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Conserved domains on  [gi|499411890|ref|WP_011099357|]
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3'-5' exonuclease [Clostridium tetani]

Protein Classification

3'-5' exonuclease( domain architecture ID 11482424)

3'-5' exonuclease similar to DNA polymerase III subunit epsilon and exodeoxyribonuclease 10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06807 PRK06807
3'-5' exonuclease;
75-380 5.15e-158

3'-5' exonuclease;


:

Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 446.57  E-value: 5.15e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  75 NYSKSVFDEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLP 154
Cdd:PRK06807   1 MGNISLPLDYVVIDFETTGFNPYNDKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 155 ELLKFIKEYPLVAHNASFDIKFLNANLALINR-EIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEdNSHRALPDCI 233
Cdd:PRK06807  81 LFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLpEPKNKVIDTVFLAKKYMKHAPNHKLETLKRMLGIRL-SSHNAFDDCI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 234 TTAEIYLDYCYKANNNLKEFN---ELEKACFKVIKDMLNKNNRDTEFLKLKHTGNYTDIAYFYPLVRIKVGDRKQYFLTN 310
Cdd:PRK06807 160 TCAAVYQKCASIEEEAKRKSNkevLDETAVYEAVKEILVKNKRDIEWIRCMNVGSYLDIKAFYPVMRLKVKGRKKYVLTD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499411890 311 IPLEELKEHET----EKPSKSENFKSRIHLKSEEDLKPFEEYIIQIFDEKKKSFEWYKNNIKSSEIEIVKYLAN 380
Cdd:PRK06807 240 ILEDDVKEICTslkcEPALKSEVGNTRIMLNSLEDVLKLESYILEQYDFVLQALHDYKNNEMNADEKLKEYLNI 313
 
Name Accession Description Interval E-value
PRK06807 PRK06807
3'-5' exonuclease;
75-380 5.15e-158

3'-5' exonuclease;


Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 446.57  E-value: 5.15e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  75 NYSKSVFDEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLP 154
Cdd:PRK06807   1 MGNISLPLDYVVIDFETTGFNPYNDKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 155 ELLKFIKEYPLVAHNASFDIKFLNANLALINR-EIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEdNSHRALPDCI 233
Cdd:PRK06807  81 LFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLpEPKNKVIDTVFLAKKYMKHAPNHKLETLKRMLGIRL-SSHNAFDDCI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 234 TTAEIYLDYCYKANNNLKEFN---ELEKACFKVIKDMLNKNNRDTEFLKLKHTGNYTDIAYFYPLVRIKVGDRKQYFLTN 310
Cdd:PRK06807 160 TCAAVYQKCASIEEEAKRKSNkevLDETAVYEAVKEILVKNKRDIEWIRCMNVGSYLDIKAFYPVMRLKVKGRKKYVLTD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499411890 311 IPLEELKEHET----EKPSKSENFKSRIHLKSEEDLKPFEEYIIQIFDEKKKSFEWYKNNIKSSEIEIVKYLAN 380
Cdd:PRK06807 240 ILEDDVKEICTslkcEPALKSEVGNTRIMLNSLEDVLKLESYILEQYDFVLQALHDYKNNEMNADEKLKEYLNI 313
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 83-240 3.88e-73

DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 225.41  E-value: 3.88e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:COG2176    9 TYVVFDLETTGLSPKKDEIIEIGAVKVENGEIVDRFSTLVNPGRPIPPFITELTGITDEMVADAPPFEEVLPEFLEFLGD 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411890 163 YPLVAHNASFDIKFLNANLALINREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:COG2176   89 AVLVAHNASFDLGFLNAALKRLGLPFDNPVLDTLELARRLLPELKSYKLDTLAERLGIPLEDRHRALGDAEATAELFL 166
DEDDh cd06127
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ...
 85-240 1.07e-59

DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.


Pssm-ID: 176648 [Multi-domain]  Cd Length: 159  Bit Score: 190.20  E-value: 1.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVTDKIIEITAIKYKSG-QIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:cd06127    1 VVFDTETTGLDPKKDRIIEIGAVKVDGGiEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFLGGR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499411890 164 PLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIK-EHLCISEDNSHRALPDCITTAEIYL 240
Cdd:cd06127   81 VLVAHNASFDLRFLNRELRRLGGPpLPNPWIDTLRLARRLLPGLRSHRLGLLLaERYGIPLEGAHRALADALATAELLL 159
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 83-244 3.42e-45

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 153.22  E-value: 3.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890    83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:smart00479   1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFLRG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   163 YPLVAHN-ASFDIKFLNANLAL--INREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISED-NSHRALPDCITTAEI 238
Cdd:smart00479  81 RILVAGNsAHFDLRFLKLEHPRlgIKQPPKLPVIDTLKLARATNPGLPKYSLKKLAKRLLLEVIqRAHRALDDARATAKL 160


                   ....*.
gi 499411890   239 YLDYCY 244
Cdd:smart00479 161 FKKLLE 166
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 85-239 6.92e-30

