NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1376724297|gb|PTP19645|]
View 

TatD family deoxyribonuclease [Vibrio splendidus]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
1-253 1.76e-123

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


:

Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 351.28  E-value: 1.76e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVcRSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNV-YAAVGLHPHDAKEHDEEDLAELEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGSSLE 160
Cdd:COG0084    80 LAAHPKVVAIGEIGLDYYRDKSPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSGSLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:COG0084   160 QAKRALDLGFYISFGGIVTFKNAkKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISLEEL 239
                         250
                  ....*....|....
gi 1376724297 240 ENITTINAKSLFNL 253
Cdd:COG0084   240 AEATTANARRLFGL 253
 
Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
1-253 1.76e-123

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


Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 351.28  E-value: 1.76e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVcRSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNV-YAAVGLHPHDAKEHDEEDLAELEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGSSLE 160
Cdd:COG0084    80 LAAHPKVVAIGEIGLDYYRDKSPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSGSLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:COG0084   160 QAKRALDLGFYISFGGIVTFKNAkKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISLEEL 239
                         250
                  ....*....|....
gi 1376724297 240 ENITTINAKSLFNL 253
Cdd:COG0084   240 AEATTANARRLFGL 253
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
1-252 3.49e-99

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: 289.47  E-value: 3.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCrSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:cd01310     1 LIDTHCHLDFPQFDADRDDVLARAREAGVIKIIVVGTDLKSSKRALELAKKYDNVY-AAVGLHPHDADEHVDEDLDLLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLrKEQDGSLRGVFHCFGSSLE 160
Cdd:cd01310    80 LAANPKVVAIGEIGLDYYRDKSPREVQKEVFRAQLELAKELNLPVVIHSRDAHEDVLEIL-KEYGPPKRGVFHCFSGSAE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:cd01310   159 EAKELLDLGFYISISGIVTFKNAnELREVVKEIPLERLLLETDSPYLAPVPFRGKRNEPAYVKHVAEKIAELKGISVEEV 238
                         250
                  ....*....|...
gi 1376724297 240 ENITTINAKSLFN 252
Cdd:cd01310   239 AEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
2-252 2.41e-97

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: 284.92  E-value: 2.41e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   2 IDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMMGLHPCYVDANIEQTLKTIRAW 81
Cdd:pfam01026   1 IDTHCHLDFKDFDEDRDEVIERAREAGVTGVVVVGTDLEDFLRVLELAEKYPDRVYAAVGVHPHEADEASEDDLEALEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  82 FDKHDFIAVGEIGIDLYW-DKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGSSLE 160
Cdd:pfam01026  81 AEHPKVVAIGEIGLDYYYvDESPKEAQEEVFRRQLELAKELGLPVVIHTRDAEEDLLEILKEAGAPGARGVLHCFTGSVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:pfam01026 161 EARKFLDLGFYISISGIVTFKNAkKLREVAAAIPLDRLLVETDAPYLAPVPYRGKRNEPAYVPYVVEKLAELKGISPEEV 240
                         250
                  ....*....|...
gi 1376724297 240 ENITTINAKSLFN 252
Cdd:pfam01026 241 AEITTENAERLFG 253
TIGR00010 TIGR00010
hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large ...
1-253 1.86e-83

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: 249.87  E-value: 1.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMmGLHPCYVDANIEQTLKTIRA 80
Cdd:TIGR00010   1 LIDAHCHLDFLDFEEDVEEVIERAKAAGVTAVVAVGTDLEDFLRALELAEKYPNVYAAV-GVHPLDVDDDTKEDIKELER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 wFDKHDFI-AVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQdGSLRGVFHCFGSSL 159
Cdd:TIGR00010  80 -LAAHPKVvAIGETGLDYYKADEYKRRQEEVFRAQLQLAEELNLPVIIHARDAEEDVLDILREEK-PKVGGVLHCFTGDA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 160 EEAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEE 238
Cdd:TIGR00010 158 ELAKKLLDLGFYISISGIVTFKNAkSLREVVRKIPLERLLVETDSPYLAPVPYRGKRNEPAFVRYTVEAIAEIKGIDVEE 237
                         250
                  ....*....|....*
gi 1376724297 239 VENITTINAKSLFNL 253
Cdd:TIGR00010 238 LAQITTKNAKRLFGL 252
PRK10812 PRK10812
putative DNAse; Provisional
1-253 1.07e-44

