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Conserved domains on  [gi|1209303776|ref|WP_088348868|]
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MULTISPECIES: TatD family hydrolase [Rhodomicrobium]

Protein Classification

TatD family hydrolase( domain architecture ID 11437802)

TatD family hydrolase with similarity to Schizosaccharomyces pombe deoxyribonuclease Tat-D, a cytoplasmic protein that exhibits magnesium-dependent exo- and endonuclease activities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1099 COG1099
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
1-259 4.59e-168

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


:

Pssm-ID: 440716 [Multi-domain]  Cd Length: 260  Bit Score: 466.24  E-value: 4.59e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   1 MYIDPHAHMISRTTNDYEAMAAAGIVAVIEPAFWVGQPRTYVGTYIDYLSAIVGWERFRAGQFGIRHYCTAGLNSKEANN 80
Cdd:COG1099     2 RIIDPHIHMTSRTTDDYEAMAAAGVVAVIEPAFWLGQPRTSAGSFRDYFDSLVGWERFRAAQFGIKHYCTLGLNPKEANN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  81 EELAEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPHRDKKRGTTRSMDVALEHGLDP 160
Cdd:COG1099    82 RRLAEEVLELLPRYLDKEGVVAIGEIGLDDQTPEEEEVFREQLELARELDLPVLVHTPHRDKKEGTRRILDVLRESGLDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 161 SQVIVDHNNEETVAEVLQRGFWAAFSIYPSTKMGDARMVQLLKQYGAERIIVDSACDWGVSEPLGVPKTAELALKSGVPE 240
Cdd:COG1099   162 ERVLIDHNNEETVKLVLDTGFWAGFTIYPSTKMSPERAVDILEEYGTERILVNSAADWGPSDPLAVPKTALEMLRRGIDE 241

                         250
                  ....*....|....*....
gi 1209303776 241 RHVRMACYENALAAYGRSG 259
Cdd:COG1099   242 EDIRKVVYENPLAFFGQSG 260
 
Name Accession Description Interval E-value
COG1099 COG1099
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
1-259 4.59e-168

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 440716 [Multi-domain]  Cd Length: 260  Bit Score: 466.24  E-value: 4.59e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   1 MYIDPHAHMISRTTNDYEAMAAAGIVAVIEPAFWVGQPRTYVGTYIDYLSAIVGWERFRAGQFGIRHYCTAGLNSKEANN 80
Cdd:COG1099     2 RIIDPHIHMTSRTTDDYEAMAAAGVVAVIEPAFWLGQPRTSAGSFRDYFDSLVGWERFRAAQFGIKHYCTLGLNPKEANN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  81 EELAEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPHRDKKRGTTRSMDVALEHGLDP 160
Cdd:COG1099    82 RRLAEEVLELLPRYLDKEGVVAIGEIGLDDQTPEEEEVFREQLELARELDLPVLVHTPHRDKKEGTRRILDVLRESGLDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 161 SQVIVDHNNEETVAEVLQRGFWAAFSIYPSTKMGDARMVQLLKQYGAERIIVDSACDWGVSEPLGVPKTAELALKSGVPE 240
Cdd:COG1099   162 ERVLIDHNNEETVKLVLDTGFWAGFTIYPSTKMSPERAVDILEEYGTERILVNSAADWGPSDPLAVPKTALEMLRRGIDE 241

                         250
                  ....*....|....*....
gi 1209303776 241 RHVRMACYENALAAYGRSG 259
Cdd:COG1099   242 EDIRKVVYENPLAFFGQSG 260
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
 2-256 7.61e-43

TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent DNase activity.


