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Conserved domains on  [gi|568912253|ref|XP_006497465|]
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phosphotriesterase-related protein isoform X3 [Mus musculus]

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 ...
15-279 5.26e-126

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: 360.72  E-value: 5.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   15 VEPSQLGRTLTHEHLTMTFDSFYCPPPPCHEVTSKEP------------------IMMKN---------LFWI------- 60
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKEVaaireellylkargvgalVENTTtglgrdvhtLKWVaeqtgvn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   61 --------QKNPYSHRENLQLNQELTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVII 132
Cdd:pfam02126  81 ivagtgfyVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPIST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  133 HPGRNPGAPFQIIRILQEAGADISKTVMSHLDrTIFDKKELLEFAQLGCYLEYDLFGTELlnyqlspdidMPDDNKRIRR 212
Cdd:pfam02126 161 HTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRR 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912253  213 VHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNIVPKMLLRGLTERVLDKILIENPKQWLT 279
Cdd:pfam02126 230 VHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-279 5.26e-126

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 360.72  E-value: 5.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   15 VEPSQLGRTLTHEHLTMTFDSFYCPPPPCHEVTSKEP------------------IMMKN---------LFWI------- 60
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKEVaaireellylkargvgalVENTTtglgrdvhtLKWVaeqtgvn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   61 --------QKNPYSHRENLQLNQELTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVII 132
Cdd:pfam02126  81 ivagtgfyVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPIST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  133 HPGRNPGAPFQIIRILQEAGADISKTVMSHLDrTIFDKKELLEFAQLGCYLEYDLFGTELlnyqlspdidMPDDNKRIRR 212
Cdd:pfam02126 161 HTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRR 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912253  213 VHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNIVPKMLLRGLTERVLDKILIENPKQWLT 279
Cdd:pfam02126 230 VHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-278 2.85e-102

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: 299.95  E-value: 2.85e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  21 GRTLTHEHLTMTFDSFYCPPPP------------CHEVTSKE------------------PIMMKNL------------- 57
Cdd:cd00530    1 GVTLTHEHLIIDSSGFVRDPPEvddfdladveaaKEELKRFRahggrtivdatppgigrdVEKLAEVaratgvnivaatg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  58 FWIQKNpYSHRENLQLNQELTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVIIHPGRN 137
Cdd:cd00530   81 FYKDAF-YPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLEEKVLRAAARAQKETGVPISTHTQAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 138 PGAPFQIIRILQEAGADISKTVMSHLDRTIfDKKELLEFAQLGCYLEYDLFGTELLNyqlspdiDMPDDNKRIRRVHFLV 217
Cdd:cd00530  160 LTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDKIF-------GYPSDETRADAVKALI 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912253 218 DEGYEDRILMAHDIHTKHRLMK-YGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQWL 278
Cdd:cd00530  232 DEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILVENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-280 2.65e-67

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 211.57  E-value: 2.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   5 SGKVQTVLGLVEPSQLGRTLTHEHLTMTFDSFYCPPPP-----------CHEVT-------------------------- 47
Cdd:COG1735    1 MGFVRTVLGPIPPEELGVTLMHEHLFVDLPGVRQDPPAdddelddveaaVEELErfkaaggrtivdatpiglgrdpealr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  48 --SKE---PIMMKNLFWiqKNPYSHRENLQLN-QELTDVLINEILHGADGTSIKCGVIgEIGCS-WPLTDSERKILEATA 120
Cdd:COG1735   81 riSEAtglNIVAATGFY--KEPFHPEWVLGASvDELAELLIREITEGIDGTGVRAGVI-KIGTSyGGITPDEEKVLRAAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 121 HAQAQLGCPVIIHPGRNPGAPfQIIRILQEAGADISKTVMSHLDRTiFDKKELLEFAQLGCYLEYDLFGteLLNYQlspd 200
Cdd:COG1735  158 RAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRELADRGAYLEFDGIG--RDKYY---- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 201 idmpDDNKRIRRVHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQWLTF 280
Cdd:COG1735  230 ----PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPRLRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
75-277 2.19e-26

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 104.52  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  75 QELTDVLINEILHGADGTSIKCGVIGEIGCS-WPLTDSERKILEATAHAQAQLGCPVIIHPGRNPGAPFQIiRILQEAGA 153
Cdd:PRK09875  99 QELAQEMVDEIEQGIDGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQL-ALLQAHGV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 154 DISKTVMSHLDrtIFDKKE-LLEFAQLGCYLEYDLFGTEllNYqlspdidMPDDnKRIRRVHFLVDEGYEDRILMAHDIH 232
Cdd:PRK09875 178 DLSRVTVGHCD--LKDNLDnILKMIDLGAYVQFDTIGKN--SY-------YPDE-KRIAMLHALRDRGLLNRVMLSMDIT 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568912253 233 TKHRLMKYGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQW 277
Cdd:PRK09875 246 RRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-279 5.26e-126