putative DNAse; Provisional


Pssm-ID: 236767 [Multi-domain]  Cd Length: 265  Bit Score: 151.06  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFD---EDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMmGLHPCYVDANIEqtLKT 77
Cdd:PRK10812    3 LVDSHCHLDGLDYQslhKDVDDVLAKAAARDVKFCLAVATTLPGYRHMRDLVGERDNVVFSC-GVHPLNQDEPYD--VEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  78 IRAWFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGS 157
Cdd:PRK10812   80 LRRLAAEEGVVAMGETGLDYYYTPETKVRQQESFRHHIQIGRELNKPVIVHTRDARADTLAILREEKVTDCGGVLHCFTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 158 SLEEAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITL 236
Cdd:PRK10812  160 DRETAGKLLDLGFYISFSGIVTFRNAeQLRDAARYVPLDRLLVETDSPYLAPVPHRGKENQPAMVRDVAEYMAVLKGVSV 239
                         250
                  ....*....|....*..
gi 1376724297 237 EEVENITTINAKSLFNL 253
Cdd:PRK10812  240 EELAQVTTDNFARLFHI 256
 
Name Accession Description Interval E-value
TatD COG0084
3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
1-253 1.76e-123

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


Pssm-ID: 439854 [Multi-domain]  Cd Length: 253  Bit Score: 351.28  E-value: 1.76e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVcRSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:COG0084     1 LIDTHCHLDFPEFDEDRDEVLARARAAGVERIVVVGTDLESSERALELAERYPNV-YAAVGLHPHDAKEHDEEDLAELEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGSSLE 160
Cdd:COG0084    80 LAAHPKVVAIGEIGLDYYRDKSPREVQEEAFRAQLALAKELGLPVIIHSRDAHDDTLEILKEEGAPALGGVFHCFSGSLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:COG0084   160 QAKRALDLGFYISFGGIVTFKNAkKLREVAAAIPLDRLLLETDAPYLAPVPFRGKRNEPAYVPHVAEKLAELRGISLEEL 239
                         250
                  ....*....|....
gi 1376724297 240 ENITTINAKSLFNL 253
Cdd:COG0084   240 AEATTANARRLFGL 253
TatD_DNAse cd01310
TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent ...
1-252 3.49e-99

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: 289.47  E-value: 3.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCrSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:cd01310     1 LIDTHCHLDFPQFDADRDDVLARAREAGVIKIIVVGTDLKSSKRALELAKKYDNVY-AAVGLHPHDADEHVDEDLDLLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLrKEQDGSLRGVFHCFGSSLE 160
Cdd:cd01310    80 LAANPKVVAIGEIGLDYYRDKSPREVQKEVFRAQLELAKELNLPVVIHSRDAHEDVLEIL-KEYGPPKRGVFHCFSGSAE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:cd01310   159 EAKELLDLGFYISISGIVTFKNAnELREVVKEIPLERLLLETDSPYLAPVPFRGKRNEPAYVKHVAEKIAELKGISVEEV 238
                         250
                  ....*....|...
gi 1376724297 240 ENITTINAKSLFN 252
Cdd:cd01310   239 AEVTTENAKRLFG 251
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
2-252 2.41e-97

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: 284.92  E-value: 2.41e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   2 IDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMMGLHPCYVDANIEQTLKTIRAW 81
Cdd:pfam01026   1 IDTHCHLDFKDFDEDRDEVIERAREAGVTGVVVVGTDLEDFLRVLELAEKYPDRVYAAVGVHPHEADEASEDDLEALEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  82 FDKHDFIAVGEIGIDLYW-DKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGSSLE 160
Cdd:pfam01026  81 AEHPKVVAIGEIGLDYYYvDESPKEAQEEVFRRQLELAKELGLPVVIHTRDAEEDLLEILKEAGAPGARGVLHCFTGSVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 161 EAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEEV 239
Cdd:pfam01026 161 EARKFLDLGFYISISGIVTFKNAkKLREVAAAIPLDRLLVETDAPYLAPVPYRGKRNEPAYVPYVVEKLAELKGISPEEV 240
                         250
                  ....*....|...
gi 1376724297 240 ENITTINAKSLFN 252
Cdd:pfam01026 241 AEITTENAERLFG 253
TIGR00010 TIGR00010
hydrolase, TatD family; PSI-BLAST, starting with a urease alpha subunit, finds a large ...
1-253 1.86e-83

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: 249.87  E-value: 1.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMmGLHPCYVDANIEQTLKTIRA 80
Cdd:TIGR00010   1 LIDAHCHLDFLDFEEDVEEVIERAKAAGVTAVVAVGTDLEDFLRALELAEKYPNVYAAV-GVHPLDVDDDTKEDIKELER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 wFDKHDFI-AVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQdGSLRGVFHCFGSSL 159
Cdd:TIGR00010  80 -LAAHPKVvAIGETGLDYYKADEYKRRQEEVFRAQLQLAEELNLPVIIHARDAEEDVLDILREEK-PKVGGVLHCFTGDA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 160 EEAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEE 238
Cdd:TIGR00010 158 ELAKKLLDLGFYISISGIVTFKNAkSLREVVRKIPLERLLVETDSPYLAPVPYRGKRNEPAFVRYTVEAIAEIKGIDVEE 237
                         250
                  ....*....|....*
gi 1376724297 239 VENITTINAKSLFNL 253
Cdd:TIGR00010 238 LAQITTKNAKRLFGL 252
PRK10812 PRK10812
putative DNAse; Provisional
1-253 1.07e-44