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 112.83  E-value: 6.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   85 VVIDLETTGLYPVTDKIIEITAIKYKSGQ--IVEKYNTLINPK--INIPKRATEINNITNNMVKDSPVIEDVLPELLKFI 160
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGEneIGETFHTYVKPTrlPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  161 KE-YPLVAHNASFDIKFLNANLALI-NREIKNVA--IDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNS-HRALPDCITT 235
Cdd:pfam00929  81 RKgNLLVAHNASFDVGFLRYDDKRFlKKPMPKLNpvIDTLILDKATYKELPGRSLDALAEKLGLEHIGRaHRALDDARAT 160


                  ....
gi 499411890  236 AEIY 239
Cdd:pfam00929 161 AKLF 164
dinG_rel TIGR01407
DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of ...
 84-240 4.88e-29

DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of proteins in Gram-positive bacteria. The N-terminal region of about 200 amino acids resembles the epsilon subunit of E. coli DNA polymerase III and the homologous region of the Gram-positive type DNA polymerase III alpha subunit. The epsilon subunit contains an exonuclease domain. The remainder of this protein family resembles a predicted ATP-dependent helicase, the DNA damage-inducible protein DinG of E. coli. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273602 [Multi-domain]  Cd Length: 850  Bit Score: 119.14  E-value: 4.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   84 FVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:TIGR01407   2 YAVVDLETTGTQLSFDKIIQIGIVVVEDGEIVDTFHTDVNPNEPIPPFIQELTGISDNMLQQAPYFSQVAQEIYDLLEDG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411890  164 PLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:TIGR01407  82 IFVAHNVHFDLNFLAKALKDCGYEpLPKPRIDTVELAQIFFPTEESYQLSELSEALGLTHENPHRADSDAQATAELLL 159
 
Name Accession Description Interval E-value
PRK06807 PRK06807
3'-5' exonuclease;
75-380 5.15e-158

3'-5' exonuclease;


Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 446.57  E-value: 5.15e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  75 NYSKSVFDEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLP 154
Cdd:PRK06807   1 MGNISLPLDYVVIDFETTGFNPYNDKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 155 ELLKFIKEYPLVAHNASFDIKFLNANLALINR-EIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEdNSHRALPDCI 233
Cdd:PRK06807  81 LFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLpEPKNKVIDTVFLAKKYMKHAPNHKLETLKRMLGIRL-SSHNAFDDCI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 234 TTAEIYLDYCYKANNNLKEFN---ELEKACFKVIKDMLNKNNRDTEFLKLKHTGNYTDIAYFYPLVRIKVGDRKQYFLTN 310
Cdd:PRK06807 160 TCAAVYQKCASIEEEAKRKSNkevLDETAVYEAVKEILVKNKRDIEWIRCMNVGSYLDIKAFYPVMRLKVKGRKKYVLTD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499411890 311 IPLEELKEHET----EKPSKSENFKSRIHLKSEEDLKPFEEYIIQIFDEKKKSFEWYKNNIKSSEIEIVKYLAN 380
Cdd:PRK06807 240 ILEDDVKEICTslkcEPALKSEVGNTRIMLNSLEDVLKLESYILEQYDFVLQALHDYKNNEMNADEKLKEYLNI 313
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 83-240 3.88e-73

DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 225.41  E-value: 3.88e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:COG2176    9 TYVVFDLETTGLSPKKDEIIEIGAVKVENGEIVDRFSTLVNPGRPIPPFITELTGITDEMVADAPPFEEVLPEFLEFLGD 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411890 163 YPLVAHNASFDIKFLNANLALINREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:COG2176   89 AVLVAHNASFDLGFLNAALKRLGLPFDNPVLDTLELARRLLPELKSYKLDTLAERLGIPLEDRHRALGDAEATAELFL 166
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 83-240 1.62e-61

DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 195.01  E-value: 1.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:COG0847    1 RFVVLDTETTGLDPAKDRIIEIGAVKVDDGRIVETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEFLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499411890 163 YPLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:COG0847   81 AVLVAHNAAFDLGFLNAELRRAGLPlPPFPVLDTLRLARRLLPGLPSYSLDALCERLGIPFDERHRALADAEATAELFL 159
DEDDh cd06127
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ...
 85-240 1.07e-59

DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.


