|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06722 |
PRK06722 |
exonuclease; Provisional |
1-281 |
0e+00 |
|
exonuclease; Provisional
Pssm-ID: 180670 [Multi-domain] Cd Length: 281 Bit Score: 576.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 1 MENTTHFIVFDIERNFRPYKSDDPSEIVDIGAVKIEASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQI 80
Cdd:PRK06722 1 MENATHFIVFDIERNFRPYKSEDPSEIVDIGAVKIEASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLIGVEKFPQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 81 IEKFIQFIGEDSIFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEELFEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:PRK06722 81 IEKFIQFIGEDSIFVTWGKEDYRFLSHDCTLHSVECPCMEKERRIDLQKFVFQAYEELFEHTPSLQSAVEQLGLIWEGKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 161 HRALADAENTANILLKVYSERDIHKRYKRHGELELVENGKLTEKAKKKMRKWVFKEMRKNTERPFVWSTFESSDTWESIT 240
Cdd:PRK06722 161 HRALADAENTANILLKAYSERDITKRYKRHGELELVKNGKLTEKAKKKMRKWVFKEMRKNTERPFVWSTFESSDTWESIT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 872545819 241 ERYYISEATIELLKKHFRTAVRKAERQIKYLVEMEKNAEVK 281
Cdd:PRK06722 241 ERYYISESTIELLKKHFRTAVRKAERQIRYLAEMEKVVEEN 281
|
|
| ERI-1_3'hExo_like |
cd06133 |
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ... |
7-178 |
5.55e-47 |
|
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: 155.07 E-value: 5.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERN--FRPYKSDDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLMGIEEFPQIIE 82
Cdd:cd06133 1 YLVIDFEATcwEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPviNPKLSDFCTELTGITQEDVDNAPSFPEVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 83 KFIQFIGEDS--IFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEelFEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:cd06133 81 EFLEWLGKNGkyAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYG--LKKRTGLSKALEYLGLEFEGRH 158
|
170
....*....|....*...
gi 872545819 161 HRALADAENTANILLKVY 178
Cdd:cd06133 159 HRGLDDARNIARILKRLL 176
|
|
| KapD |
COG5018 |
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ... |
6-183 |
5.38e-46 |
|
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];
Pssm-ID: 444042 [Multi-domain] Cd Length: 181 Bit Score: 152.71 E-value: 5.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 6 HFIVFDIERN--FRPYKSDDPSEIVDIGAVKIEASTmKVIGEFSELVKPGAR--LTRHTTKLTGITKKDLMGIEEFPQII 81
Cdd:COG5018 3 KYLVIDLEATcwDGKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRpkLSPFCTELTGITQEDVDSAPSFAEAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 82 EKFIQFIG-EDSIFVSWGREDYRFLSHDCTLHGVECPSMEKERkfDLQKFvFQAYEELfEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:COG5018 82 EDFKKWIGsEDYILCSWGDYDRKQLERNCRFHGVPYPFGDRHI--NLKKL-FALYFGL-KKRIGLKKALELLGLEFEGTH 157
|
170 180
....*....|....*....|...
gi 872545819 161 HRALADAENTANILLKVYSERDI 183
Cdd:COG5018 158 HRALDDARNTAKLFKKILGDKRL 180
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
7-177 |
3.34e-24 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 95.83 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERNfrpYKSDDPSEIVDIGAVKIEasTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQ 86
Cdd:smart00479 2 LVVIDCETT---GLDPGKDEIIEIAAVDVD--GGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 87 FIGEDSIFV-SWGREDYRFLSHDCTLHGVECPSMEKERK-FDLQKFVFQAYeelfeHTPSLQFAVEQLGLTWEGKQHRAL 164
Cdd:smart00479 77 FLRGRILVAgNSAHFDLRFLKLEHPRLGIKQPPKLPVIDtLKLARATNPGL-----PKYSLKKLAKRLLLEVIQRAHRAL 151
|
170
....*....|...
