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Conserved domains on  [gi|1137940917|gb|OMS60671|]
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DNAase [Burkholderia pseudomallei]

Protein Classification

TatD family hydrolase( domain architecture ID 10000566)

TatD family hydrolase is a metal-dependent hydrolase similar to Homo sapiens deoxyribonuclease TATDN3

CATH:  3.20.20.140
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016788|GO:0004536
PubMed:  10747959
SCOP:  4002861

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
2-257 2.50e-134

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


:

Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 379.40  E-value: 2.50e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDH-EDAREPTVAELVEL 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNVYAAVGLHPHDaKEHDEEDLAELEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEgrsiADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTE 160
Cdd:COG0084    81 AAHPKVVAIGEIGLDYYRDK----SPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:COG0084   157 SLEQAKRALDLGFYISFGGIVTFKNAKKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISL 236
                         250
                  ....*....|....*..
gi 1137940917 241 EALGAATSRNFFRLFKI 257
Cdd:COG0084   237 EELAEATTANARRLFGL 253
 
Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
2-257 2.50e-134

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


Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 379.40  E-value: 2.50e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDH-EDAREPTVAELVEL 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNVYAAVGLHPHDaKEHDEEDLAELEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEgrsiADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTE 160
Cdd:COG0084    81 AAHPKVVAIGEIGLDYYRDK----SPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:COG0084   157 SLEQAKRALDLGFYISFGGIVTFKNAKKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISL 236
                         250
                  ....*....|....*..
gi 1137940917 241 EALGAATSRNFFRLFKI 257
Cdd:COG0084   237 EELAEATTANARRLFGL 253
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
2-256 3.04e-107

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: 310.66  E-value: 3.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDH-EDAREPTVAELVEL 80
Cdd:cd01310     1 LIDTHCHLDFPQFDADRDDVLARAREAGVIKIIVVGTDLKSSKRALELAKKYDNVYAAVGLHPHDaDEHVDEDLDLLELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEGrsiaDMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERaSVPGGVMHCFTE 160
Cdd:cd01310    81 AANPKVVAIGEIGLDYYRDKS----PREVQKEVFRAQLELAKELNLPVVIHSRDAHEDVLEILKEYG-PPKRGVFHCFSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:cd01310   156 SAEEAKELLDLGFYISISGIVTFKNANELREVVKEIPLERLLLETDSPYLAPVPFRGKRNEPAYVKHVAEKIAELKGISV 235
                         250
                  ....*....|....*.
gi 1137940917 241 EALGAATSRNFFRLFK 256
Cdd:cd01310   236 EEVAEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
3-256 1.21e-101

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: 296.48  E-value: 1.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   3 VDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDN-VFASVGVHP-DHEDAREPTVAELVEL 80
Cdd:pfam01026   1 IDTHCHLDFKDFDEDRDEVIERAREAGVTGVVVVGTDLEDFLRVLELAEKYPDrVYAAVGVHPhEADEASEDDLEALEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRlegRSIADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTE 160
Cdd:pfam01026  81 AEHPKVVAIGEIGLDYYY---VDESPKEAQEEVFRRQLELAKELGLPVVIHTRDAEEDLLEILKEAGAPGARGVLHCFTG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:pfam01026 158 SVEEARKFLDLGFYISISGIVTFKNAKKLREVAAAIPLDRLLVETDAPYLAPVPYRGKRNEPAYVPYVVEKLAELKGISP 237
                         250
                  ....*....|....*.
gi 1137940917 241 EALGAATSRNFFRLFK 256
Cdd:pfam01026 238 EEVAEITTENAERLFG 253
TIGR00010 TIGR00010
hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large ...
2-257 3.73e-96

hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large superfamily of proteins, including a number of different enzymes that act as hydrolases at C-N bonds other than peptide bonds (EC 3.5.-.-), many uncharacterized proteins, and the members of this family. Several genomes have multiple paralogs related to this family. However, a set of 17 proteins can be found, one each from 17 of the first 20 genomes, such that each member forms a bidirectional best hit across genomes with all other members of the set. This core set (and one other near-perfect member), but not the other paralogs, form the seed for this model. Additionally, members of the seed alignment and all trusted hits, but not all paralogs, have a conserved motif DxHxH near the amino end. The member from E. coli was recently shown to have DNase activity. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272852 [Multi-domain]  Cd Length: 252  Bit Score: 282.61  E-value: 3.73e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHP-DHEDAREPTVAELVEL 80
Cdd:TIGR00010   1 LIDAHCHLDFLDFEEDVEEVIERAKAAGVTAVVAVGTDLEDFLRALELAEKYPNVYAAVGVHPlDVDDDTKEDIKELERL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEGrsiaDMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGgVMHCFTE 160
Cdd:TIGR00010  81 AAHPKVVAIGETGLDYYKADE----YKRRQEEVFRAQLQLAEELNLPVIIHARDAEEDVLDILREEKPKVGG-VLHCFTG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:TIGR00010 156 DAELAKKLLDLGFYISISGIVTFKNAKSLREVVRKIPLERLLVETDSPYLAPVPYRGKRNEPAFVRYTVEAIAEIKGIDV 235
                         250
                  ....*....|....*..
gi 1137940917 241 EALGAATSRNFFRLFKI 257
Cdd:TIGR00010 236 EELAQITTKNAKRLFGL 252
PRK10812 PRK10812
putative DNAse; Provisional
1-257 2.68e-78

putative DNAse; Provisional


Pssm-ID: 236767 [Multi-domain]  Cd Length: 265  Bit Score: 237.73  E-value: 2.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   1 MF-VDSHCHIN---FEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDHEDarEP-TVA 75
Cdd:PRK10812    1 MFlVDSHCHLDgldYQSLHKDVDDVLAKAAARDVKFCLAVATTLPGYRHMRDLVGERDNVVFSCGVHPLNQD--EPyDVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  76 ELVELAAHPKVVAIGETGLDYYRLEgrsiADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVM 155
Cdd:PRK10812   79 ELRRLAAEEGVVAMGETGLDYYYTP----ETKVRQQESFRHHIQIGRELNKPVIVHTRDARADTLAILREEKVTDCGGVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 156 HCFTEPWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQ 235
Cdd:PRK10812  155 HCFTEDRETAGKLLDLGFYISFSGIVTFRNAEQLRDAARYVPLDRLLVETDSPYLAPVPHRGKENQPAMVRDVAEYMAVL 234
                         250       260
                  ....*....|....*....|..
gi 1137940917 236 REMTDEALGAATSRNFFRLFKI 257
Cdd:PRK10812  235 KGVSVEELAQVTTDNFARLFHI 256
 
Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
2-257 2.50e-134

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


Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 379.40  E-value: 2.50e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDH-EDAREPTVAELVEL 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNVYAAVGLHPHDaKEHDEEDLAELEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEgrsiADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTE 160
Cdd:COG0084    81 AAHPKVVAIGEIGLDYYRDK----SPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:COG0084   157 SLEQAKRALDLGFYISFGGIVTFKNAKKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISL 236
                         250
                  ....*....|....*..
gi 1137940917 241 EALGAATSRNFFRLFKI 257
Cdd:COG0084   237 EELAEATTANARRLFGL 253
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
2-256 3.04e-107

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: 310.66  E-value: 3.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDH-EDAREPTVAELVEL 80
Cdd:cd01310     1 LIDTHCHLDFPQFDADRDDVLARAREAGVIKIIVVGTDLKSSKRALELAKKYDNVYAAVGLHPHDaDEHVDEDLDLLELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEGrsiaDMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERaSVPGGVMHCFTE 160
Cdd:cd01310    81 AANPKVVAIGEIGLDYYRDKS----PREVQKEVFRAQLELAKELNLPVVIHSRDAHEDVLEILKEYG-PPKRGVFHCFSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:cd01310   156 SAEEAKELLDLGFYISISGIVTFKNANELREVVKEIPLERLLLETDSPYLAPVPFRGKRNEPAYVKHVAEKIAELKGISV 235
                         250
                  ....*....|....*.
gi 1137940917 241 EALGAATSRNFFRLFK 256
Cdd:cd01310   236 EEVAEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
3-256 1.21e-101