putative DNAse; Provisional


Pssm-ID: 236767 [Multi-domain]  Cd Length: 265  Bit Score: 151.06  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFD---EDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVCRSMmGLHPCYVDANIEqtLKT 77
Cdd:PRK10812    3 LVDSHCHLDGLDYQslhKDVDDVLAKAAARDVKFCLAVATTLPGYRHMRDLVGERDNVVFSC-GVHPLNQDEPYD--VEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  78 IRAWFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDGSLRGVFHCFGS 157
Cdd:PRK10812   80 LRRLAAEEGVVAMGETGLDYYYTPETKVRQQESFRHHIQIGRELNKPVIVHTRDARADTLAILREEKVTDCGGVLHCFTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 158 SLEEAQAINELGFHLGLGGVSTFKNS-GMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITL 236
Cdd:PRK10812  160 DRETAGKLLDLGFYISFSGIVTFRNAeQLRDAARYVPLDRLLVETDSPYLAPVPHRGKENQPAMVRDVAEYMAVLKGVSV 239
                         250
                  ....*....|....*..
gi 1376724297 237 EEVENITTINAKSLFNL 253
Cdd:PRK10812  240 EELAQVTTDNFARLFHI 256
PRK11449 PRK11449
metal-dependent hydrolase;
2-253 7.77e-44

metal-dependent hydrolase;


Pssm-ID: 171118 [Multi-domain]  Cd Length: 258  Bit Score: 148.57  E-value: 7.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   2 IDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEVcRSMMGLHPCYVDANIEQTLKTIRAW 81
Cdd:PRK11449    6 IDTHCHFDFPPFSGDEEASLQRAAQAGVGKIIVPATEAENFARVLALAERYQPL-YAALGLHPGMLEKHSDVSLDQLQQA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  82 FDKH--DFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSiEETLALLRKEQDGSLRGVFHCFGSSL 159
Cdd:PRK11449   85 LERRpaKVVAVGEIGLDLFGDDPQFERQQWLLDEQLKLAKRYDLPVILHSRRT-HDKLAMHLKRHDLPRTGVVHGFSGSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 160 EEAQAINELGFHLGLGGVSTF-KNSGMDKVIPHLDMNYVILETDCPYLAPTPNRGKRNEPAYTELVAKRIAELRGITLEE 238
Cdd:PRK11449  164 QQAERFVQLGYKIGVGGTITYpRASKTRDVIAKLPLASLLLETDAPDMPLNGFQGQPNRPEQAARVFDVLCELRPEPADE 243
                         250
                  ....*....|....*
gi 1376724297 239 VENITTINAKSLFNL 253
Cdd:PRK11449  244 IAEVLLNNTYTLFNV 258
PRK10425 PRK10425
3'-5' ssDNA/RNA exonuclease TatD;
1-253 7.16e-43

3'-5' ssDNA/RNA exonuclease TatD;


Pssm-ID: 182449  Cd Length: 258  Bit Score: 145.97  E-value: 7.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDREQVVQRALAQGIDTILLPNIDLESIEPMLATEAQFPEvCRSMMGLHPCYVDANIEQTLKTIRA 80
Cdd:PRK10425    1 MFDIGVNLTSSQFAKDRDDVVARAFAAGVNGMLITGTNLRESQQAQKLARQYPS-CWSTAGVHPHDSSQWQAATEEAIIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  81 WFDKHDFIAVGEIGIDLYWDKTFKAEQEMAFVTQLQWAKELDLPVVIHTRDSIEETLALLRKEQDgSLRG-VFHCFGSSL 159
Cdd:PRK10425   80 LAAQPEVVAIGECGLDFNRNFSTPEEQERAFVAQLAIAAELNMPVFMHCRDAHERFMALLEPWLD-KLPGaVLHCFTGTR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 160 EEAQAINELGFHLGLGGVSTFKNSGMD--KVIPHLDMNYVILETDCPYLAPTPNRGK----RNEPAYTELVAKRIAELRG 233
Cdd:PRK10425  159 EEMQACLARGLYIGITGWVCDERRGLElrELLPLIPAERLLLETDAPYLLPRDLTPKpasrRNEPAFLPHILQRIAHWRG 238
                         250       260
                  ....*....|....*....|
gi 1376724297 234 ITLEEVENITTINAKSLFNL 253
Cdd:PRK10425  239 EDAAWLAATTDANARTLFGL 258
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
2-247 3.36e-10