Pssm-ID: 176648 [Multi-domain]  Cd Length: 159  Bit Score: 190.20  E-value: 1.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVTDKIIEITAIKYKSG-QIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:cd06127    1 VVFDTETTGLDPKKDRIIEIGAVKVDGGiEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFLGGR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499411890 164 PLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIK-EHLCISEDNSHRALPDCITTAEIYL 240
Cdd:cd06127   81 VLVAHNASFDLRFLNRELRRLGGPpLPNPWIDTLRLARRLLPGLRSHRLGLLLaERYGIPLEGAHRALADALATAELLL 159
polC PRK00448
DNA polymerase III PolC; Validated
 82-258 2.83e-49

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 178.49  E-value: 2.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   82 DEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIK 161
Cdd:PRK00448  419 ATYVVFDVETTGLSAVYDEIIEIGAVKIKNGEIIDKFEFFIKPGHPLSAFTTELTGITDDMVKDAPSIEEVLPKFKEFCG 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  162 EYPLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:PRK00448  499 DSILVAHNASFDVGFINTNYEKLGLEkIKNPVIDTLELSRFLYPELKSHRLNTLAKKFGVELEHHHRADYDAEATAYLLI 578

                         170
                  ....*....|....*....
gi 499411890  241 DYCYKAN-NNLKEFNELEK 258
Cdd:PRK00448  579 KFLKDLKeKGITNLDELNK 597
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 83-244 3.42e-45

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 153.22  E-value: 3.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890    83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:smart00479   1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFLRG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   163 YPLVAHN-ASFDIKFLNANLAL--INREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISED-NSHRALPDCITTAEI 238
Cdd:smart00479  81 RILVAGNsAHFDLRFLKLEHPRlgIKQPPKLPVIDTLKLARATNPGLPKYSLKKLAKRLLLEVIqRAHRALDDARATAKL 160


                   ....*.
gi 499411890   239 YLDYCY 244
Cdd:smart00479 161 FKKLLE 166
PRK07883 PRK07883
DEDD exonuclease domain-containing protein;
84-238 5.50e-40

DEDD exonuclease domain-containing protein;


Pssm-ID: 236123 [Multi-domain]  Cd Length: 557  Bit Score: 148.91  E-value: 5.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:PRK07883  17 FVVVDLETTGGSPAGDAITEIGAVKVRGGEVLGEFATLVNPGRPIPPFITVLTGITTAMVAGAPPIEEVLPAFLEFARGA 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411890 164 PLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTF--LPNHKLTTIKEHLCISEDNSHRALPDCITTAEI 238
Cdd:PRK07883  97 VLVAHNAPFDIGFLRAAAARCGYPwPGPPVLCTVRLARRVLPRdeAPNVRLSTLARLFGATTTPTHRALDDARATVDV 174
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 82-240 1.35e-38

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 147.02  E-value: 1.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  82 DEFVVIDLETTGLYPVT-DKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFI 160
Cdd:PRK08074   3 KRFVVVDLETTGNSPKKgDKIIQIAAVVVEDGEILERFSSFVNPERPIPPFITELTGISEEMVKQAPLFEDVAPEIVELL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 161 KEYPLVAHNASFDIKFLNANLALIN-REIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIY 239
Cdd:PRK08074  83 EGAYFVAHNVHFDLNFLNEELERAGyTEIHCPKLDTVELARILLPTAESYKLRDLSEELGLEHDQPHRADSDAEVTAELF 162


                 .
gi 499411890 240 L 240
Cdd:PRK08074 163 L 163
DNA_pol_III_epsilon_like cd06130
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with ...
 84-241 4.47e-32

an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III; This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.


Pssm-ID: 99834 [Multi-domain]  Cd Length: 156  Bit Score: 118.38  E-value: 4.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPvtDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:cd06130    1 FVAIDFETANADR--ASACSIGLVKVRDGQIVDTFYTLIRPPTRFDPFNIAIHGITPEDVADAPTFPEVWPEIKPFLGGS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499411890 164 PLVAHNASFDIKFLNANLALINREIKNV-AIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNsHRALPDCITTAEIYLD 241
Cdd:cd06130   79 LVVAHNASFDRSVLRAALEAYGLPPPPYqYLCTVRLARRVWPLLPNHKLNTVAEHLGIELNH-HDALEDARACAEILLA 156
DNA_pol_III_epsilon_Ecoli_like cd06131
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III ...
 85-240 1.73e-31

DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III and similar proteins; This subfamily is composed of the epsilon subunit of Escherichia coli DNA polymerase III (Pol III) and similar proteins. Pol III is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. It is a holoenzyme complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.


Pssm-ID: 99835 [Multi-domain]  Cd Length: 167  Bit Score: 117.25  E-value: 1.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVT-DKIIEITAIKYKSGQIVEK-YNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:cd06131    2 IVLDTETTGLDPREgHRIIEIGCVELINRRLTGNtFHVYINPERDIPEEAFKVHGITDEFLADKPKFAEIADEFLDFIRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 163 YPLVAHNASFDIKFLNANLALI--NREIKNVA--IDTLQLSRAMYTFLPNhKLttikEHLC----IseDNSHR----ALP 230
Cdd:cd06131   82 AELVIHNASFDVGFLNAELSLLglGKKIIDFCrvIDTLALARKKFPGKPN-SL----DALCkrfgI--DNSHRtlhgALL 154

                        170
                 ....*....|
gi 499411890 231 DCITTAEIYL 240
Cdd:cd06131  155 DAELLAEVYL 164
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 85-239 6.92e-30

