRVYAAVGVHPH----------EADEAS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61889077   147 DVLISEILHGADGTSIKCgvIGEIGC-SWPLTDSER----KVLQATAHAQAQLGCPVIIHpgrNPGAPFQIIRVLQEAGA 221
Cdd:pfam01026  71 EDDLEALEKLAEHPKVVA--IGEIGLdYYYVDESPKeaqeEVFRRQLELAKELGLPVVIH---TRDAEEDLLEILKEAGA 145
                         170       180       190
                  ....*....|....*....|....*....|..
gi 61889077   222 DISKTVMSHldrsiF--DKKELLEFAQLGCYL 251
Cdd:pfam01026 146 PGARGVLHC-----FtgSVEEARKFLDLGFYI 172
 
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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