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Conserved domains on  [gi|2462513472|ref|XP_054194649|]
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ERI1 exoribonuclease 3 isoform X2 [Homo sapiens]

Protein Classification

3'-5' exonuclease( domain architecture ID 10150039)

3'-5' exonuclease catalyzes the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction; similar to human ERI1 exoribonuclease 3

CATH:  3.30.420.10
EC:  3.1.-.-
Gene Ontology:  GO:0008408|GO:0003676
PubMed:  11988770|11222749
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 146-281 1.19e-60

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: 190.12  E-value: 1.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 222
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513472 223 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 281
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAK 133
 
Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 146-281 1.19e-60

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: 190.12  E-value: 1.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 222
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513472 223 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 281
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAK 133
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 144-277 3.57e-39

3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 135.37  E-value: 3.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 144 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 220
Cdd:COG5018     2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513472 221 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKK 277
Cdd:COG5018    81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKK 128
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 139-277 1.09e-37

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 140.03  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 139 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 217
Cdd:PTZ00315   51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462513472 218 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKK 277
Cdd:PTZ00315  131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKK 193
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 147-281 5.05e-37

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: 129.01  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 147 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 226
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462513472 227 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKTTAR 281
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKE 129
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 145-270 6.89e-28

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 105.46  E-value: 6.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472  145 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 224
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462513472  225 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFK 270
Cdd:smart00479  75 LEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPK--LPVIDTLK 118
 
Name Accession Description Interval E-value
ERI-1_3'hExo_like cd06133
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ...
 146-281 1.19e-60

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: 190.12  E-value: 1.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 222
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513472 223 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 281
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAK 133
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 144-277 3.57e-39

3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 135.37  E-value: 3.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 144 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 220
Cdd:COG5018     2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513472 221 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKK 277
Cdd:COG5018    81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKK 128
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 139-277 1.09e-37

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 140.03  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 139 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 217
Cdd:PTZ00315   51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462513472 218 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKK 277
Cdd:PTZ00315  131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKK 193
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 147-281 5.05e-37

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: 129.01  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 147 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 226
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462513472 227 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKTTAR 281
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKE 129
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 145-270 6.89e-28

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 105.46  E-value: 6.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472  145 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 224
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462513472  225 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFK 270
Cdd:smart00479  75 LEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPK--LPVIDTLK 118
PRK07748 PRK07748
3'-5' exonuclease KapD;
146-264 5.95e-16

3'-5' exonuclease KapD;


Pssm-ID: 236087  Cd Length: 207  Bit Score: 74.72  E-value: 5.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDKPQIHPQ----EIIEFPILKLNGRtmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVL 221
Cdd:PRK07748    6 FLFLDFEFTMPQHKKKPKgffpEIIEVGLVSVVGC--EVEDTFSSYVKPKTFPSLTERCKSFLGITQEDVDKGISFEELV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462513472 222 ERVDEwmakeglLDPNVKSIFVTCGDWDLKVmLPGQCQYLGLP 264
Cdd:PRK07748   84 EKLAE-------YDKRCKPTIVTWGNMDMKV-LKHNCEKAGVP 118
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 146-228 2.96e-11

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


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 60.93  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDKPQIHpqEIIEFPILKLNGrtMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 225
Cdd:COG2176    10 YVVFDLETTGLSPKKD--EIIEIGAVKVEN--GEIVDRFSTLVNP--GRPIPPFITELTGITDEMVADAPPFEEVLPEFL 83


                  ...
gi 2462513472 226 EWM 228
Cdd:COG2176    84 EFL 86
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 146-229 5.10e-10

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


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 57.11  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 225
Cdd:COG0847     2 FVVLDTETTGLDPAKD--RIIEIGAVKVDDG--RIVETFHTLVNP--ERPIPPEATAIHGITDEDVADAPPFAEVLPELL 75


                  ....
gi 2462513472 226 EWMA 229
Cdd:COG0847    76 EFLG 79
polC PRK00448
DNA polymerase III PolC; Validated
 146-228 1.04e-09

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 59.08  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472  146 FLVLDFEATCDKPQIHpqEIIEFPILKL-NGrtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 224
Cdd:PRK00448   421 YVVFDVETTGLSAVYD--EIIEIGAVKIkNG---EIIDKFEFFIKP--GHPLSAFTTELTGITDDMVKDAPSIEEVLPKF 493


                   ....
gi 2462513472  225 DEWM 228
Cdd:PRK00448   494 KEFC 497
PRK08517 PRK08517
3'-5' exonuclease;
146-223 1.22e-05

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 45.78  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462513472 146 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvhPQLTPFCTELTGIIQAMVDGQPSLQQVLER 223
Cdd:PRK08517   70 FCFVDIETNGSKPKKH--QIIEIGAVKVKNG--EIIDRFESFVKA---KEVPEYITELTGITYEDLENAPSLKEVLEE 140
PRK07740 PRK07740
hypothetical protein; Provisional
 146-223 2.31e-05

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 44.66  E-value: 2.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462513472 146 FLVLDFEATCDKPQiHPQEIIEFPILKLNGRTMEIEsTFHMYVQPVVHPqlTPFCTELTGIIQAMVDGQPSLQQVLER 223
Cdd:PRK07740   61 FVVFDLETTGFSPQ-QGDEILSIGAVKTKGGEVETD-TFYSLVKPKRPI--PEHILELTGITAEDVAFAPPLAEVLHR 134
PRK07883 PRK07883
DEDD exonuclease domain-containing protein;
146-227 4.52e-05

DEDD exonuclease domain-containing protein;


Pssm-ID: 236123 [Multi-domain]  Cd Length: 557  Bit Score: 44.52  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDKPqiHPQEIIEFPILKLNGRtmEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 225
Cdd:PRK07883   17 FVVVDLETTGGSP--AGDAITEIGAVKVRGG--EVLGEFATLVNPGR--PIPPFITVLTGITTAMVAGAPPIEEVLPAFL 90


                  ..
gi 2462513472 226 EW 227
Cdd:PRK07883   91 EF 92
PRK06722 PRK06722
exonuclease; Provisional
 145-253 5.40e-05

exonuclease; Provisional


Pssm-ID: 180670 [Multi-domain]  Cd Length: 281  Bit Score: 43.89  E-value: 5.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 145 YFLVLDFEATCdKP--QIHPQEIIEFPILKLNGRTMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 222
Cdd:PRK06722    6 HFIVFDIERNF-RPykSEDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLIGVEKFPQIIE 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462513472 223 RVDEWMAKEglldpnvkSIFVTCGDWDLKVM 253
Cdd:PRK06722   83 KFIQFIGED--------SIFVTWGKEDYRFL 105
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 146-224 8.87e-05

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 43.79  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 146 FLVLDFEATCDKPQiHPQEIIEFPILKL-NGRTMEIESTFhmyvqpvVHPQ--LTPFCTELTGIIQAMVDGQPSLQQVLE 222
Cdd:PRK08074    5 FVVVDLETTGNSPK-KGDKIIQIAAVVVeDGEILERFSSF-------VNPErpIPPFITELTGISEEMVKQAPLFEDVAP 76


                  ..
gi 2462513472 223 RV 224
Cdd:PRK08074   77 EI 78
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 147-225 3.33e-03

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 38.42  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513472 147 LVLDFEATCDKPQIHpqEIIEFPILK----LNGRTMEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQ----PSLQ 218
Cdd:PRK09182   40 VILDTETTGLDPRKD--EIIEIGMVAfeydDDGRIGDVLDTFGGLQQPSR--PIPPEITRLTGITDEMVAGQtidpAAVD 115


                  ....*..
gi 2462513472 219 QVLERVD 225
Cdd:PRK09182  116 ALIAPAD 122
PRK06807 PRK06807
3'-5' exonuclease;
146-221 3.87e-03

3'-5' exonuclease;


Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 38.26  E-value: 3.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462513472 146 FLVLDFEATCDKPqiHPQEIIEFPILKLngRTMEIESTFHMYVQPVVHpqLTPFCTELTGIIQAMVDGQPSLQQVL 221
Cdd:PRK06807   10 YVVIDFETTGFNP--YNDKIIQVAAVKY--RNHELVDQFVSYVNPERP--IPDRITSLTGITNYRVSDAPTIEEVL 79
 
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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