gi 872545819 165 ADAENTANILLKV 177
Cdd:smart00479 152 DDARATAKLFKKL 164
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
8-174 |
5.11e-20 |
|
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: 84.33 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 8 IVFDIERN-FRPYKSddpsEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLMGIEEFPQIIEKF 84
Cdd:pfam00929 1 VVIDLETTgLDPEKD----EIIEIAAVVIDGGENEIGETFHTYVKPtrLPKLTDECTKFTGITQAMLDNKPSFEEVLEEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 85 IQFIGEDSIFVSWGRE-DYRFLSHDCTLHG-VECPSMEKerKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWEGKQHR 162
Cdd:pfam00929 77 LEFLRKGNLLVAHNASfDVGFLRYDDKRFLkKPMPKLNP--VIDTLILDKATYKELPGR--SLDALAEKLGLEHIGRAHR 152
|
170
....*....|..
gi 872545819 163 ALADAENTANIL 174
Cdd:pfam00929 153 ALDDARATAKLF 164
|
|
| dnaq |
TIGR00573 |
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ... |
27-178 |
6.01e-06 |
|
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, Degradation of DNA]
Pssm-ID: 129663 [Multi-domain] Cd Length: 217 Bit Score: 46.29 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 27 IVDIGAVKIeASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQFIGEDSIFVSWGREDYRFLS 106
Cdd:TIGR00573 25 IIEIGAVEI-INRRITGNKFHTYIKPDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADYIRGAELVIHNASFDVGFLN 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872545819 107 HDCTLhgvECPSMEKERKF-DLQKFVFQAYEELFEHTPSLQFAVEQLGLTwegKQHRALADAENTANILLKVY 178
Cdd:TIGR00573 104 YEFSK---LYKVEPKTNDViDTTDTLQYARPEFPGKRNTLDALCKRYEIT---NSHRALHGALADAFILAKLY 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06722 |
PRK06722 |
exonuclease; Provisional |
1-281 |
0e+00 |
|
exonuclease; Provisional
Pssm-ID: 180670 [Multi-domain] Cd Length: 281 Bit Score: 576.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 1 MENTTHFIVFDIERNFRPYKSDDPSEIVDIGAVKIEASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQI 80
Cdd:PRK06722 1 MENATHFIVFDIERNFRPYKSEDPSEIVDIGAVKIEASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLIGVEKFPQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 81 IEKFIQFIGEDSIFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEELFEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:PRK06722 81 IEKFIQFIGEDSIFVTWGKEDYRFLSHDCTLHSVECPCMEKERRIDLQKFVFQAYEELFEHTPSLQSAVEQLGLIWEGKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 161 HRALADAENTANILLKVYSERDIHKRYKRHGELELVENGKLTEKAKKKMRKWVFKEMRKNTERPFVWSTFESSDTWESIT 240
Cdd:PRK06722 161 HRALADAENTANILLKAYSERDITKRYKRHGELELVKNGKLTEKAKKKMRKWVFKEMRKNTERPFVWSTFESSDTWESIT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 872545819 241 ERYYISEATIELLKKHFRTAVRKAERQIKYLVEMEKNAEVK 281
Cdd:PRK06722 241 ERYYISESTIELLKKHFRTAVRKAERQIRYLAEMEKVVEEN 281
|
|
| ERI-1_3'hExo_like |
cd06133 |
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ... |
7-178 |
5.55e-47 |
|
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: 155.07 E-value: 5.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERN--FRPYKSDDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLMGIEEFPQIIE 82
Cdd:cd06133 1 YLVIDFEATcwEGNSKPDYPNEIIEIGAVLVDVKTKEIIDTFSSYVKPviNPKLSDFCTELTGITQEDVDNAPSFPEVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 83 KFIQFIGEDS--IFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEelFEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:cd06133 81 EFLEWLGKNGkyAFVTWGDWDLKDLLQNQCKYKIINLPPFFRQWIDLKKEFAKFYG--LKKRTGLSKALEYLGLEFEGRH 158
|
170
....*....|....*...
