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Conserved domains on  [gi|1907154163|ref|XP_036019559|]
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ERI1 exoribonuclease 3 isoform X11 [Mus musculus]

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 ...
 35-192 4.61e-63

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: 195.13  E-value: 4.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  35 WMGPSWGQHPGEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEG 114
Cdd:cd06133    11 WEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLKEFLEWLGKNG 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907154163 115 lldpnvKSIFVTCGDWDLKVMLPGQCHYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:cd06133    91 ------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEFEGRHHRGL 162
 
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 ...
 35-192 4.61e-63

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: 195.13  E-value: 4.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  35 WMGPSWGQHPGEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEG 114
Cdd:cd06133    11 WEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLKEFLEWLGKNG 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907154163 115 lldpnvKSIFVTCGDWDLKVMLPGQCHYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:cd06133    91 ------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEFEGRHHRGL 162
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 42-192 1.11e-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: 132.48  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  42 QHPGEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLDPNVK 121
Cdd:pfam00929  12 PEKDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFLRKGNLLVAHNA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154163 122 SIFVTCGDWDLKVMLPGQChylgLPVADYFKQWINLKKAYSFAMGcwpkNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:pfam00929  92 SFDVGFLRYDDKRFLKKPM----PKLNPVIDTLILDKATYKELPG----RSLDALAEKLGLEHIGRAHRAL 154
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 35-192 2.11e-35

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


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 124.59  E-value: 2.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  35 WMGPSWGQHPGEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEg 114
Cdd:COG5018    14 WDGKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEAIEDFKKWIGSE- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163 115 lldpnvKSIFVTCGDWDLKVMLPgQCHYLGLPVaDYFKQWINLKKAYSFAMGCwpkNGLLDMNKGLSLQHI---GRPHSG 191
Cdd:COG5018    92 ------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---KKRIGLKKALELLGLefeGTHHRA 160


                  .
gi 1907154163 192 I 192
Cdd:COG5018   161 L 161
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 46-192 1.26e-34

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 130.40  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  46 EIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLD--PNVKSI 123
Cdd:PTZ00315   77 EVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPFPVVYCEALQFLAEAGLGDapPLRSYC 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163 124 FVTCGDWDLKVMLPGQ---CHYLGLPVAdyFKQWINLKKAYS---FAMGCW---------PKNGLLDMNKGLSLQHIGRP 188
Cdd:PTZ00315  157 VVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgFGNGSGcgggatpplGPSDMPDMLQMLGLPLQGRH 234


                  ....
gi 1907154163 189 HSGI 192
Cdd:PTZ00315  235 HSGI 238
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 46-192 4.32e-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: 105.07  E-value: 4.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163   46 EIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFV 125
Cdd:smart00479  18 EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFLRGRILVAGNSAHFDL 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154163  126 TCGDWDLKVMLPGQCHYlgLPVADYFKqwinLKKAYSFAmgcWPKNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:smart00479  94 RFLKLEHPRLGIKQPPK--LPVIDTLK----LARATNPG---LPKYSLKKLAKRLLLEVIQRAHRAL 151
 
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 ...
 35-192 4.61e-63

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: 195.13  E-value: 4.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  35 WMGPSWGQHPGEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEG 114
Cdd:cd06133    11 WEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLKEFLEWLGKNG 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907154163 115 lldpnvKSIFVTCGDWDLKVMLPGQCHYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:cd06133    91 ------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEFEGRHHRGL 162
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 42-192 1.11e-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: 132.48  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  42 QHPGEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLDPNVK 121
Cdd:pfam00929  12 PEKDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLEFLRKGNLLVAHNA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154163 122 SIFVTCGDWDLKVMLPGQChylgLPVADYFKQWINLKKAYSFAMGcwpkNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:pfam00929  92 SFDVGFLRYDDKRFLKKPM----PKLNPVIDTLILDKATYKELPG----RSLDALAEKLGLEHIGRAHRAL 154
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 35-192 2.11e-35

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


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 124.59  E-value: 2.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  35 WMGPSWGQHPGEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEg 114
Cdd:COG5018    14 WDGKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEAIEDFKKWIGSE- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163 115 lldpnvKSIFVTCGDWDLKVMLPgQCHYLGLPVaDYFKQWINLKKAYSFAMGCwpkNGLLDMNKGLSLQHI---GRPHSG 191
Cdd:COG5018    92 ------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---KKRIGLKKALELLGLefeGTHHRA 160


                  .
gi 1907154163 192 I 192
Cdd:COG5018   161 L 161
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 46-192 1.26e-34

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 130.40  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  46 EIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLD--PNVKSI 123
Cdd:PTZ00315   77 EVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPFPVVYCEALQFLAEAGLGDapPLRSYC 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163 124 FVTCGDWDLKVMLPGQ---CHYLGLPVAdyFKQWINLKKAYS---FAMGCW---------PKNGLLDMNKGLSLQHIGRP 188
Cdd:PTZ00315  157 VVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgFGNGSGcgggatpplGPSDMPDMLQMLGLPLQGRH 234