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: 296.48  E-value: 1.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   3 VDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDN-VFASVGVHP-DHEDAREPTVAELVEL 80
Cdd:pfam01026   1 IDTHCHLDFKDFDEDRDEVIERAREAGVTGVVVVGTDLEDFLRVLELAEKYPDrVYAAVGVHPhEADEASEDDLEALEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRlegRSIADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTE 160
Cdd:pfam01026  81 AEHPKVVAIGEIGLDYYY---VDESPKEAQEEVFRRQLELAKELGLPVVIHTRDAEEDLLEILKEAGAPGARGVLHCFTG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:pfam01026 158 SVEEARKFLDLGFYISISGIVTFKNAKKLREVAAAIPLDRLLVETDAPYLAPVPYRGKRNEPAYVPYVVEKLAELKGISP 237
                         250
                  ....*....|....*.
gi 1137940917 241 EALGAATSRNFFRLFK 256
Cdd:pfam01026 238 EEVAEITTENAERLFG 253
TIGR00010 TIGR00010
hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large ...
2-257 3.73e-96

hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large superfamily of proteins, including a number of different enzymes that act as hydrolases at C-N bonds other than peptide bonds (EC 3.5.-.-), many uncharacterized proteins, and the members of this family. Several genomes have multiple paralogs related to this family. However, a set of 17 proteins can be found, one each from 17 of the first 20 genomes, such that each member forms a bidirectional best hit across genomes with all other members of the set. This core set (and one other near-perfect member), but not the other paralogs, form the seed for this model. Additionally, members of the seed alignment and all trusted hits, but not all paralogs, have a conserved motif DxHxH near the amino end. The member from E. coli was recently shown to have DNase activity. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272852 [Multi-domain]  Cd Length: 252  Bit Score: 282.61  E-value: 3.73e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHP-DHEDAREPTVAELVEL 80
Cdd:TIGR00010   1 LIDAHCHLDFLDFEEDVEEVIERAKAAGVTAVVAVGTDLEDFLRALELAEKYPNVYAAVGVHPlDVDDDTKEDIKELERL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  81 AAHPKVVAIGETGLDYYRLEGrsiaDMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGgVMHCFTE 160
Cdd:TIGR00010  81 AAHPKVVAIGETGLDYYKADE----YKRRQEEVFRAQLQLAEELNLPVIIHARDAEEDVLDILREEKPKVGG-VLHCFTG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 161 PWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQREMTD 240
Cdd:TIGR00010 156 DAELAKKLLDLGFYISISGIVTFKNAKSLREVVRKIPLERLLVETDSPYLAPVPYRGKRNEPAFVRYTVEAIAEIKGIDV 235
                         250
                  ....*....|....*..
gi 1137940917 241 EALGAATSRNFFRLFKI 257
Cdd:TIGR00010 236 EELAQITTKNAKRLFGL 252
PRK10812 PRK10812
putative DNAse; Provisional
1-257 2.68e-78

putative DNAse; Provisional


Pssm-ID: 236767 [Multi-domain]  Cd Length: 265  Bit Score: 237.73  E-value: 2.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   1 MF-VDSHCHIN---FEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDHEDarEP-TVA 75
Cdd:PRK10812    1 MFlVDSHCHLDgldYQSLHKDVDDVLAKAAARDVKFCLAVATTLPGYRHMRDLVGERDNVVFSCGVHPLNQD--EPyDVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  76 ELVELAAHPKVVAIGETGLDYYRLEgrsiADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVM 155
Cdd:PRK10812   79 ELRRLAAEEGVVAMGETGLDYYYTP----ETKVRQQESFRHHIQIGRELNKPVIVHTRDARADTLAILREEKVTDCGGVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 156 HCFTEPWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAAQ 235
Cdd:PRK10812  155 HCFTEDRETAGKLLDLGFYISFSGIVTFRNAEQLRDAARYVPLDRLLVETDSPYLAPVPHRGKENQPAMVRDVAEYMAVL 234
                         250       260
                  ....*....|....*....|..
gi 1137940917 236 REMTDEALGAATSRNFFRLFKI 257
Cdd:PRK10812  235 KGVSVEELAQVTTDNFARLFHI 256
PRK10425 PRK10425
3'-5' ssDNA/RNA exonuclease TatD;
19-257 4.96e-36

3'-5' ssDNA/RNA exonuclease TatD;