Pssm-ID: 238635 [Multi-domain]  Cd Length: 251  Bit Score: 147.33  E-value: 7.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   2 YIDPHAHMISRT-----TNDYEAMAAAGIVAVIEPAFWVGqprtyvgtyidylsaivGWERFR--AGQFGiRHYCTAGLN 74
Cdd:cd01310     1 LIDTHCHLDFPQfdadrDDVLARAREAGVIKIIVVGTDLK-----------------SSKRALelAKKYD-NVYAAVGLH 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  75 SKEANNEElaEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDK-----YFRAQLELAKELELPVMIHTPHRDKkrgttRS 149
Cdd:cd01310    63 PHDADEHV--DEDLDLLELLAANPKVVAIGEIGLDYYRDKSPRevqkeVFRAQLELAKELNLPVVIHSRDAHE-----DV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 150 MDVALEHGLDPsQVIVDHNNE--ETVAEVLQRGFWAAFSIYPSTKMGDaRMVQLLKQYGAERIIV--DSACDWGV----- 220
Cdd:cd01310   136 LEILKEYGPPK-RGVFHCFSGsaEEAKELLDLGFYISISGIVTFKNAN-ELREVVKEIPLERLLLetDSPYLAPVpfrgk 213

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1209303776 221 -SEPLGVPKTAEL--ALKsGVPERHVRMACYENALAAYG 256
Cdd:cd01310   214 rNEPAYVKHVAEKiaELK-GISVEEVAEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
 60-256 2.15e-17

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: 79.61  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  60 AGQFGIRHYCTAGL---NSKEANNEELAEgvmeiLPRFALKDGVVAIGEIG----YDEQTPLED--KYFRAQLELAKELE 130
Cdd:pfam01026  48 AEKYPDRVYAAVGVhphEADEASEDDLEA-----LEKLAEHPKVVAIGEIGldyyYVDESPKEAqeEVFRRQLELAKELG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 131 LPVMIHTphrdkkRGTTRSMDVALEHGLDPSQVIVDHN---NEETVAEVLQRGFWAAFSIYpSTKMGDARMVQLLKQYGA 207
Cdd:pfam01026 123 LPVVIHT------RDAEEDLLEILKEAGAPGARGVLHCftgSVEEARKFLDLGFYISISGI-VTFKNAKKLREVAAAIPL 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209303776 208 ERIIVDSACDWG--------VSEPLGVPKTAE-LALKSGVPERHVRMACYENALAAYG 256
Cdd:pfam01026 196 DRLLVETDAPYLapvpyrgkRNEPAYVPYVVEkLAELKGISPEEVAEITTENAERLFG 253
PRK10425 PRK10425
3'-5' ssDNA/RNA exonuclease TatD;
70-136 1.82e-06

3'-5' ssDNA/RNA exonuclease TatD;


Pssm-ID: 182449  Cd Length: 258  Bit Score: 48.13  E-value: 1.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209303776  70 TAGLNSKEANneELAEGVMEILPRFALKDGVVAIGEIGYDEQ----TPLEDKY-FRAQLELAKELELPVMIH 136
Cdd:PRK10425   58 TAGVHPHDSS--QWQAATEEAIIELAAQPEVVAIGECGLDFNrnfsTPEEQERaFVAQLAIAAELNMPVFMH 127
 
Name Accession Description Interval E-value
COG1099 COG1099
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
1-259 4.59e-168

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 440716 [Multi-domain]  Cd Length: 260  Bit Score: 466.24  E-value: 4.59e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   1 MYIDPHAHMISRTTNDYEAMAAAGIVAVIEPAFWVGQPRTYVGTYIDYLSAIVGWERFRAGQFGIRHYCTAGLNSKEANN 80
Cdd:COG1099     2 RIIDPHIHMTSRTTDDYEAMAAAGVVAVIEPAFWLGQPRTSAGSFRDYFDSLVGWERFRAAQFGIKHYCTLGLNPKEANN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  81 EELAEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPHRDKKRGTTRSMDVALEHGLDP 160
Cdd:COG1099    82 RRLAEEVLELLPRYLDKEGVVAIGEIGLDDQTPEEEEVFREQLELARELDLPVLVHTPHRDKKEGTRRILDVLRESGLDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 161 SQVIVDHNNEETVAEVLQRGFWAAFSIYPSTKMGDARMVQLLKQYGAERIIVDSACDWGVSEPLGVPKTAELALKSGVPE 240
Cdd:COG1099   162 ERVLIDHNNEETVKLVLDTGFWAGFTIYPSTKMSPERAVDILEEYGTERILVNSAADWGPSDPLAVPKTALEMLRRGIDE 241

                         250
                  ....*....|....*....
gi 1209303776 241 RHVRMACYENALAAYGRSG 259
Cdd:COG1099   242 EDIRKVVYENPLAFFGQSG 260
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
 2-256 7.61e-43

TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent DNase activity.


Pssm-ID: 238635 [Multi-domain]  Cd Length: 251  Bit Score: 147.33  E-value: 7.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   2 YIDPHAHMISRT-----TNDYEAMAAAGIVAVIEPAFWVGqprtyvgtyidylsaivGWERFR--AGQFGiRHYCTAGLN 74
Cdd:cd01310     1 LIDTHCHLDFPQfdadrDDVLARAREAGVIKIIVVGTDLK-----------------SSKRALelAKKYD-NVYAAVGLH 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  75 SKEANNEElaEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDK-----YFRAQLELAKELELPVMIHTPHRDKkrgttRS 149
Cdd:cd01310    63 PHDADEHV--DEDLDLLELLAANPKVVAIGEIGLDYYRDKSPRevqkeVFRAQLELAKELNLPVVIHSRDAHE-----DV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 150 MDVALEHGLDPsQVIVDHNNE--ETVAEVLQRGFWAAFSIYPSTKMGDaRMVQLLKQYGAERIIV--DSACDWGV----- 220
Cdd:cd01310   136 LEILKEYGPPK-RGVFHCFSGsaEEAKELLDLGFYISISGIVTFKNAN-ELREVVKEIPLERLLLetDSPYLAPVpfrgk 213

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1209303776 221 -SEPLGVPKTAEL--ALKsGVPERHVRMACYENALAAYG 256
Cdd:cd01310   214 rNEPAYVKHVAEKiaELK-GISVEEVAEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
 60-256 2.15e-17

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: 79.61  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  60 AGQFGIRHYCTAGL---NSKEANNEELAEgvmeiLPRFALKDGVVAIGEIG----YDEQTPLED--KYFRAQLELAKELE 130
Cdd:pfam01026  48 AEKYPDRVYAAVGVhphEADEASEDDLEA-----LEKLAEHPKVVAIGEIGldyyYVDESPKEAqeEVFRRQLELAKELG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 131 LPVMIHTphrdkkRGTTRSMDVALEHGLDPSQVIVDHN---NEETVAEVLQRGFWAAFSIYpSTKMGDARMVQLLKQYGA 207
Cdd:pfam01026 123 LPVVIHT------RDAEEDLLEILKEAGAPGARGVLHCftgSVEEARKFLDLGFYISISGI-VTFKNAKKLREVAAAIPL 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209303776 208 ERIIVDSACDWG--------VSEPLGVPKTAE-LALKSGVPERHVRMACYENALAAYG 256
Cdd:pfam01026 196 DRLLVETDAPYLapvpyrgkRNEPAYVPYVVEkLAELKGISPEEVAEITTENAERLFG 253
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
68-256 1.52e-14

3'->5' ssDNA/RNA exonuclease TatD [Cell motility];


Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 71.62  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  68 YCTAGL---NSKEANNEELAEgvmeiLPRFALKDGVVAIGEIG---YDEQTPLED--KYFRAQLELAKELELPVMIHTph 139
Cdd:COG0084    56 YAAVGLhphDAKEHDEEDLAE-----LEELAAHPKVVAIGEIGldyYRDKSPREVqeEAFRAQLALAKELGLPVIIHS-- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 140 RDkkrGTTRSMDVALEHGLDPSQVIVdHN---NEETVAEVLQRGFWaaFSI-----YPSTKmgdaRMVQLLKQYGAERII 211
Cdd:COG0084   129 RD---AHDDTLEILKEEGAPALGGVF-HCfsgSLEQAKRALDLGFY--ISFggivtFKNAK----KLREVAAAIPLDRLL 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 212 V--DS-----------ACdwgvsEPLGVPKTAE-LA-LKsGVPERHVRMACYENALAAYG 256
Cdd:COG0084   199 LetDApylapvpfrgkRN-----EPAYVPHVAEkLAeLR-GISLEELAEATTANARRLFG 252
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
 103-200 3.38e-09