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 112.83  E-value: 6.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   85 VVIDLETTGLYPVTDKIIEITAIKYKSGQ--IVEKYNTLINPK--INIPKRATEINNITNNMVKDSPVIEDVLPELLKFI 160
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGEneIGETFHTYVKPTrlPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  161 KE-YPLVAHNASFDIKFLNANLALI-NREIKNVA--IDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNS-HRALPDCITT 235
Cdd:pfam00929  81 RKgNLLVAHNASFDVGFLRYDDKRFlKKPMPKLNpvIDTLILDKATYKELPGRSLDALAEKLGLEHIGRaHRALDDARAT 160


                  ....
gi 499411890  236 AEIY 239
Cdd:pfam00929 161 AKLF 164
dinG_rel TIGR01407
DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of ...
 84-240 4.88e-29

DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of proteins in Gram-positive bacteria. The N-terminal region of about 200 amino acids resembles the epsilon subunit of E. coli DNA polymerase III and the homologous region of the Gram-positive type DNA polymerase III alpha subunit. The epsilon subunit contains an exonuclease domain. The remainder of this protein family resembles a predicted ATP-dependent helicase, the DNA damage-inducible protein DinG of E. coli. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273602 [Multi-domain]  Cd Length: 850  Bit Score: 119.14  E-value: 4.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   84 FVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:TIGR01407   2 YAVVDLETTGTQLSFDKIIQIGIVVVEDGEIVDTFHTDVNPNEPIPPFIQELTGISDNMLQQAPYFSQVAQEIYDLLEDG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411890  164 PLVAHNASFDIKFLNANLALINRE-IKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:TIGR01407  82 IFVAHNVHFDLNFLAKALKDCGYEpLPKPRIDTVELAQIFFPTEESYQLSELSEALGLTHENPHRADSDAQATAELLL 159
PRK08517 PRK08517
3'-5' exonuclease;
83-245 5.56e-28

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 110.50  E-value: 5.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKiNIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:PRK08517  69 VFCFVDIETNGSKPKKHQIIEIGAVKVKNGEIIDRFESFVKAK-EVPEYITELTGITYEDLENAPSLKEVLEEFRLFLGD 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 163 YPLVAHNASFDIKFLNANLALINR-EIKNVAIDTLQLSRAmyTFL-PNHKLTTIKEHLCISEDNSHRALPDCITTAEIyL 240
Cdd:PRK08517 148 SVFVAHNVNFDYNFISRSLEEIGLgPLLNRKLCTIDLAKR--TIEsPRYGLSFLKELLGIEIEVHHRAYADALAAYEI-F 224


                 ....*
gi 499411890 241 DYCYK 245
Cdd:PRK08517 225 KICLL 229
PRK06310 PRK06310
DNA polymerase III subunit epsilon; Validated
 83-256 2.87e-27

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180525 [Multi-domain]  Cd Length: 250  Bit Score: 108.38  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:PRK06310   8 EFVCLDCETTGLDVKKDRIIEFAAIRFTFDEVIDSVEFLINPERVVSAESQRIHHISDAMLRDKPKIAEVFPQIKGFFKE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 163 YP-LVAHNASFDIKFLNANLALINREI---KNVAIDTLQLSRaMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEI 238
Cdd:PRK06310  88 GDyIVGHSVGFDLQVLSQESERIGETFlskHYYIIDTLRLAK-EYGDSPNNSLEALAVHFNVPYDGNHRAMKDVEINIKV 166

                        170
                 ....*....|....*...
gi 499411890 239 YLDYCyKANNNLKEFNEL 256
Cdd:PRK06310 167 FKHLC-KRFRTLEQLKQI 183
PRK05711 PRK05711
DNA polymerase III subunit epsilon; Provisional
 85-240 1.73e-26

DNA polymerase III subunit epsilon; Provisional


Pssm-ID: 235574 [Multi-domain]  Cd Length: 240  Bit Score: 105.71  E-value: 1.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVT-DKIIEITAIkyksgQIVEKY---NTL---INPKINIPKRATEINNITNNMVKDSPVIEDVLPELL 157
Cdd:PRK05711   7 IVLDTETTGLNQREgHRIIEIGAV-----ELINRRltgRNFhvyIKPDRLVDPEALAVHGITDEFLADKPTFAEVADEFL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 158 KFIKEYPLVAHNASFDIKFLNANLALINREIKNVA-----IDTLQLSRAMYTFLPNhKLttikEHLC----IseDNSHR- 227
Cdd:PRK05711  82 DFIRGAELIIHNAPFDIGFMDYEFALLGRDIPKTNtfckvTDTLAMARRMFPGKRN-SL----DALCkrygI--DNSHRt 154

                        170
                 ....*....|....*.
gi 499411890 228 ---ALPDCITTAEIYL 240
Cdd:PRK05711 155 lhgALLDAEILAEVYL 170
dnaq TIGR00573
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ...
 80-241 2.92e-25

exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, Degradation of DNA]