Pssm-ID: 182449  Cd Length: 258  Bit Score: 129.02  E-value: 4.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  19 PQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHPDHEDAREPTVAE-LVELAAHPKVVAIGETGLDYy 97
Cdd:PRK10425   18 DDVVARAFAAGVNGMLITGTNLRESQQAQKLARQYPSCWSTAGVHPHDSSQWQAATEEaIIELAAQPEVVAIGECGLDF- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  98 rleGRSIADMQWQRERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERASVPGGVMHCFTEPWPVAEAALAQNFHISL 177
Cdd:PRK10425   97 ---NRNFSTPEEQERAFVAQLAIAAELNMPVFMHCRDAHERFMALLEPWLDKLPGAVLHCFTGTREEMQACLARGLYIGI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 178 SGIVT-FKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGK----RNEPAYVSYVGRFIAAQREMTDEALGAATSRNFF 252
Cdd:PRK10425  174 TGWVCdERRGLELRELLPLIPAERLLLETDAPYLLPRDLTPKpasrRNEPAFLPHILQRIAHWRGEDAAWLAATTDANAR 253

                  ....*
gi 1137940917 253 RLFKI 257
Cdd:PRK10425  254 TLFGL 258
PRK11449 PRK11449
metal-dependent hydrolase;
2-257 8.01e-29

metal-dependent hydrolase;


Pssm-ID: 171118 [Multi-domain]  Cd Length: 258  Bit Score: 110.05  E-value: 8.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLPQVLENMREHGVTHALCVSVDLETLPAVLAIARDHDNVFASVGVHP----DHEDAREPTVAEl 77
Cdd:PRK11449    5 FIDTHCHFDFPPFSGDEEASLQRAAQAGVGKIIVPATEAENFARVLALAERYQPLYAALGLHPgmleKHSDVSLDQLQQ- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  78 vELAAHP-KVVAIGETGLDYYRlegrsiADMQWQR-ERF-RTHIRAAHATGKPLIVHTRaSSEDTLRIMAEERASVPGGV 154
Cdd:PRK11449   84 -ALERRPaKVVAVGEIGLDLFG------DDPQFERqQWLlDEQLKLAKRYDLPVILHSR-RTHDKLAMHLKRHDLPRTGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 155 MHCFTEPWPVAEAALAQNFHISLSGIVTFKSAADVQEVARRVPLERLLIETDSPYLAPVPYRGKRNEPAYVSYVGRFIAA 234
Cdd:PRK11449  156 VHGFSGSLQQAERFVQLGYKIGVGGTITYPRASKTRDVIAKLPLASLLLETDAPDMPLNGFQGQPNRPEQAARVFDVLCE 235
                         250       260
                  ....*....|....*....|...
gi 1137940917 235 QREMTDEALGAATSRNFFRLFKI 257
Cdd:PRK11449  236 LRPEPADEIAEVLLNNTYTLFNV 258
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-259 2.34e-10

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 59.22  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   1 MFVDSHCHInfeglaERLPQVLENMREHGVTHALCVSVDLETLP----------AVLAIARDHDNVFASVG-VHPDHEDA 69
Cdd:COG2159     2 MIIDVHTHL------GTPEERLADMDEAGIDKAVLSPTPLADPElaalaraandWLAELVARYPDRFIGFAtVDPQDPDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  70 repTVAELVELAAHPKVVAIgETGLDYYrleGRSIADmqwqrERFRTHIRAAHATGKPLIVHTRASSEDTLRIMAEERAS 149
Cdd:COG2159    76 ---AVEELERAVEELGFRGV-KLHPAVG---GFPLDD-----PRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 150 VP-GGVMHCFTE----------PW--PVAEAALAQ--NFHISLSGIVTFKSAadVQEVARRVPLERLLIETDSPYLAPVP 214
Cdd:COG2159   144 LIlSGVAERFPDlkfilahgggPWlpELLGRLLKRlpNVYFDTSGVFPRPEA--LRELLETLGADRILFGSDYPHWDPPE 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1137940917 215 YRgkrnepayvsyvgRFIAAQREMTDEALGAATSRNFFRLFKIAR 259
Cdd:COG2159   222 AL-------------EALEELPGLSEEDREKILGGNAARLLGLDA 253
COG1099 COG1099
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
57-206 2.35e-05

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


Pssm-ID: 440716 [Multi-domain]  Cd Length: 260  Bit Score: 44.44  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  57 FASVGVHP----DHEDAREpTVAELVELAAHPKVVAIGETGLDyyrlegrsiaDMQ-WQRERFRTHIRAAHATGKPLIVH 131
Cdd:COG1099    69 YCTLGLNPkeanNRRLAEE-VLELLPRYLDKEGVVAIGEIGLD----------DQTpEEEEVFREQLELARELDLPVLVH 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 132 T--RASSEDTLRIMAEERAS--VPGGVM--HCFTEpwpVAEAALAQNFHISLS-GIVTFKSAADVQEVARRVPLERLLIE 204
Cdd:COG1099   138 TphRDKKEGTRRILDVLRESglDPERVLidHNNEE---TVKLVLDTGFWAGFTiYPSTKMSPERAVDILEEYGTERILVN 214

                  ..
gi 1137940917 205 TD 206
Cdd:COG1099   215 SA 216
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
3-208 4.94e-05

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 43.66  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   3 VDSHCHInFEGLAERLP---------------QVLENMREHGVTHALCVSVD---LETlPAVLAIARDHDNVFASVG-VH 63
Cdd:COG3618     3 IDAHHHV-WDPDRGRYPwlpdrsypprdatpeDYLALLDALGVDRAVLVQASfygADN-RYLLDAAARHPDRLRGVAwVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  64 PDHEDAreptVAELVELAAHpKVVAIgetgldyyR--LEGRSIADMqwQRERFRTHIRAAHATGKPLIVHTRAsseDTLR 141
Cdd:COG3618    81 LDAPDA----AAELARLAAA-GVRGV--------RfnLQGEPDGWL--LDPAFRRGLARLAELGLHFDLLVDP---RQLP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 142 IMAEERASVPGGVM---HCF-------TEPWPVAEAALAQ--NFHISLSGIVTF----KSAADVQEVARRV----PLERL 201
Cdd:COG3618   143 ALAPLLARLPDLPVvidHLGkpdiaagDDPWFAALLALAArpNVWVKLSGLYREsdagWPYADLRPYARALleafGPDRL 222

                  ....*..
gi 1137940917 202 LIETDSP 208
Cdd:COG3618   223 MWGSDWP 229
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
2-247 1.24e-03

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: 39.62  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   2 FVDSHCHINFEGLAERLP--------------------QVLENMREHGVTHALCVSV------DLETLPAVLAIARDHDN 55
Cdd:cd01292     1 FIDTHVHLDGSALRGTRLnlelkeaeelspedlyedtlRALEALLAGGVTTVVDMGStpppttTKAAIEAVAEAARASAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  56 VFASVGVHPDHEDAREPTVAELVELAAHPKVVAIGETGLDYYRLEGRSIADMqwqrERFRTHIRAAHATGKPLIVHTRAS 135
Cdd:cd01292    81 IRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSD----ESLRRVLEEARKLGLPVVIHAGEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917 136 S---EDTLRIMAEERASVPGGVMHCFTEPWPVAEAALAQNFHISLSGIVTFKSAADVQ--EVARRVpLE---RLLIETDS 207
Cdd:cd01292   157 PdptRALEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGEgaEALRRL-LElgiRVTLGTDG 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1137940917 208 PYLAPVPYrgkrnePAYVSYVGRFIAAQREMTDEALGAAT 247
Cdd:cd01292   236 PPHPLGTD------LLALLRLLLKVLRLGLSLEEALRLAT 269
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
4-171 6.85e-03

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: 37.24  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917   4 DSHCHINFEGLAERLP-QVLENMREHGVtHALcvsVDLETL------PAVLAIARDHD-NVFASVGVHPDH---EDAREP 72
Cdd:cd00530    19 DPPEVDDFDLADVEAAkEELKRFRAHGG-RTI---VDATPPgigrdvEKLAEVARATGvNIVAATGFYKDAfypEWVRLR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137940917  73 TVAELVEL--------AAHPKVVA--IGETGlDYYRLEgrsiadmQWQRERFRTHIRAAHATGKPLIVHTRASS---EDT 139
Cdd:cd00530    95 SVEELTDMlireieegIEGTGIKAgiIKEAG-GSPAIT-------PLEEKVLRAAARAQKETGVPISTHTQAGLtmgLEQ 166
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1137940917 140 LRIMAEERASvPGGVM--HCFTEPWPVAEAALAQ 171
Cdd:cd00530   167 LRILEEEGVD-PSKVVigHLDRNDDPDYLLKIAA 199
 
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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