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: 56.50  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 103 IGEIG-YDEQTPLEDKYFRAQLELAKELELPVMIHTPhrdkkRGTTRSMDVA---LEHGLDPSQVIVDH----NNEETVA 174
Cdd:cd00530   121 IKEAGgSPAITPLEEKVLRAAARAQKETGVPISTHTQ-----AGLTMGLEQLrilEEEGVDPSKVVIGHldrnDDPDYLL 195

                          90       100
                  ....*....|....*....|....*.
gi 1209303776 175 EVLQRGFWAAFSIYPSTKMGDARMVQ 200
Cdd:cd00530   196 KIAALGAYLEFDGIGKDKIFGYPSDE 221
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 16-251 4.89e-07

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.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 50.02  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  16 DYEAMAAAGIVAVIEPA--FWVGQPRTYVGTYIDYLSAIVGwerfragqfgIRHYCTAGLNSKEANNEELAEGVMEILPR 93
Cdd:cd01292    40 ALEALLAGGVTTVVDMGstPPPTTTKAAIEAVAEAARASAG----------IRVVLGLGIPGVPAAVDEDAEALLLELLR 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  94 FALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPHRDKKRGTTRSMdvaLEHGLDPSQVIVDHNN---E 170
Cdd:cd01292   110 RGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPTRALEDL---VALLRLGGRVVIGHVShldP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 171 ETVAEVLQRGFWaaFSIYPST------KMGDARMVQLLKQYGAeRII--VDSACDWGVSEPLGVPKTAELALKSGVPERH 242
Cdd:cd01292   187 ELLELLKEAGVS--LEVCPLSnyllgrDGEGAEALRRLLELGI-RVTlgTDGPPHPLGTDLLALLRLLLKVLRLGLSLEE 263

                         250
                  ....*....|
gi 1209303776 243 V-RMACYENA 251
Cdd:cd01292   264 AlRLATINPA 273
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
 81-185 1.62e-06

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


Pssm-ID: 441341  Cd Length: 305  Bit Score: 48.63  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  81 EELAEGVMEIlprfALKDGVVAIGeIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPHrdkkrGTT--RSMDVALEHGL 158
Cdd:COG1735   120 REITEGIDGT----GVRAGVIKIG-TSYGGITPDEEKVLRAAARAHRETGAPISTHTEA-----GTMglEQLDLLEEEGV 189

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1209303776 159 DPSQVIVDHNNEET----VAEVLQRGFWAAF 185
Cdd:COG1735   190 DPERVVIGHMDRNPdldyHRELADRGAYLEF 220
PRK10425 PRK10425
3'-5' ssDNA/RNA exonuclease TatD;
70-136 1.82e-06

3'-5' ssDNA/RNA exonuclease TatD;


Pssm-ID: 182449  Cd Length: 258  Bit Score: 48.13  E-value: 1.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209303776  70 TAGLNSKEANneELAEGVMEILPRFALKDGVVAIGEIGYDEQ----TPLEDKY-FRAQLELAKELELPVMIH 136
Cdd:PRK10425   58 TAGVHPHDSS--QWQAATEEAIIELAAQPEVVAIGECGLDFNrnfsTPEEQERaFVAQLAIAAELNMPVFMH 127
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
 1-256 8.96e-06

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 46.13  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   1 MYIDPHAHMISrTTNDYEAMAAAGI-VAVIEPAFWVGQPRTY-VGTYIDYLSAIVG--WERFRAgqfgirhycTAGLNSK 76
Cdd:COG2159     2 MIIDVHTHLGT-PEERLADMDEAGIdKAVLSPTPLADPELAAlARAANDWLAELVAryPDRFIG---------FATVDPQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  77 EAnneelaEGVMEILPRFALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHT--PHRDKKRGTTRSMDVAL 154
Cdd:COG2159    72 DP------DAAVEELERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPgtPPGPPPGLDLYYAAPLI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 155 EHGldpsqVIVDHNN-------------EETVAEVLQRG--FWAAFSIYPSTKmgdARMVQLLKQYGAERIIvdsacdWG 219
Cdd:COG2159   146 LSG-----VAERFPDlkfilahgggpwlPELLGRLLKRLpnVYFDTSGVFPRP---EALRELLETLGADRIL------FG 211

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1209303776 220 VSEPLGVPKTAELALKS--GVPERHVRMACYENALAAYG 256
Cdd:COG2159   212 SDYPHWDPPEALEALEElpGLSEEDREKILGGNAARLLG 250
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
 113-257 8.39e-05

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 43.29  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 113 PLEDKYFRAQLELAKELELPVMIHTPHRDKKRGTTRSMDVALEHGLD--PS-QVIVDH---------NNEETVAEVLQR- 179
Cdd:pfam04909 118 LLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAIQPLLLAGVARkfPDlKIVLDHgggpwipegLDDPAALALLARr 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 180 -GFWAAFSIYPSTKMGDA------RMVQLLKQYGAERIIVDSacDW---GVSEPLGVPKTAELALKSGVPERHVRMACYE 249
Cdd:pfam04909 198 pNVYVKLSGLYRDLYFDApladrpYLARLLEAFGPDRILFGS--DWphpPLEISPDDGVLLDLPLLLALSDEEREKILGG 275


                  ....*...
gi 1209303776 250 NALAAYGR 257
Cdd:pfam04909 276 NAARLYGL 283
PRK11449 PRK11449
metal-dependent hydrolase;
100-137 3.85e-04

metal-dependent hydrolase;


Pssm-ID: 171118 [Multi-domain]  Cd Length: 258  Bit Score: 41.10  E-value: 3.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1209303776 100 VVAIGEIGYD-----EQTPLEDKYFRAQLELAKELELPVMIHT 137
Cdd:PRK11449   92 VVAVGEIGLDlfgddPQFERQQWLLDEQLKLAKRYDLPVILHS 134
PTE pfam02126
Phosphotriesterase family;
96-214 1.07e-03

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 39.85  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  96 LKDGVvaIGEIGYDEQ-TPLEDKYFRAQLELAKELELPVMIHtPHRDKKRGTTRsMDVALEHGLDPSQVIVDH----NNE 170
Cdd:pfam02126 122 IKAGI--IGEIGCSWPlTPSEEKVLEATAHAHAQTGCPISTH-TGRNPGAGLQQ-IRILQEAGVDLSRVVMGHcdtiFDK 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209303776 171 ETVAEVLQRGFWAAF------SIYPSTKMgdARMVQLLKQYGAERIIVDS 214
Cdd:pfam02126 198 KELLEFIQLGCYLEYdlfgyqLMPPDNKR--IRRVHFLVDRGYEDRILLS 245
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 3-239 2.14e-03

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 39.17  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776   3 IDPHAHMISRTTNDYEAMAAAGIVAVIEpAFWVGQPRTY------VGTYIDYLSAIVGW-ERFRAGQF----GIRHY-CT 70
Cdd:COG1228    68 IDAHTHLGLGGGRAVEFEAGGGITPTVD-LVNPADKRLRralaagVTTVRDLPGGPLGLrDAIIAGESkllpGPRVLaAG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776  71 AGLNSKEANNEELAEGVMEILPRfALKDGVVAIGEIGYDEQTPLEDKYFRAQLELAKELELPVMIHTPhrdkkrgTTRSM 150
Cdd:COG1228   147 PALSLTGGAHARGPEEARAALRE-LLAEGADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAH-------QADDI 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209303776 151 DVALEHGLDpsqvIVDHNN---EETVAEVLQRG---FWAAFSIYPSTKMGDARMVQLLKQYGAERIivdsacdwgvsepl 224
Cdd:COG1228   219 RLAVEAGVD----SIEHGTyldDEVADLLAEAGtvvLVPTLSLFLALLEGAAAPVAAKARKVREAA-------------- 280

                         250
                  ....*....|....*
gi 1209303776 225 gvPKTAELALKSGVP 239
Cdd:COG1228   281 --LANARRLHDAGVP 293
 
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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