Pssm-ID: 129663 [Multi-domain]  Cd Length: 217  Bit Score: 101.76  E-value: 2.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   80 VFDEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKF 159
Cdd:TIGR00573   5 VLDTETTGDNETTGLYAGHDIIEIGAVEIINRRITGNKFHTYIKPDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  160 IKEYPLVAHNASFDIKFLNANLALINREI--KNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAE 237
Cdd:TIGR00573  85 IRGAELVIHNASFDVGFLNYEFSKLYKVEpkTNDVIDTTDTLQYARPEFPGKRNTLDALCKRYEITNSHRALHGALADAF 164


                  ....
gi 499411890  238 IYLD 241
Cdd:TIGR00573 165 ILAK 168
PRK07740 PRK07740
hypothetical protein; Provisional
 83-242 3.54e-22

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 93.97  E-value: 3.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVT-DKIIEITAIKYKSGQIV-EKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFI 160
Cdd:PRK07740  60 PFVVFDLETTGFSPQQgDEILSIGAVKTKGGEVEtDTFYSLVKPKRPIPEHILELTGITAEDVAFAPPLAEVLHRFYAFI 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 161 KEYPLVAHNASFDIKFLNANLAlinREIKNV----AIDTLQLSRAMYtflPNHKLTTIKEhLCISED----NSHRALPDC 232
Cdd:PRK07740 140 GAGVLVAHHAGHDKAFLRHALW---RTYRQPfthrLIDTMFLTKLLA---HERDFPTLDD-ALAYYGipipRRHHALGDA 212

                        170
                 ....*....|
gi 499411890 233 ITTAEIYLDY 242
Cdd:PRK07740 213 LMTAKLWAIL 222
PRK09145 PRK09145
3'-5' exonuclease;
82-240 4.73e-22

3'-5' exonuclease;


Pssm-ID: 236391 [Multi-domain]  Cd Length: 202  Bit Score: 92.66  E-value: 4.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  82 DEFVVIDLETTGLYPVTDKIIEITAIKYKSGQIV--EKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKF 159
Cdd:PRK09145  29 DEWVALDCETTGLDPRRAEIVSIAAVKIRGNRILtsERLELLVRPPQSLSAESIKIHRLRHQDLEDGLSEEEALRQLLAF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 160 IKEYPLVAHNASFDIKFLN-ANLALINREIKNVAIDTLQL-SRAMYTFLPNHK----LTTIKEHLCISEDNSHRALPDCI 233
Cdd:PRK09145 109 IGNRPLVGYYLEFDVAMLNrYVRPLLGIPLPNPLIEVSALyYDKKERHLPDAYidlrFDAILKHLDLPVLGRHDALNDAI 188


                 ....*..
gi 499411890 234 TTAEIYL 240
Cdd:PRK09145 189 MAALIFL 195
PRK06063 PRK06063
DEDDh family exonuclease;
84-238 4.21e-21

DEDDh family exonuclease;


Pssm-ID: 180377 [Multi-domain]  Cd Length: 313  Bit Score: 92.46  E-value: 4.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPVTDKIIEITAIKYKS-GQIVEKYNTLINPKINiPKrATEINNITNNMVKDSPVIEDVLPELLKFIKE 162
Cdd:PRK06063  17 WAVVDVETSGFRPGQARIISLAVLGLDAdGNVEQSVVTLLNPGVD-PG-PTHVHGLTAEMLEGQPQFADIAGEVAELLRG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 163 YPLVAHNASFDIKFLNANLALINREIknvAID----TLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEI 238
Cdd:PRK06063  95 RTLVAHNVAFDYSFLAAEAERAGAEL---PVDqvmcTVELARRLGLGLPNLRLETLAAHWGVPQQRPHDALDDARVLAGI 171
PRK06309 PRK06309
DNA polymerase III subunit epsilon; Validated
 88-234 5.23e-20

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180524 [Multi-domain]  Cd Length: 232  Bit Score: 87.94  E-value: 5.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  88 DLETTGLYPVTDKIIEITAIKYKSGqivEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFI-KEYPLV 166
Cdd:PRK06309   8 DTETTGTQIDKDRIIEIAAYNGVTS---ESFQTLVNPEIPIPAEASKIHGITTDEVADAPKFPEAYQKFIEFCgTDNILV 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499411890 167 AHNA-SFDIKFLNANL---ALINREIKnvAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCIT 234
Cdd:PRK06309  85 AHNNdAFDFPLLRKECrrhGLEPPTLR--TIDSLKWAQKYRPDLPKHNLQYLRQVYGFEENQAHRALDDVIT 154
PRK07983 PRK07983
exodeoxyribonuclease X; Provisional
 84-241 3.52e-18

exodeoxyribonuclease X; Provisional


Pssm-ID: 181186 [Multi-domain]  Cd Length: 219  Bit Score: 82.46  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLypvTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPellKFIKEY 163
Cdd:PRK07983   2 LRVIDTETCGL---QGGIVEIASVDVIDGKIVNPMSHLVRPDRPISPQAMAIHRITEAMVADKPWIEDVIP---HYYGSE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 164 PLVAHNASFDIKFLNanlalinrEIKNVAIDTLQLSRAMYtflPNHKLT------TIKEHLCISED-NSHRALPDCITTA 236
Cdd:PRK07983  76 WYVAHNASFDRRVLP--------EMPGEWICTMKLARRLW---PGIKYSnmalykSRKLNVQTPPGlHHHRALYDCYITA 144