gi 872545819 161 HRALADAENTANILLKVY 178
Cdd:cd06133 159 HRGLDDARNIARILKRLL 176
|
|
| KapD |
COG5018 |
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction ... |
6-183 |
5.38e-46 |
|
3'-5' exonuclease KapD, inhibitor of KinA-controlled sporulation [Signal transduction mechanisms];
Pssm-ID: 444042 [Multi-domain] Cd Length: 181 Bit Score: 152.71 E-value: 5.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 6 HFIVFDIERN--FRPYKSDDPSEIVDIGAVKIEASTmKVIGEFSELVKPGAR--LTRHTTKLTGITKKDLMGIEEFPQII 81
Cdd:COG5018 3 KYLVIDLEATcwDGKPPPGFPMEIIEIGAVKVDENG-EIIDEFSSFVKPVRRpkLSPFCTELTGITQEDVDSAPSFAEAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 82 EKFIQFIG-EDSIFVSWGREDYRFLSHDCTLHGVECPSMEKERkfDLQKFvFQAYEELfEHTPSLQFAVEQLGLTWEGKQ 160
Cdd:COG5018 82 EDFKKWIGsEDYILCSWGDYDRKQLERNCRFHGVPYPFGDRHI--NLKKL-FALYFGL-KKRIGLKKALELLGLEFEGTH 157
|
170 180
....*....|....*....|...
gi 872545819 161 HRALADAENTANILLKVYSERDI 183
Cdd:COG5018 158 HRALDDARNTAKLFKKILGDKRL 180
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
5-180 |
1.15e-32 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 118.32 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 5 THFIVFDIERN-FRPYKSddpsEIVDIGAVKIEasTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEK 83
Cdd:COG2176 8 LTYVVFDLETTgLSPKKD----EIIEIGAVKVE--NGEIVDRFSTLVNPGRPIPPFITELTGITDEMVADAPPFEEVLPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 84 FIQFIGeDSIFVSWG-REDYRFLSHDCTLHGVECpsmeKERKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWEgKQHR 162
Cdd:COG2176 82 FLEFLG-DAVLVAHNaSFDLGFLNAALKRLGLPF----DNPVLDTLELARRLLPELKSY--KLDTLAERLGIPLE-DRHR 153
|
170
....*....|....*...
gi 872545819 163 ALADAENTANILLKVYSE 180
Cdd:COG2176 154 ALGDAEATAELFLKLLEK 171
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
7-176 |
2.81e-25 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 98.33 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIER-NFRPYKSddpsEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFI 85
Cdd:COG0847 2 FVVLDTETtGLDPAKD----RIIEIGAVKVDDG--RIVETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 86 QFIgEDSIFVSWGRE-DYRFLSHDCTLHGVECPSMekeRKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWEGkQHRAL 164
Cdd:COG0847 76 EFL-GGAVLVAHNAAfDLGFLNAELRRAGLPLPPF---PVLDTLRLARRLLPGLPSY--SLDALCERLGIPFDE-RHRAL 148
|
170
....*....|..
gi 872545819 165 ADAENTANILLK 176
Cdd:COG0847 149 ADAEATAELFLA 160
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
7-177 |
3.34e-24 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 95.83 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERNfrpYKSDDPSEIVDIGAVKIEasTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQ 86
Cdd:smart00479 2 LVVIDCETT---GLDPGKDEIIEIAAVDVD--GGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 87 FIGEDSIFV-SWGREDYRFLSHDCTLHGVECPSMEKERK-FDLQKFVFQAYeelfeHTPSLQFAVEQLGLTWEGKQHRAL 164
Cdd:smart00479 77 FLRGRILVAgNSAHFDLRFLKLEHPRLGIKQPPKLPVIDtLKLARATNPGL-----PKYSLKKLAKRLLLEVIQRAHRAL 151
|
170
....*....|...
gi 872545819 165 ADAENTANILLKV 177
Cdd:smart00479 152 DDARATAKLFKKL 164
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
8-175 |
6.25e-21 |
|
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.
Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 86.59 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 8 IVFDIERN-FRPYKSddpsEIVDIGAVKIEAStMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQ 86
Cdd:cd06127 1 VVFDTETTgLDPKKD----RIIEIGAVKVDGG-IEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 87 FIGeDSIFVSWGRE-DYRFLSHDCTLHGVEcpsMEKERKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWEGKQHRALA 165
Cdd:cd06127 76 FLG-GRVLVAHNASfDLRFLNRELRRLGGP---PLPNPWIDTLRLARRLLPGLRSH--RLGLLLAERYGIPLEGAHRALA 149
|
170
....*....|
gi 872545819 166 DAENTANILL 175
Cdd:cd06127 150 DALATAELLL 159
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
8-174 |
5.11e-20 |
|
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: 84.33 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 8 IVFDIERN-FRPYKSddpsEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLMGIEEFPQIIEKF 84
Cdd:pfam00929 1 VVIDLETTgLDPEKD----EIIEIAAVVIDGGENEIGETFHTYVKPtrLPKLTDECTKFTGITQAMLDNKPSFEEVLEEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 85 IQFIGEDSIFVSWGRE-DYRFLSHDCTLHG-VECPSMEKerKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWEGKQHR 162
Cdd:pfam00929 77 LEFLRKGNLLVAHNASfDVGFLRYDDKRFLkKPMPKLNP--VIDTLILDKATYKELPGR--SLDALAEKLGLEHIGRAHR 152
|
170
....*....|..
gi 872545819 163 ALADAENTANIL 174
Cdd:pfam00929 153 ALDDARATAKLF 164
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
7-210 |
7.36e-18 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 83.35 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIE------RNfrpyksddpSEIVDIGAVKIEasTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQI 80
Cdd:PRK00448 421 YVVFDVEttglsaVY---------DEIIEIGAVKIK--NGEIIDKFEFFIKPGHPLSAFTTELTGITDDMVKDAPSIEEV 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 81 IEKFIQFIGeDSIFVSW-GREDYRFLSHDCTLHG---VECPSMekerkfD---LQKFVfqaYEELFEHtpSLQFAVEQLG 153
Cdd:PRK00448 490 LPKFKEFCG-DSILVAHnASFDVGFINTNYEKLGlekIKNPVI------DtleLSRFL---YPELKSH--RLNTLAKKFG 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 154 LTWEgKQHRALADAENTANILLKVYS---ERDIHKrykrHGELELVENGkltEKAKKKMR 210
Cdd:PRK00448 558 VELE-HHHRADYDAEATAYLLIKFLKdlkEKGITN----LDELNKKLGS---EDAYKKAR 609
|
|
| PRK07748 |
PRK07748 |
3'-5' exonuclease KapD; |
14-205 |
1.61e-17 |
|
3'-5' exonuclease KapD;
Pssm-ID: 236087 Cd Length: 207 Bit Score: 78.96 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 14 RNFRPyksddpsEIVDIGAVKIEASTmkVIGEFSELVKPG--ARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQFIGE- 90
Cdd:PRK07748 23 KGFFP-------EIIEVGLVSVVGCE--VEDTFSSYVKPKtfPSLTERCKSFLGITQEDVDKGISFEELVEKLAEYDKRc 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 91 DSIFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQkfvfqaYEELF--EHTPSLQFAVEQLGLTWEGKQHRALADAE 168
Cdd:PRK07748 94 KPTIVTWGNMDMKVLKHNCEKAGVPFPFKGQCRDLSLE------YKKFFgeRNQTGLWKAIEEYGKEGTGKHHCALDDAM 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 872545819 169 NTANILLKVYSERDIHKRYKRHGELELVENGKLTEKA 205
Cdd:PRK07748 168 TTYNIFKLVEKDKEYLVKPEPPTIGERVDFSKVLKKV 204
|
|
| DNA_pol_III_epsilon_like |
cd06130 |
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with ... |
7-175 |
6.49e-12 |
|
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III; This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains 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. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.