                  ....
gi 1907154163 189 HSGI 192
Cdd:PTZ00315  235 HSGI 238
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 46-192 4.32e-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: 105.07  E-value: 4.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163   46 EIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFV 125
Cdd:smart00479  18 EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFLRGRILVAGNSAHFDL 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154163  126 TCGDWDLKVMLPGQCHYlgLPVADYFKqwinLKKAYSFAmgcWPKNGLLDMNKGLSLQHIGRPHSGI 192
Cdd:smart00479  94 RFLKLEHPRLGIKQPPK--LPVIDTLK----LARATNPG---LPKYSLKKLAKRLLLEVIQRAHRAL 151
PRK07748 PRK07748
3'-5' exonuclease KapD;
46-160 4.79e-11

3'-5' exonuclease KapD;


Pssm-ID: 236087  Cd Length: 207  Bit Score: 60.47  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  46 EIIEFPILKLNGRtmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEwmakeglLDPNVKSIFV 125
Cdd:PRK07748   28 EIIEVGLVSVVGC--EVEDTFSSYVKPKTFPSLTERCKSFLGITQEDVDKGISFEELVEKLAE-------YDKRCKPTIV 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907154163 126 TCGDWDLKVM--------LP----GQCHYLGLPVADYF--KQWINLKKA 160
Cdd:PRK07748   99 TWGNMDMKVLkhncekagVPfpfkGQCRDLSLEYKKFFgeRNQTGLWKA 147
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 46-110 3.99e-09

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


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 54.38  E-value: 3.99e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907154163  46 EIIEFPILKLNGrtMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWM 110
Cdd:COG2176    26 EIIEIGAVKVEN--GEIVDRFSTLVNP--GRPIPPFITELTGITDEMVADAPPFEEVLPEFLEFL 86
polC PRK00448
DNA polymerase III PolC; Validated
 46-110 7.90e-09

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 56.00  E-value: 7.90e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154163   46 EIIEFPILKL-NGrtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWM 110
Cdd:PRK00448   437 EIIEIGAVKIkNG---EIIDKFEFFIKP--GHPLSAFTTELTGITDDMVKDAPSIEEVLPKFKEFC 497
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 46-111 6.79e-06

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


Pssm-ID: 440608 [Multi-domain]  Cd Length: 163  Bit Score: 45.17  E-value: 6.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154163  46 EIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMA 111
Cdd:COG0847    18 RIIEIGAVKVDDG--RIVETFHTLVNP--ERPIPPEATAIHGITDEDVADAPPFAEVLPELLEFLG 79
PRK06722 PRK06722
exonuclease; Provisional
 38-135 6.43e-05

exonuclease; Provisional


Pssm-ID: 180670 [Multi-domain]  Cd Length: 281  Bit Score: 43.12  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154163  38 PSWGQHPGEIIEFPILKLNGRTMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEglld 117
Cdd:PRK06722   18 PYKSEDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLIGVEKFPQIIEKFIQFIGED---- 91

                          90
                  ....*....|....*...
gi 1907154163 118 pnvkSIFVTCGDWDLKVM 135
Cdd:PRK06722   92 ----SIFVTWGKEDYRFL 105
PRK07883 PRK07883
DEDD exonuclease domain-containing protein;
80-109 5.28e-04

DEDD exonuclease domain-containing protein;


Pssm-ID: 236123 [Multi-domain]  Cd Length: 557  Bit Score: 41.06  E-value: 5.28e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907154163  80 PFCTELTGIIQAMVDGQPSLQQVLERVDEW 109
Cdd:PRK07883   63 PFITVLTGITTAMVAGAPPIEEVLPAFLEF 92
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 46-106 8.01e-04

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 40.32  E-value: 8.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154163  46 EIIEFPILKL-NGRTMEIESTFhmyvqpvVHPQ--LTPFCTELTGIIQAMVDGQPSLQQVLERV 106
Cdd:PRK08074   22 KIIQIAAVVVeDGEILERFSSF-------VNPErpIPPFITELTGISEEMVKQAPLFEDVAPEI 78
PRK08517 PRK08517
3'-5' exonuclease;
45-105 1.05e-03

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 39.62  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154163  45 GEIIEFPILKLNGRtmEIESTFHMYVQPvvhPQLTPFCTELTGIIQAMVDGQPSLQQVLER 105
Cdd:PRK08517   85 HQIIEIGAVKVKNG--EIIDRFESFVKA---KEVPEYITELTGITYEDLENAPSLKEVLEE 140
PRK07740 PRK07740
hypothetical protein; Provisional
 42-105 1.86e-03

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 38.50  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154163  42 QHPGEIIEFPILKLNGRTMEiESTFHMYVQPVVHPqlTPFCTELTGIIQAMVDGQPSLQQVLER 105
Cdd:PRK07740   74 QQGDEILSIGAVKTKGGEVE-TDTFYSLVKPKRPI--PEHILELTGITAEDVAFAPPLAEVLHR 134
 
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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