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Conserved domains on  [gi|2462513478|ref|XP_054194652|]
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ERI1 exoribonuclease 3 isoform X5 [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 ...
 68-245 7.42e-80

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: 237.89  E-value: 7.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQH 224
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEF 154

                         170       180
                  ....*....|....*....|.
gi 2462513478 225 IGRPHSGIDDCKNIANIMKTL 245
Cdd:cd06133   155 EGRHHRGLDDARNIARILKRL 175
 
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 ...
 68-245 7.42e-80

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: 237.89  E-value: 7.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQH 224
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEF 154

                         170       180
                  ....*....|....*....|.
gi 2462513478 225 IGRPHSGIDDCKNIANIMKTL 245
Cdd:cd06133   155 EGRHHRGLDDARNIARILKRL 175
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 61-255 4.01e-53

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 180.86  E-value: 4.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  61 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 139
Cdd:PTZ00315   51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 140 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKKAYS---FAMGCW--- 208
Cdd:PTZ00315  131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgFGNGSGcgg 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462513478 209 ------PKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQT 255
Cdd:PTZ00315  209 gatpplGPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPT 261
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 66-245 2.91e-50

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


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 162.72  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  66 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 142
Cdd:COG5018     2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 143 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKKAYSFAMGCwpkNGLLDMNKGLSL 222
Cdd:COG5018    81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---KKRIGLKKALEL 148

                         170       180
                  ....*....|....*....|....*.
gi 2462513478 223 QHI---GRPHSGIDDCKNIANIMKTL 245
Cdd:COG5018   149 LGLefeGTHHRALDDARNTAKLFKKI 174
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 69-242 1.33e-49

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: 160.59  E-value: 1.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  69 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 148
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 149 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKAYSFAMGcwpkNGLLDMNKGLSLQHIGRP 228
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPG----RSLDALAEKLGLEHIGRA 150

                         170
                  ....*....|....
gi 2462513478 229 HSGIDDCKNIANIM 242
Cdd:pfam00929 151 HRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 67-250 7.05e-42

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 140.90  E-value: 7.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478   67 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  147 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFKqwinLKKAYSFAmgcWPKNGLLDMNKGLSLQHIG 226
Cdd:smart00479  75 LEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPK--LPVIDTLK----LARATNPG---LPKYSLKKLAKRLLLEVIQ 145

                          170       180
                   ....*....|....*....|....
gi 2462513478  227 RPHSGIDDCKNIANIMKTLAYRGF 250
Cdd:smart00479 146 RAHRALDDARATAKLFKKLLERLE 169
 
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 ...
 68-245 7.42e-80

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: 237.89  E-value: 7.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDK---PQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:cd06133     1 YLVIDFEATCWEgnsKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPVINPKLSDFCTELTGITQEDVDNAPSFPEVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 145 RVDEWMAKEGlldpnvKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQH 224
Cdd:cd06133    81 EFLEWLGKNG------KYAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEF 154

                         170       180
                  ....*....|....*....|.
gi 2462513478 225 IGRPHSGIDDCKNIANIMKTL 245
Cdd:cd06133   155 EGRHHRGLDDARNIARILKRL 175
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 61-255 4.01e-53

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 180.86  E-value: 4.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  61 PPQRYHYFLVLDFEATCDKPQ-IHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSL 139
Cdd:PTZ00315   51 APQPFDAYVVLDFEATCEADRrIEDAEVIEFPMVLVDARTATPVAEFQRYVRPVKNPVLSRFCTELTGITQSMVSRADPF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 140 QQVLERVDEWMAKEGLLD--PNVKSIFVTCGDWDLKVMLPGQ---CQYLGLPVAdyFKQWINLKKAYS---FAMGCW--- 208
Cdd:PTZ00315  131 PVVYCEALQFLAEAGLGDapPLRSYCVVTCGDWDLKTMLPSQmrvSGQQGTPLS--FQRWCNLKKYMSqlgFGNGSGcgg 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462513478 209 ------PKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQT 255
Cdd:PTZ00315  209 gatpplGPSDMPDMLQMLGLPLQGRHHSGIDDCRNIAAVLCELLRRGLVIDPT 261
KapD COG5018
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ...
 66-245 2.91e-50

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


Pssm-ID: 444042 [Multi-domain]  Cd Length: 181  Bit Score: 162.72  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  66 HYFLVLDFEATC---DKPQIHPQEIIEFPILKLNGRTmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQV 142
Cdd:COG5018     2 MKYLVIDLEATCwdgKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRPKLSPFCTELTGITQEDVDSAPSFAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 143 LERVDEWMAKEglldpnvKSIFVTCGDWDLKVMLPgQCQYLGLPVaDYFKQWINLKKAYSFAMGCwpkNGLLDMNKGLSL 222
Cdd:COG5018    81 IEDFKKWIGSE-------DYILCSWGDYDRKQLER-NCRFHGVPY-PFGDRHINLKKLFALYFGL---KKRIGLKKALEL 148

                         170       180
                  ....*....|....*....|....*.
gi 2462513478 223 QHI---GRPHSGIDDCKNIANIMKTL 245
Cdd:COG5018   149 LGLefeGTHHRALDDARNTAKLFKKI 174
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 69-242 1.33e-49

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: 160.59  E-value: 1.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  69 LVLDFEATCDKPQihPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDE 148
Cdd:pfam00929   1 VVIDLETTGLDPE--KDEIIEIAAVVIDGGENEIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 149 WMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQylglPVADYFKQWINLKKAYSFAMGcwpkNGLLDMNKGLSLQHIGRP 228
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMP----KLNPVIDTLILDKATYKELPG----RSLDALAEKLGLEHIGRA 150

                         170
                  ....*....|....
gi 2462513478 229 HSGIDDCKNIANIM 242
Cdd:pfam00929 151 HRALDDARATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 67-250 7.05e-42

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 140.90  E-value: 7.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478   67 YFLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:smart00479   1 TLVVIDCETTGLDPGKD--EIIEIAAVDVDGG--EIIEVFDTYVKP--DRPITDYATEIHGITPEMLDDAPTFEEVLEEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  147 DEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYlgLPVADYFKqwinLKKAYSFAmgcWPKNGLLDMNKGLSLQHIG 226
Cdd:smart00479  75 LEFLRGRILVAGNSAHFDLRFLKLEHPRLGIKQPPK--LPVIDTLK----LARATNPG---LPKYSLKKLAKRLLLEVIQ 145

                          170       180
                   ....*....|....*....|....
gi 2462513478  227 RPHSGIDDCKNIANIMKTLAYRGF 250
Cdd:smart00479 146 RAHRALDDARATAKLFKKLLERLE 169
PRK07748 PRK07748
3'-5' exonuclease KapD;
68-243 3.45e-19

3'-5' exonuclease KapD;


Pssm-ID: 236087  Cd Length: 207  Bit Score: 82.81  E-value: 3.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDKPQIHPQ----EIIEFPILKLNGRtmEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVL 143
Cdd:PRK07748    6 FLFLDFEFTMPQHKKKPKgffpEIIEVGLVSVVGC--EVEDTFSSYVKPKTFPSLTERCKSFLGITQEDVDKGISFEELV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 144 ERVDEwmakeglLDPNVKSIFVTCGDWDLKVmLPGQCQYLGLPVAdyFK-QWINLKKAYSFAMGCWPKNGLLDMNKGLSL 222
Cdd:PRK07748   84 EKLAE-------YDKRCKPTIVTWGNMDMKV-LKHNCEKAGVPFP--FKgQCRDLSLEYKKFFGERNQTGLWKAIEEYGK 153

                         170       180
                  ....*....|....*....|.
gi 2462513478 223 QHIGRPHSGIDDCKNIANIMK 243
Cdd:PRK07748  154 EGTGKHHCALDDAMTTYNIFK 174
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 68-150 2.20e-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: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGrtMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:COG2176    10 YVVFDLETTGLSPKKD--EIIEIGAVKVEN--GEIVDRFSTLVNP--GRPIPPFITELTGITDEMVADAPPFEEVLPEFL 83


                  ...
gi 2462513478 148 EWM 150
Cdd:COG2176    84 EFL 86
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 68-151 3.94e-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: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:COG0847     2 FVVLDTETTGLDPAKD--RIIEIGAVKVDDG--RIVETFHTLVNP--ERPIPPEATAIHGITDEDVADAPPFAEVLPELL 75


                  ....
gi 2462513478 148 EWMA 151
Cdd:COG0847    76 EFLG 79
polC PRK00448
DNA polymerase III PolC; Validated
 68-150 7.04e-10

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 59.08  E-value: 7.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478   68 FLVLDFEATCDKPQIHpqEIIEFPILKL-NGrtmEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLERV 146
Cdd:PRK00448   421 YVVFDVETTGLSAVYD--EIIEIGAVKIkNG---EIIDKFEFFIKP--GHPLSAFTTELTGITDDMVKDAPSIEEVLPKF 493


                   ....
gi 2462513478  147 DEWM 150
Cdd:PRK00448   494 KEFC 497
PRK06722 PRK06722
exonuclease; Provisional
 67-242 6.47e-07

exonuclease; Provisional


Pssm-ID: 180670 [Multi-domain]  Cd Length: 281  Bit Score: 49.28  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  67 YFLVLDFEATCdKP--QIHPQEIIEFPILKLNGRTMEIESTFHMYVQPvvHPQLTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:PRK06722    6 HFIVFDIERNF-RPykSEDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLIGVEKFPQIIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478 145 RVDEWMAKEglldpnvkSIFVTCGDWDLKvMLPGQCQYLGLPVADYFKQ-WINLKK----AYSFAMGCWPKngLLDMNKG 219
Cdd:PRK06722   83 KFIQFIGED--------SIFVTWGKEDYR-FLSHDCTLHSVECPCMEKErRIDLQKfvfqAYEELFEHTPS--LQSAVEQ 151

                         170       180
                  ....*....|....*....|...
gi 2462513478 220 LSLQHIGRPHSGIDDCKNIANIM 242
Cdd:PRK06722  152 LGLIWEGKQHRALADAENTANIL 174
PRK08517 PRK08517
3'-5' exonuclease;
68-145 9.95e-06

3'-5' exonuclease;


Pssm-ID: 236281 [Multi-domain]  Cd Length: 257  Bit Score: 45.78  E-value: 9.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462513478  68 FLVLDFEATCDKPQIHpqEIIEFPILKLNGRtmEIESTFHMYVQPvvhPQLTPFCTELTGIIQAMVDGQPSLQQVLER 145
Cdd:PRK08517   70 FCFVDIETNGSKPKKH--QIIEIGAVKVKNG--EIIDRFESFVKA---KEVPEYITELTGITYEDLENAPSLKEVLEE 140
PRK07883 PRK07883
DEDD exonuclease domain-containing protein;
68-149 1.17e-05

DEDD exonuclease domain-containing protein;


Pssm-ID: 236123 [Multi-domain]  Cd Length: 557  Bit Score: 46.06  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDKPqiHPQEIIEFPILKLNGRtmEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQPSLQQVLERVD 147
Cdd:PRK07883   17 FVVVDLETTGGSP--AGDAITEIGAVKVRGG--EVLGEFATLVNPGR--PIPPFITVLTGITTAMVAGAPPIEEVLPAFL 90


                  ..
gi 2462513478 148 EW 149
Cdd:PRK07883   91 EF 92
PRK07740 PRK07740
hypothetical protein; Provisional
 68-145 1.65e-05

hypothetical protein; Provisional


Pssm-ID: 236085 [Multi-domain]  Cd Length: 244  Bit Score: 45.04  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462513478  68 FLVLDFEATCDKPQiHPQEIIEFPILKLNGRTMEIEsTFHMYVQPVVHPqlTPFCTELTGIIQAMVDGQPSLQQVLER 145
Cdd:PRK07740   61 FVVFDLETTGFSPQ-QGDEILSIGAVKTKGGEVETD-TFYSLVKPKRPI--PEHILELTGITAEDVAFAPPLAEVLHR 134
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
 68-146 6.95e-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: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  68 FLVLDFEATCDKPQiHPQEIIEFPILKL-NGRTMEIESTFhmyvqpvVHPQ--LTPFCTELTGIIQAMVDGQPSLQQVLE 144
Cdd:PRK08074    5 FVVVDLETTGNSPK-KGDKIIQIAAVVVeDGEILERFSSF-------VNPErpIPPFITELTGISEEMVKQAPLFEDVAP 76


                  ..
gi 2462513478 145 RV 146
Cdd:PRK08074   77 EI 78
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 69-147 1.55e-03

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 39.19  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513478  69 LVLDFEATCDKPQIHpqEIIEFPILK----LNGRTMEIESTFHMYVQPVVhpQLTPFCTELTGIIQAMVDGQ----PSLQ 140
Cdd:PRK09182   40 VILDTETTGLDPRKD--EIIEIGMVAfeydDDGRIGDVLDTFGGLQQPSR--PIPPEITRLTGITDEMVAGQtidpAAVD 115


                  ....*..
gi 2462513478 141 QVLERVD 147
Cdd:PRK09182  116 ALIAPAD 122
PRK06807 PRK06807
3'-5' exonuclease;
68-143 3.22e-03

3'-5' exonuclease;


Pssm-ID: 235864 [Multi-domain]  Cd Length: 313  Bit Score: 38.26  E-value: 3.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462513478  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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