                 ....*
gi 499411890 237 EIYLD 241
Cdd:PRK07983 145 ALLID 149
PRK06195 PRK06195
DNA polymerase III subunit epsilon; Validated
 84-258 1.68e-17

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 235735 [Multi-domain]  Cd Length: 309  Bit Score: 82.14  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGlyPVTDKIIEITAIKYKSGQIVEKYNTLINPK------INIpkratEINNITNNMVKDSPVIEDVLPELL 157
Cdd:PRK06195   3 FVAIDFETAN--EKRNSPCSIGIVVVKDGEIVEKVHYLIKPKemrfmpINI-----GIHGIRPHMVEDELEFDKIWEKIK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 158 KFIKEYPLVAHNASFDIKFLNANLALINREIKNVA-IDTLQLSRAMYTFLPNHKLTTIKEHLCIsEDNSHRALPDCITTA 236
Cdd:PRK06195  76 HYFNNNLVIAHNASFDISVLRKTLELYNIPMPSFEyICTMKLAKNFYSNIDNARLNTVNNFLGY-EFKHHDALADAMACS 154

                        170       180
                 ....*....|....*....|..
gi 499411890 237 EIYLDYCykANNNLKEFNELEK 258
Cdd:PRK06195 155 NILLNIS--KELNSKDINEISK 174
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 85-179 8.17e-16

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 76.94  E-value: 8.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVTDKIIEITAIKY---KSGQI---VEKYNTLINPKINIPKRATEINNITNNMVKDSpVIEDvlPELLK 158
Cdd:PRK09182  40 VILDTETTGLDPRKDEIIEIGMVAFeydDDGRIgdvLDTFGGLQQPSRPIPPEITRLTGITDEMVAGQ-TIDP--AAVDA 116

                         90       100
                 ....*....|....*....|..
gi 499411890 159 FIKEYPLV-AHNASFDIKFLNA 179
Cdd:PRK09182 117 LIAPADLIiAHNAGFDRPFLER 138
PRK07246 PRK07246
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 84-240 1.21e-13

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180905 [Multi-domain]  Cd Length: 820  Bit Score: 72.41  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPvTDKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIKEY 163
Cdd:PRK07246   9 YAVVDLEATGAGP-NASIIQVGIVIIEGGEIIDSYTTDVNPHEPLDEHIKHLTGITDQQLAQAPDFSQVARHIYDLIEDC 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499411890 164 PLVAHNASFDIKFLNANLALINREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISEDNSHRALPDCITTAEIYL 240
Cdd:PRK07246  88 IFVAHNVKFDANLLAEALFLEGYELRTPRVDTVELAQVFFPTLEKYSLSHLSRELNIDLADAHTAIADARATAELFL 164
PRK07942 PRK07942
DNA polymerase III subunit epsilon; Provisional
 88-238 2.52e-13

DNA polymerase III subunit epsilon; Provisional


Pssm-ID: 181176 [Multi-domain]  Cd Length: 232  Bit Score: 68.85  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  88 DLETTGLYPVTDKI-----IEITAikykSGQIVEKYNTLINPKINIPKRATEINNITNNMV-KDSPVIEDVLPELLKFIK 161
Cdd:PRK07942  12 DLETTGVDPETARIvtaalVVVDA----DGEVVESREWLADPGVEIPEEASAVHGITTEYArAHGRPAAEVLAEIADALR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 162 EY-----PLVAHNASFDIKFLNANLALINREIKNVA--IDTLQLSRAMYTFLP-NHKLTTIKEHLCISEDNSHRALPDCI 233
Cdd:PRK07942  88 EAwargvPVVVFNAPYDLTVLDRELRRHGLPSLVPGpvIDPYVIDKAVDRYRKgKRTLTALCEHYGVRLDNAHEATADAL 167


                 ....*
gi 499411890 234 TTAEI 238
Cdd:PRK07942 168 AAARV 172
RNaseT cd06134
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' ...
 85-247 5.79e-12

DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site.


Pssm-ID: 99837 [Multi-domain]  Cd Length: 189  Bit Score: 63.85  E-value: 5.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVTDKIIEITAIKY---KSG--QIVEKYNTLINP--KINIPKRATEINNITNN----MVKDSpviEDVL 153
Cdd:cd06134    8 VVVDVETGGFNPQTDALLEIAAVTLemdEQGnlYPDETFHFHILPfeGANLDPAALEFNGIDPFhpfrFAVDE---KEAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 154 PELLKFIKEYP---------LVAHNASFDIKFLNanlALINR-EIKN------VAIDTLQLSRAMYTflpnhklTTIKEH 217
Cdd:cd06134   85 KEIFKPIRKALkaqgctraiLVGHNAHFDLGFLN---AAVARcKIKRnpfhpfSTFDTATLAGLAYG-------QTVLAK 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499411890 218 LC----ISEDNS--HRALPDCITTAEIyldYCYKAN 247
Cdd:cd06134  155 ACqaagIEFDNKeaHSALYDTQKTAEL---FCKIVN 187
PRK09146 PRK09146
DNA polymerase III subunit epsilon; Validated
 83-237 8.12e-11

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236392 [Multi-domain]  Cd Length: 239  Bit Score: 61.48  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  83 EFVVIDLETTGLYPVTDKIIEITAIKYKSGQIV--EKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFI 160
Cdd:PRK09146  48 PFVALDFETTGLDAEQDAIVSIGLVPFTLQRIRcrQARHWVVKPRRPLEEESVVIHGITHSELQDAPDLERILDELLEAL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 161 KEYPLVAHNASFDIKFLNANL-ALINREIKNVAIDTLQL--------SRAMYTFLPNHKLTTIKEHLCISEDN-----SH 226
Cdd:PRK09146 128 AGKVVVVHYRRIERDFLDQALrNRIGEGIEFPVIDTMEIeariqrkqAGGLWNRLKGKKPESIRLADSRLRYGlpaysPH 207

                        170
                 ....*....|.
gi 499411890 227 RALPDCITTAE 237
Cdd:PRK09146 208 HALTDAIATAE 218
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 84-238 6.49e-10

DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.


Pssm-ID: 99836 [Multi-domain]  Cd Length: 176  Bit Score: 57.62  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPVTDK-----IIEITAIKY--KSGQIVEKYNTLINPKIN--IPKRATEINNITNNMVKDSPVIEDVLP 154
Cdd:cd06133    1 YLVIDFEATCWEGNSKPdypneIIEIGAVLVdvKTKEIIDTFSSYVKPVINpkLSDFCTELTGITQEDVDNAPSFPEVLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 155 ELLKFIKEYPLVAhNASF---DIKFLNANLALINR----EIKNVAIDtlqLSRAMYTFLPNHKLTTIK---EHLCISEDN 224
Cdd:cd06133   81 EFLEWLGKNGKYA-FVTWgdwDLKDLLQNQCKYKIinlpPFFRQWID---LKKEFAKFYGLKKRTGLSkalEYLGLEFEG 156

                        170
                 ....*....|....*
gi 499411890 225 S-HRALPDCITTAEI 238
Cdd:cd06133  157 RhHRGLDDARNIARI 171
TREX1_2 cd06136
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar ...
 84-242 7.32e-10

DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins; Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture.


Pssm-ID: 99839 [Multi-domain]  Cd Length: 177  Bit Score: 57.73  E-value: 7.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYP-VTDKIIEITAI-------------KYKSGQIVEKYNTLINPKINIPKRATEINNITN-NMVKDSPV 148
Cdd:cd06136    1 FVFLDLETTGLPKhNRPEITELCLVavhrdhllntsrdKPALPRVLDKLSLCFNPGRAISPGASEITGLSNdLLEHKAPF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 149 IEDVLPELLKFIKEYP----LVAHNAS-FDIKFLNANLALINREIKN--VAIDTLQLSRAMYTFLPN-HKLTTIKEHLci 220
Cdd:cd06136   81 DSDTANLIKLFLRRQPkpicLVAHNGNrFDFPILRSELERLGTKLPDdiLCVDSLPAFRELDQSLGSlYKRLFGQEPK-- 158

                        170       180
                 ....*....|....*....|..
gi 499411890 221 sedNSHRALPDCITTAEIYLDY 242
Cdd:cd06136  159 ---NSHTAEGDVLALLKCALHK 177
PRK07247 PRK07247
3'-5' exonuclease;
82-239 1.12e-09

3'-5' exonuclease;


Pssm-ID: 180906 [Multi-domain]  Cd Length: 195  Bit Score: 57.48  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  82 DEFVVIDLETTGLYPVTdKIIEITAIKYKSGQIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLKFIK 161
Cdd:PRK07247   5 ETYIAFDLEFNTVNGVS-HIIQVSAVKYDDHKEVDSFDSYVYTDVPLQSFINGLTGITADKIADAPKVEEVLAAFKEFVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 162 EYPLVAHNA-SFDIKFLNAN-LALINREIKNVAIDTLQLSRAMYTFLPNHKLTTIKEHLCISeDNSHRALPDCITTAEIY 239
Cdd:PRK07247  84 ELPLIGYNAqKSDLPILAENgLDLSDQYQVDLYDEAFERRSSDLNGIANLKLQTVADFLGIK-GRGHNSLEDARMTARVY 162
PRK06722 PRK06722
exonuclease; Provisional
 84-281 1.25e-04

exonuclease; Provisional


Pssm-ID: 180670 [Multi-domain]  Cd Length: 281  Bit Score: 43.50  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETT-GLYPVTD--KIIEITAIKYKSG--QIVEKYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLPELLK 158
Cdd:PRK06722   7 FIVFDIERNfRPYKSEDpsEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLIGVEKFPQIIEKFIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 159 FIKEYPLVAHNASFDIKFLNANLALINREI----KNVAIDTLQLSRAMYTFLPNH--KLTTIKEHLCIS-EDNSHRALPD 231
Cdd:PRK06722  87 FIGEDSIFVTWGKEDYRFLSHDCTLHSVECpcmeKERRIDLQKFVFQAYEELFEHtpSLQSAVEQLGLIwEGKQHRALAD 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499411890 232 CITTAEIYLD-YCYK-ANNNLKEFNELEkacfkvikdmLNKNNRDTEFLKLK 281
Cdd:PRK06722 167 AENTANILLKaYSERdITKRYKRHGELE----------LVKNGKLTEKAKKK 208
DEDDh_RNase cd06137
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX) ...
 85-240 1.94e-04

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX)-1,-3, and -4, ISG20, and similar proteins; This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p), REX4 (or Rex4p), ISG20, and similar proteins. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. REX proteins are required for the processing and maturation of many RNA species, and ISG20 is an interferon-induced antiviral exonuclease with a strong preference for single-stranded RNA.


Pssm-ID: 99840  Cd Length: 161  Bit Score: 41.50  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  85 VVIDLETTGLYPVTDKIIEITAIKYKSGQIVekYNTLINPKINIPKRATEINNITNNMVKDSPVIEDVLP-------ELL 157
Cdd:cd06137    1 VALDCEMVGLADGDSEVVRISAVDVLTGEVL--IDSLVRPSVRVTDWRTRFSGVTPADLEEAAKAGKTIFgweaaraALW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890 158 KFI-KEYPLVAHNASFDIKFLnanlalinREIKNVAIDTLQLSRAMYTFlPNHKLTTIKEHLC-------ISED-NSHRA 228
Cdd:cd06137   79 KFIdPDTILVGHSLQNDLDAL--------RMIHTRVVDTAILTREAVKG-PLAKRQWSLRTLCrdflglkIQGGgEGHDS 149

                        170
                 ....*....|..
gi 499411890 229 LPDCITTAEIYL 240
Cdd:cd06137  150 LEDALAAREVVL 161
Orn COG1949
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
87-107 4.91e-04

Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];


Pssm-ID: 441552  Cd Length: 177  Bit Score: 40.48  E-value: 4.91e-04
                         10        20
                 ....*....|....*....|.
gi 499411890  87 IDLETTGLYPVTDKIIEITAI 107
Cdd:COG1949    7 IDLEMTGLDPETDRIIEIATI 27
PRK05359 PRK05359
oligoribonuclease; Provisional
 82-107 6.16e-04

oligoribonuclease; Provisional


Pssm-ID: 235429  Cd Length: 181  Bit Score: 40.14  E-value: 6.16e-04
                         10        20
                 ....*....|....*....|....*.
gi 499411890  82 DEFVVIDLETTGLYPVTDKIIEITAI 107
Cdd:PRK05359   3 DNLIWIDLEMTGLDPERDRIIEIATI 28
Orn cd06135
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ...
 84-177 1.01e-03

DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Orn is essential for Escherichia coli survival. The human homolog, also called Sfn (small fragment nuclease), is able to hydrolyze short single-stranded RNA and DNA oligomers. It plays a role in cellular nucleotide recycling.


Pssm-ID: 99838 [Multi-domain]  Cd Length: 173  Bit Score: 39.45  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890  84 FVVIDLETTGLYPVTDKIIEITAI--KYKSGQIVEKYNTLINPkiniPKRATE------INNITNN----MVKDSPV-IE 150
Cdd:cd06135    1 LVWIDLEMTGLDPEKDRILEIACIitDGDLNIIAEGPELVIHQ----PDEVLDgmdewcTEMHTKSglteRVRASTVtLA 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499411890 151 DVLPELLKFIKEY------PLVAHNASFDIKFL 177
Cdd:cd06135   77 QAEAELLEFIKKYvpkgksPLAGNSVHQDRRFL 109
UvrD_C pfam13361
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 49-137 1.48e-03

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 433145 [Multi-domain]  Cd Length: 377  Bit Score: 40.47  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411890   49 DKGREETSDLSSDEYYKKLCGRDKHINYSKSvfDEFVVIDLETTGLYPVTDKIIEITAIKY-KSGQIVEKYNTLINPKIN 127
Cdd:pfam13361 155 REYKKRGLRLSDFINPDTLTYGDPFVIALEQ--DNIVVFDVETTGLDTTEDEIIQIAAIKLnKKGVVIESFERFLRLKKP 232

                          90
                  ....*....|
gi 499411890  128 IPKRATEINN 137
Cdd:pfam13361 233 VGDSLQVHGF 242
 
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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