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Conserved domains on  [gi|71982768|ref|NP_001021323|]
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Egalitarian protein homolog [Caenorhabditis elegans]

Protein Classification

3'-5' exonuclease family protein( domain architecture ID 10150270)

3'-5' exonuclease family protein belonging to the DnaQ-like (or DEDD) 3'-5' exonuclease superfamily, similar to human piRNA biogenesis protein EXD1, an RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis

CATH:  3.30.420.10
Gene Ontology:  GO:0003676
PubMed:  11988770|11222749
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 309-503 1.61e-76

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


:

Pssm-ID: 99851  Cd Length: 197  Bit Score: 240.65  E-value: 1.61e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 309 DINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATtSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAH 388
Cdd:cd06148   4 IIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATRT-GQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDALYH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 389 KYAVHMRNVFDTQVAHSLLQHEKFNKsLNEMRPISFINLQRVYYPQSI-MLSDVTPRKMSMCPNWGVRPITEEFQLTIVE 467
Cdd:cd06148  83 QYGIKLNNVFDTQVADALLQEQETGG-FNPDRVISLVQLLDKYLYISIsLKEDVKKLMREDPKFWALRPLTEDMIRYAAL 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 71982768 468 EAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPE 503
Cdd:cd06148 162 DVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
 
Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 309-503 1.61e-76

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 99851  Cd Length: 197  Bit Score: 240.65  E-value: 1.61e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 309 DINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATtSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAH 388
Cdd:cd06148   4 IIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATRT-GQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDALYH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 389 KYAVHMRNVFDTQVAHSLLQHEKFNKsLNEMRPISFINLQRVYYPQSI-MLSDVTPRKMSMCPNWGVRPITEEFQLTIVE 467
Cdd:cd06148  83 QYGIKLNNVFDTQVADALLQEQETGG-FNPDRVISLVQLLDKYLYISIsLKEDVKKLMREDPKFWALRPLTEDMIRYAAL 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 71982768 468 EAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPE 503
Cdd:cd06148 162 DVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 290-484 9.80e-23

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 95.12  E-value: 9.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768    290 IHFVKALKPAQDLISRLWqdinnMEKKVVGLDLKTVTVG-VDGEIflsLGVIATTSQIGIFDLASSDVIILESGFKGILE 368
Cdd:smart00474   1 VIVVTDSETLEELLEKLR-----AAGGEVALDTETTGLDsYSGKL---VLIQISVTGEGAFIIDPLALGDDLEILKDLLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768    369 SEKVVKVIHDARRVASLLAHkYAVHMRNVFDTQVAHSLLqhekfnkslneMRPISFINLQRVYYpqsiMLSDVTPRKMSM 448
Cdd:smart00474  73 DETITKVGHNAKFDLHVLAR-FGIELENIFDTMLAAYLL-----------LGGPSKHGLATLLL----GYLGVELDKEEQ 136

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 71982768    449 CPNWGVRPITEEFQLTIVEEAHCLLSaLYQSLSNLI 484
Cdd:smart00474 137 KSDWGARPLSEEQLEYAAEDADALLR-LYEKLEKEL 171
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 290-485 1.99e-09

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 56.93  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768   290 IHFVKALKPAQDLISRLwqdinnMEKKVVGLDlkTVTVGVDGEIFLSLGV---IATTSQIGIFD-LASSDVIIleSGFKG 365
Cdd:pfam01612   1 YRIVTTEDELEDLIEEL------LNAPYVAVD--TETTSLDTYSYYLRGAliqIGTGEGAYIIDpLALGDDVL--SALKR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768   366 ILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKfNKSLNEMrpisfinLQRvyypqsimLSDVTPRK 445
Cdd:pfam01612  71 LLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLGYDR-SHSLADL-------AEK--------YLGVELDK 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 71982768   446 MSMCPNWGVRPITEEFQLTIVEEAHCLLSaLYQSLSNLIP 485
Cdd:pfam01612 135 EEQCSDWQARPLSEEQLRYAALDADYLLR-LYDKLRKELE 173
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
327-464 6.19e-07

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 51.80  E-value: 6.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 327 VGVDGEiFLS-------LGVI--ATTSQIGIFD-LASSDViileSGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRN 396
Cdd:COG0349  21 VAVDTE-FMRertyyprLCLIqlADGEEVALIDpLAIGDL----SPLWELLADPAIVKVFHAAREDLEILYHLFGILPKP 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982768 397 VFDTQVAHSLLQHEKfnkslnemrPISFINLQRVYYpqsimlsDVTPRKMSMCPNWGVRPITEEfQLT 464
Cdd:COG0349  96 LFDTQIAAALLGYGD---------SVGYAALVEELL-------GVELDKSEQRSDWLRRPLSEE-QLE 146
 
Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 309-503 1.61e-76

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 99851  Cd Length: 197  Bit Score: 240.65  E-value: 1.61e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 309 DINNMEKKVVGLDLKTVTVGVDGEIFLSLGVIATtSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAH 388
Cdd:cd06148   4 IIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATRT-GQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDALYH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 389 KYAVHMRNVFDTQVAHSLLQHEKFNKsLNEMRPISFINLQRVYYPQSI-MLSDVTPRKMSMCPNWGVRPITEEFQLTIVE 467
Cdd:cd06148  83 QYGIKLNNVFDTQVADALLQEQETGG-FNPDRVISLVQLLDKYLYISIsLKEDVKKLMREDPKFWALRPLTEDMIRYAAL 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 71982768 468 EAHCLLSALYQSLSNLIPVHLRGVFEDKCIEVNHPE 503
Cdd:cd06148 162 DVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 290-484 9.80e-23

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 95.12  E-value: 9.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768    290 IHFVKALKPAQDLISRLWqdinnMEKKVVGLDLKTVTVG-VDGEIflsLGVIATTSQIGIFDLASSDVIILESGFKGILE 368
Cdd:smart00474   1 VIVVTDSETLEELLEKLR-----AAGGEVALDTETTGLDsYSGKL---VLIQISVTGEGAFIIDPLALGDDLEILKDLLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768    369 SEKVVKVIHDARRVASLLAHkYAVHMRNVFDTQVAHSLLqhekfnkslneMRPISFINLQRVYYpqsiMLSDVTPRKMSM 448
Cdd:smart00474  73 DETITKVGHNAKFDLHVLAR-FGIELENIFDTMLAAYLL-----------LGGPSKHGLATLLL----GYLGVELDKEEQ 136

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 71982768    449 CPNWGVRPITEEFQLTIVEEAHCLLSaLYQSLSNLI 484
Cdd:smart00474 137 KSDWGARPLSEEQLEYAAEDADALLR-LYEKLEKEL 171
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 300-463 9.31e-11

DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D is a bacterial enzyme involved in the maturation of small stable RNAs and the 3' maturation of tRNA. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. In vivo, RNase D only becomes essential upon removal of other ribonucleases. Eukaryotic RNase D homologs include yeast Rrp6p, human PM/Scl-100, and the Drosophila melanogaster egalitarian protein.


Pssm-ID: 176654 [Multi-domain]  Cd Length: 178  Bit Score: 61.01  E-value: 9.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 300 QDLISRLWQDinnmekKVVGLDLKTVTVGVDGEIfLSLGVIATTSQIGIFD-LASSDViileSGFKGILESEKVVKVIHD 378
Cdd:cd06142   3 EDLCERLASA------GVIAVDTEFMRLNTYYPR-LCLIQISTGGEVYLIDpLAIGDL----SPLKELLADPNIVKVFHA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 379 ARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKfnkslnemrPISFINLQRVYYpqsimlsDVTPRKMSMCPNWGVRPIT 458
Cdd:cd06142  72 AREDLELLKRDFGILPQNLFDTQIAARLLGLGD---------SVGLAALVEELL-------GVELDKGEQRSDWSKRPLT 135


                ....*
gi 71982768 459 EEfQL 463
Cdd:cd06142 136 DE-QL 139
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 290-485 1.99e-09

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 56.93  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768   290 IHFVKALKPAQDLISRLwqdinnMEKKVVGLDlkTVTVGVDGEIFLSLGV---IATTSQIGIFD-LASSDVIIleSGFKG 365
Cdd:pfam01612   1 YRIVTTEDELEDLIEEL------LNAPYVAVD--TETTSLDTYSYYLRGAliqIGTGEGAYIIDpLALGDDVL--SALKR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768   366 ILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDTQVAHSLLQHEKfNKSLNEMrpisfinLQRvyypqsimLSDVTPRK 445
Cdd:pfam01612  71 LLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLGYDR-SHSLADL-------AEK--------YLGVELDK 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 71982768   446 MSMCPNWGVRPITEEFQLTIVEEAHCLLSaLYQSLSNLIP 485
Cdd:pfam01612 135 EEQCSDWQARPLSEEQLRYAALDADYLLR-LYDKLRKELE 173
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
327-464 6.19e-07

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 51.80  E-value: 6.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 327 VGVDGEiFLS-------LGVI--ATTSQIGIFD-LASSDViileSGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRN 396
Cdd:COG0349  21 VAVDTE-FMRertyyprLCLIqlADGEEVALIDpLAIGDL----SPLWELLADPAIVKVFHAAREDLEILYHLFGILPKP 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982768 397 VFDTQVAHSLLQHEKfnkslnemrPISFINLQRVYYpqsimlsDVTPRKMSMCPNWGVRPITEEfQLT 464
Cdd:COG0349  96 LFDTQIAAALLGYGD---------SVGYAALVEELL-------GVELDKSEQRSDWLRRPLSEE-QLE 146
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 299-460 8.43e-06

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D 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. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 46.42  E-value: 8.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 299 AQDLISRLwqdinNMEKKVVGLDLKTVTVGVDGEIF-LSLGVIATTSQIGIFDLASSDviILESGFKGILESEKVVKV-- 375
Cdd:cd06141   7 AEEAVKEL-----LGKEKVVGFDTEWRPSFRKGKRNkVALLQLATESRCLLFQLAHMD--KLPPSLKQLLEDPSILKVgv 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982768 376 --IHDARRvaslLAHKYAVHMRNVFDTQVAHsllqhekfNKSLNEMRPISFINL------QRVYYPQSIMLSdvtprkms 447
Cdd:cd06141  80 giKGDARK----LARDFGIEVRGVVDLSHLA--------KRVGPRRKLVSLARLveevlgLPLSKPKKVRCS-------- 139

                       170
                ....*....|...
gi 71982768 448 mcpNWGVRPITEE 460
Cdd:cd06141 140 ---NWEARPLSKE 149
DNA_polA_I_Bacillus_like_exo cd06140
inactive DEDDy 3'-5' exonuclease domain of Bacillus stearothermophilus DNA polymerase I and ...
 347-403 2.05e-04

inactive DEDDy 3'-5' exonuclease domain of Bacillus stearothermophilus DNA polymerase I and similar family-A DNA polymerases; Bacillus stearothermophilus-like Polymerase I (Pol I), a subgroup of the family-A DNA polymerases, contains an inactive DnaQ-like 3'-5' exonuclease domain in the same polypeptide chain as the polymerase region. The exonuclease-like domain of these proteins possess the same fold as the Klenow fragment (KF) of Escherichia coli Pol I, but does not contain the four critical metal-binding residues necessary for activity. The function of this domain is unknown. It might act as a spacer between the polymerase and the 5'-3' exonuclease domains. Some members of this subgroup, such as those from Bacillus sphaericus and Thermus aquaticus, are thermostable DNA polymerases.


Pssm-ID: 176652 [Multi-domain]  Cd Length: 178  Bit Score: 42.25  E-value: 2.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71982768 347 GIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLaHKYAVHMRNV-FDTQVA 403
Cdd:cd06140  32 GAYYIPLELALLDLAALKEWLEDEKIPKVGHDAKRAYVAL-KRHGIELAGVaFDTMLA 88
PolA COG0749
DNA polymerase I, 3'-5' exonuclease and polymerase domains [Replication, recombination and ...
 363-419 7.49e-04

DNA polymerase I, 3'-5' exonuclease and polymerase domains [Replication, recombination and repair];


Pssm-ID: 440512 [Multi-domain]  Cd Length: 575  Bit Score: 42.35  E-value: 7.49e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71982768 363 FKGILESEKVVKVIHDARRVASLLAhKYAVHMRNV-FDTQVAHSLLQHEKFNKSLNEM 419
Cdd:COG0749  54 LKPLLEDPAIPKIGQNLKYDLHVLA-RYGIELAGVaFDTMLASYLLNPGRRRHGLDDL 110
 
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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