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 360.72  E-value: 5.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   15 VEPSQLGRTLTHEHLTMTFDSFYCPPPPCHEVTSKEP------------------IMMKN---------LFWI------- 60
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKEVaaireellylkargvgalVENTTtglgrdvhtLKWVaeqtgvn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   61 --------QKNPYSHRENLQLNQELTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVII 132
Cdd:pfam02126  81 ivagtgfyVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSWPLTPSEEKVLEATAHAHAQTGCPIST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  133 HPGRNPGAPFQIIRILQEAGADISKTVMSHLDrTIFDKKELLEFAQLGCYLEYDLFGTELlnyqlspdidMPDDNKRIRR 212
Cdd:pfam02126 161 HTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYDLFGYQL----------MPPDNKRIRR 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912253  213 VHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSH--ILTNIVPKMLLRGLTERVLDKILIENPKQWLT 279
Cdd:pfam02126 230 VHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTERVLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-278 2.85e-102

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: 299.95  E-value: 2.85e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  21 GRTLTHEHLTMTFDSFYCPPPP------------CHEVTSKE------------------PIMMKNL------------- 57
Cdd:cd00530    1 GVTLTHEHLIIDSSGFVRDPPEvddfdladveaaKEELKRFRahggrtivdatppgigrdVEKLAEVaratgvnivaatg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  58 FWIQKNpYSHRENLQLNQELTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVIIHPGRN 137
Cdd:cd00530   81 FYKDAF-YPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLEEKVLRAAARAQKETGVPISTHTQAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 138 PGAPFQIIRILQEAGADISKTVMSHLDRTIfDKKELLEFAQLGCYLEYDLFGTELLNyqlspdiDMPDDNKRIRRVHFLV 217
Cdd:cd00530  160 LTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDKIF-------GYPSDETRADAVKALI 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912253 218 DEGYEDRILMAHDIHTKHRLMK-YGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQWL 278
Cdd:cd00530  232 DEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILVENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-280 2.65e-67

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 211.57  E-value: 2.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   5 SGKVQTVLGLVEPSQLGRTLTHEHLTMTFDSFYCPPPP-----------CHEVT-------------------------- 47
Cdd:COG1735    1 MGFVRTVLGPIPPEELGVTLMHEHLFVDLPGVRQDPPAdddelddveaaVEELErfkaaggrtivdatpiglgrdpealr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  48 --SKE---PIMMKNLFWiqKNPYSHRENLQLN-QELTDVLINEILHGADGTSIKCGVIgEIGCS-WPLTDSERKILEATA 120
Cdd:COG1735   81 riSEAtglNIVAATGFY--KEPFHPEWVLGASvDELAELLIREITEGIDGTGVRAGVI-KIGTSyGGITPDEEKVLRAAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 121 HAQAQLGCPVIIHPGRNPGAPfQIIRILQEAGADISKTVMSHLDRTiFDKKELLEFAQLGCYLEYDLFGteLLNYQlspd 200
Cdd:COG1735  158 RAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRELADRGAYLEFDGIG--RDKYY---- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 201 idmpDDNKRIRRVHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQWLTF 280
Cdd:COG1735  230 ----PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPRLRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
75-277 2.19e-26

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 104.52  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253  75 QELTDVLINEILHGADGTSIKCGVIGEIGCS-WPLTDSERKILEATAHAQAQLGCPVIIHPGRNPGAPFQIiRILQEAGA 153
Cdd:PRK09875  99 QELAQEMVDEIEQGIDGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQL-ALLQAHGV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253 154 DISKTVMSHLDrtIFDKKE-LLEFAQLGCYLEYDLFGTEllNYqlspdidMPDDnKRIRRVHFLVDEGYEDRILMAHDIH 232
Cdd:PRK09875 178 DLSRVTVGHCD--LKDNLDnILKMIDLGAYVQFDTIGKN--SY-------YPDE-KRIAMLHALRDRGLLNRVMLSMDIT 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568912253 233 TKHRLMKYGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQW 277
Cdd:PRK09875 246 RRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
95-183 3.88e-03

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: 38.01  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912253   95 KCGVIGEIGC-SWPLTDSER----KILEATAHAQAQLGCPVIIHpgrNPGAPFQIIRILQEAGADISKTVMSHldrtiF- 168
Cdd:pfam01026  85 KVVAIGEIGLdYYYVDESPKeaqeEVFRRQLELAKELGLPVVIH---TRDAEEDLLEILKEAGAPGARGVLHC-----Ft 156
                          90
                  ....*....|....*.
gi 568912253  169 -DKKELLEFAQLGCYL 183
Cdd:pfam01026 157 gSVEEARKFLDLGFYI 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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