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: 58.88  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   2 IDTHAHIYASEFD--------------------EDREQVVQRALAQGIDTIL------LPNIDLESIEPML--ATEAQFP 53
Cdd:cd01292     2 IDTHVHLDGSALRgtrlnlelkeaeelspedlyEDTLRALEALLAGGVTTVVdmgstpPPTTTKAAIEAVAeaARASAGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  54 EV--CRSMMGLHPCYVDANIEQTLKTIRAwFDKHDFIAVGEIGidLYWDKTFKAEQEMAfvtQLQWAKELDLPVVIHTRD 131
Cdd:cd01292    82 RVvlGLGIPGVPAAVDEDAEALLLELLRR-GLELGAVGLKLAG--PYTATGLSDESLRR---VLEEARKLGLPVVIHAGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 132 S------IEETLALLRKEqdgsLRGVF-HCFGSSLEEAQAINELGFHLGLGGVSTFKNSGMDKVIPHLD-----MNYVIL 199
Cdd:cd01292   156 LpdptraLEDLVALLRLG----GRVVIgHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGEGAEALRrllelGIRVTL 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1376724297 200 ETDCPYLAPTPnrgkrNEPAYTELVAKRIAelRGITLEEVENITTINA 247
Cdd:cd01292   232 GTDGPPHPLGT-----DLLALLRLLLKVLR--LGLSLEEALRLATINP 272
COG1099 COG1099
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
60-140 1.02e-08

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


Pssm-ID: 440716 [Multi-domain]  Cd Length: 260  Bit Score: 54.46  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  60 MGLHPCYV--DANIEQTLKTIRAWFDKHDFIAVGEIGidlYWDKTfkAEQEMAFVTQLQWAKELDLPVVIHT--RDSIEE 135
Cdd:COG1099    72 LGLNPKEAnnRRLAEEVLELLPRYLDKEGVVAIGEIG---LDDQT--PEEEEVFREQLELARELDLPVLVHTphRDKKEG 146

                  ....*
gi 1376724297 136 TLALL 140
Cdd:COG1099   147 TRRIL 151
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-253 1.51e-07

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 50.75  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYasefdeDREQVVQRALAQGID-TILLPNIDLESIEPMLATE---------AQFPEVCRSMMGLHPCYVDAN 70
Cdd:COG2159     3 IIDVHTHLG------TPEERLADMDEAGIDkAVLSPTPLADPELAALARAandwlaelvARYPDRFIGFATVDPQDPDAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  71 IEQtlktIRAWFDKHDFIAV----GEIGIDL---YWDKTFKAeqemafvtqlqwAKELDLPVVIHTRDSIEETLALLRKE 143
Cdd:COG2159    77 VEE----LERAVEELGFRGVklhpAVGGFPLddpRLDPLYEA------------AAELGLPVLVHPGTPPGPPPGLDLYY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297 144 QD-GSLRGVF-----------HCFGSSLEEA-QAINELG--FHLGLGGVSTFKNsGMDKVIPHLDMNYVILETDCPYLAP 208
Cdd:COG2159   141 AApLILSGVAerfpdlkfilaHGGGPWLPELlGRLLKRLpnVYFDTSGVFPRPE-ALRELLETLGADRILFGSDYPHWDP 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1376724297 209 TPNRgkrnepaytelvaKRIAELRGITLEEVENITTINAKSLFNL 253
Cdd:COG2159   220 PEAL-------------EALEELPGLSEEDREKILGGNAARLLGL 251
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
1-215 1.39e-04

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 42.49  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297   1 MIDTHAHIYASEFDEDR----------EQVVQRALAQGIDTIL-LPNIDLESIEPML-ATEAQF--PEVCRSMMGLHPCY 66
Cdd:pfam01979   6 LIDAHVHLEMGLLRGIPvppefayealRLGITTMLKSGTTTVLdMGATTSTGIEALLeAAEELPlgLRFLGPGCSLDTDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376724297  67 VDANIEQTLKTIRAWFDKHDFIAVG--EIGIDLYWDKTFKAEqEMAFVTQLqwAKELDLPVVIHTRDSIEETLALLRKEQ 144
Cdd:pfam01979  86 ELEGRKALREKLKAGAEFIKGMADGvvFVGLAPHGAPTFSDD-ELKAALEE--AKKYGLPVAIHALETKGEVEDAIAAFG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376724297 145 DGSLRG--VFHCFGS-SLEEAQAINELGFHLGLGGVSTFKNSGMDKVIPHLDMNYVILETDCPYLAPTPNRGKR 215
Cdd:pfam01979 163 GGIEHGthLEVAESGgLLDIIKLILAHGVHLSPTEANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGVK 236
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH