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Conserved domains on  [gi|678246462|ref|NP_001288629|]
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ERI1 exoribonuclease 3 isoform 3 [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 ...
 68-203 8.69e-62

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: 8.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133    1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 678246462 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 203
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 ...
 68-203 8.69e-62

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: 8.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133    1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 678246462 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 203
Cdd:cd06133   81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAK 133
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 66-199 3.46e-40

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: 3.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  66 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 142
Cdd:COG5018    2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 678246462 143 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKK 199
Cdd:COG5018   81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKK 128
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 61-199 1.42e-39

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 142.34  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  61 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 139
Cdd:PTZ00315  51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 678246462 140 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKK 199
Cdd:PTZ00315 131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKK 193
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 69-203 5.18e-38

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: 5.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462   69 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 148
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 678246462  149 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKTTAR 203
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKE 129
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 67-192 9.26e-29

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: 9.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462    67 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 678246462   147 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFK 192
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 ...
 68-203 8.69e-62

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: 8.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133    1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 678246462 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKTTAR 203
Cdd:cd06133   81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAK 133
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 66-199 3.46e-40

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: 3.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  66 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 142
Cdd:COG5018    2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 678246462 143 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKK 199
Cdd:COG5018   81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKK 128
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 61-199 1.42e-39

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 142.34  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  61 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 139
Cdd:PTZ00315  51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 678246462 140 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKK 199
Cdd:PTZ00315 131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKK 193
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 69-203 5.18e-38

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: 5.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462   69 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 148
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 678246462  149 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKTTAR 203
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKE 129
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 67-192 9.26e-29

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: 9.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462    67 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 678246462   147 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFK 192
Cdd:smart00479  75 LEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPK--LPVIDTLK 118
PRK07748 PRK07748
3'-5' exonuclease KapD;
68-186 1.42e-16

3'-5' exonuclease KapD;


Pssm-ID: 236087  Cd Length: 207  Bit Score: 74.72  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDKPQIHPQ----EIIEFPILKLNGRtmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVL 143
Cdd:PRK07748   6 FLFLDFEFTMPQHKKKPKgffpEIIEVGLVSVVGC--EVEDTFSSYVKPKTFPSLTERCKSFLGITQEDVDKGISFEELV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 678246462 144 ERVDEwmakeglLDPNVKSIFVTCGDWDLKVmLPGQCQYLGLP 186
Cdd:PRK07748  84 EKLAE-------YDKRCKPTIVTWGNMDMKV-LKHNCEKAGVP 118
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 68-150 1.01e-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: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGrtMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:COG2176   10 YVVFDLETTGLSPKKD--EIIEIGAVKVEN--GEIVDRFSTLVNP--GRPIPPFITELTGITDEMVADAPPFEEVLPEFL 83


                 ...
gi 678246462 148 EWM 150
Cdd:COG2176   84 EFL 86
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 68-151 2.01e-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: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:COG0847    2 FVVLDTETTGLDPAKD--RIIEIGAVKVDDG--RIVETFHTLVNP--ERPIPPEATAIHGITDEDVADAPPFAEVLPELL 75


                 ....
gi 678246462 148 EWMA 151
Cdd:COG0847   76 EFLG 79
polC PRK00448
DNA polymerase III PolC; Validated
 68-150 2.75e-10

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 59.08  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462   68 FLVLDFEATCDKPQIHpqEIIEFPILKL-NGrtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:PRK00448  421 YVVFDVETTGLSAVYD--EIIEIGAVKIkNG---EIIDKFEFFIKP--GHPLSAFTTELTGITDDMVKDAPSIEEVLPKF 493


                  ....
gi 678246462  147 DEWM 150
Cdd:PRK00448  494 KEFC 497
PRK08517 PRK08517
3'-5' exonuclease;
68-145 5.78e-06

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 45.78  E-value: 5.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678246462  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvhPQLTPFCTELTGIIQAMVDGQPSLQQVLER 145
Cdd:PRK08517  70 FCFVDIETNGSKPKKH--QIIEIGAVKVKNG--EIIDRFESFVKA---KEVPEYITELTGITYEDLENAPSLKEVLEE 140
PRK07883 PRK07883
DEDD exonuclease domain-containing protein;
68-149 6.08e-06

DEDD exonuclease domain-containing protein;


Pssm-ID: 236123 [Multi-domain]  Cd Length: 557  Bit Score: 46.06  E-value: 6.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDKPqiHPQEIIEFPILKLNGRtmEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:PRK07883  17 FVVVDLETTGGSP--AGDAITEIGAVKVRGG--EVLGEFATLVNPGR--PIPPFITVLTGITTAMVAGAPPIEEVLPAFL 90


                 ..
gi 678246462 148 EW 149
Cdd:PRK07883  91 EF 92
PRK07740 PRK07740
hypothetical protein; Provisional
 68-145 1.44e-05

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 44.27  E-value: 1.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678246462  68 FLVLDFEATCDKPQiHPQEIIEFPILKLNGRTMEiESTFHMYVQPVVHPqlTPFCTELTGIIQAMVDGQPSLQQVLER 145
Cdd:PRK07740  61 FVVFDLETTGFSPQ-QGDEILSIGAVKTKGGEVE-TDTFYSLVKPKRPI--PEHILELTGITAEDVAFAPPLAEVLHR 134
PRK06722 PRK06722
exonuclease; Provisional
 67-175 2.60e-05

exonuclease; Provisional


Pssm-ID: 180670 [Multi-domain]  Cd Length: 281  Bit Score: 43.89  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  67 YFLVLDFEATCdKP--QIHPQEIIEFPILKLNGRTMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:PRK06722   6 HFIVFDIERNF-RPykSEDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLIGVEKFPQIIE 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 678246462 145 RVDEWMAKEglldpnvkSIFVTCGDWDLKVM 175
Cdd:PRK06722  83 KFIQFIGED--------SIFVTWGKEDYRFL 105
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 68-146 5.60e-05

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 43.40  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  68 FLVLDFEATCDKPQiHPQEIIEFPILKL-NGRTMEIESTFhmyvqpvVHPQ--LTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:PRK08074   5 FVVVDLETTGNSPK-KGDKIIQIAAVVVeDGEILERFSSF-------VNPErpIPPFITELTGISEEMVKQAPLFEDVAP 76


                 ..
gi 678246462 145 RV 146
Cdd:PRK08074  77 EI 78
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 69-147 9.66e-04

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 39.19  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678246462  69 LVLDFEATCDKPQIHpqEIIEFPILK----LNGRTMEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQ----PSLQ 140
Cdd:PRK09182  40 VILDTETTGLDPRKD--EIIEIGMVAfeydDDGRIGDVLDTFGGLQQPSR--PIPPEITRLTGITDEMVAGQtidpAAVD 115


                 ....*..
gi 678246462 141 QVLERVD 147
Cdd:PRK09182 116 ALIAPAD 122
PRK06807 PRK06807
3'-5' exonuclease;
68-143 2.02e-03

3'-5' exonuclease;


Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 38.26  E-value: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678246462  68 FLVLDFEATCDKPqiHPQEIIEFPILKLngRTMEIESTFHMYVQPVVHpqLTPFCTELTGIIQAMVDGQPSLQQVL 143
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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