Pssm-ID: 99834 [Multi-domain] Cd Length: 156 Bit Score: 62.14 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERnfrpyKSDDPSEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQ 86
Cdd:cd06130 1 FVAIDFET-----ANADRASACSIGLVKVRDG--QIVDTFYTLIRPPTRFDPFNIAIHGITPEDVADAPTFPEVWPEIKP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 87 FIGeDSIFVSWG-REDYRFLSHDCTLHGVECPSMekeRKFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTWegKQHRALA 165
Cdd:cd06130 74 FLG-GSLVVAHNaSFDRSVLRAALEAYGLPPPPY---QYLCTVRLARRVWPLLPNH--KLNTVAEHLGIEL--NHHDALE 145
|
170
....*....|
gi 872545819 166 DAENTANILL 175
Cdd:cd06130 146 DARACAEILL 155
|
|
| PRK07740 |
PRK07740 |
hypothetical protein; Provisional |
7-184 |
1.67e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236085 [Multi-domain] Cd Length: 244 Bit Score: 62.76 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERN-FRPYKSDdpsEIVDIGAVKIEASTmkVIGE-FSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKF 84
Cdd:PRK07740 61 FVVFDLETTgFSPQQGD---EILSIGAVKTKGGE--VETDtFYSLVKPKRPIPEHILELTGITAEDVAFAPPLAEVLHRF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 85 IQFIGeDSIFVSW-GREDYRFLSHdctlhgveCPSMEKERKF-----DLQKFVFQAYEElfEHTPSLQFAVEQLGLTWEG 158
Cdd:PRK07740 136 YAFIG-AGVLVAHhAGHDKAFLRH--------ALWRTYRQPFthrliDTMFLTKLLAHE--RDFPTLDDALAYYGIPIPR 204
|
170 180
....*....|....*....|....*....
gi 872545819 159 KqHRALADAENTAN---ILLKVYSERDIH 184
Cdd:PRK07740 205 R-HHALGDALMTAKlwaILLVEAQQRGIT 232
|
|
| PRK06309 |
PRK06309 |
DNA polymerase III subunit epsilon; Validated |
46-166 |
4.90e-11 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180524 [Multi-domain] Cd Length: 232 Bit Score: 61.36 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 46 FSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQFIGEDSIFVSWGRE--DYRFLSHDCTLHGVECPSMekeR 123
Cdd:PRK06309 35 FQTLVNPEIPIPAEASKIHGITTDEVADAPKFPEAYQKFIEFCGTDNILVAHNNDafDFPLLRKECRRHGLEPPTL---R 111
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 872545819 124 KFDLQKFVFQAYEELFEHtpSLQFAVEQLGLTwEGKQHRALAD 166
Cdd:PRK06309 112 TIDSLKWAQKYRPDLPKH--NLQYLRQVYGFE-ENQAHRALDD 151
|
|
| PRK08074 |
PRK08074 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
7-176 |
1.90e-10 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236148 [Multi-domain] Cd Length: 928 Bit Score: 61.12 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERNFRPYKSDDpsEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQ 86
Cdd:PRK08074 5 FVVVDLETTGNSPKKGD--KIIQIAAVVVEDG--EILERFSSFVNPERPIPPFITELTGISEEMVKQAPLFEDVAPEIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 87 FIgEDSIFVSWGRE-DYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEELfehtpSLQFAVEQLGLTWEgKQHRALA 165
Cdd:PRK08074 81 LL-EGAYFVAHNVHfDLNFLNEELERAGYTEIHCPKLDTVELARILLPTAESY-----KLRDLSEELGLEHD-QPHRADS 153
|
170
....*....|.
gi 872545819 166 DAENTANILLK 176
Cdd:PRK08074 154 DAEVTAELFLQ 164
|
|
| PRK08517 |
PRK08517 |
3'-5' exonuclease; |
7-174 |
3.44e-10 |
|
3'-5' exonuclease;
Pssm-ID: 236281 [Multi-domain] Cd Length: 257 Bit Score: 58.88 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERN-FRPYKSddpsEIVDIGAVKIEAStmKVIGEFSELVKpGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFI 85
Cdd:PRK08517 70 FCFVDIETNgSKPKKH----QIIEIGAVKVKNG--EIIDRFESFVK-AKEVPEYITELTGITYEDLENAPSLKEVLEEFR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 86 QFIGeDSIFVSWG-REDYRFLSHdctlhgvecpSMEK-------ERKF---DLQKFVFQAYEElfehtpSLQFAVEQLGL 154
Cdd:PRK08517 143 LFLG-DSVFVAHNvNFDYNFISR----------SLEEiglgpllNRKLctiDLAKRTIESPRY------GLSFLKELLGI 205
|
170 180
....*....|....*....|
gi 872545819 155 TWEgKQHRALADAENTANIL 174
Cdd:PRK08517 206 EIE-VHHRAYADALAAYEIF 224
|
|
| PRK07883 |
PRK07883 |
DEDD exonuclease domain-containing protein; |
3-174 |
6.80e-09 |
|
DEDD exonuclease domain-containing protein;
Pssm-ID: 236123 [Multi-domain] Cd Length: 557 Bit Score: 56.08 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 3 NTThFIVFDIERN-FRPyksdDPSEIVDIGAVKIEASTmkVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQII 81
Cdd:PRK07883 14 DVT-FVVVDLETTgGSP----AGDAITEIGAVKVRGGE--VLGEFATLVNPGRPIPPFITVLTGITTAMVAGAPPIEEVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 82 EKFIQFIGeDSIFVSW-GREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVFQAYEelfehTPSLQFA--VEQLGLTWEG 158
Cdd:PRK07883 87 PAFLEFAR-GAVLVAHnAPFDIGFLRAAAARCGYPWPGPPVLCTVRLARRVLPRDE-----APNVRLStlARLFGATTTP 160
|
170
....*....|....*.
gi 872545819 159 KqHRALADAENTANIL 174
Cdd:PRK07883 161 T-HRALDDARATVDVL 175
|
|
| PRK07247 |
PRK07247 |
3'-5' exonuclease; |
1-198 |
1.15e-07 |
|
3'-5' exonuclease;
Pssm-ID: 180906 [Multi-domain] Cd Length: 195 Bit Score: 50.93 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 1 MENTTHFIVFDIERNfrpyKSDDPSEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQI 80
Cdd:PRK07247 1 MKRLETYIAFDLEFN----TVNGVSHIIQVSAVKYDDH--KEVDSFDSYVYTDVPLQSFINGLTGITADKIADAPKVEEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 81 IEKFIQFIGEDSIFvswgreDYRFLSHDCTL---HGVEcpsMEKERKFDLqkfvfqaYEELFEHTPS---------LQFA 148
Cdd:PRK07247 75 LAAFKEFVGELPLI------GYNAQKSDLPIlaeNGLD---LSDQYQVDL-------YDEAFERRSSdlngianlkLQTV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872545819 149 VEQLGLtwEGKQHRALADAENTANILLKvYSERDIHKRYKRHGELELVEN 198
Cdd:PRK07247 139 ADFLGI--KGRGHNSLEDARMTARVYES-FLESDQNKEYLEQQEEVTSDN 185
|
|
| PRK07246 |
PRK07246 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
25-176 |
5.79e-06 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180905 [Multi-domain] Cd Length: 820 Bit Score: 47.37 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 25 SEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQFIgEDSIFVSwgredyrf 104
Cdd:PRK07246 23 ASIIQVGIVIIEGG--EIIDSYTTDVNPHEPLDEHIKHLTGITDQQLAQAPDFSQVARHIYDLI-EDCIFVA-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 105 lshdctlHGVecpsmekerKFDLQKFVFQAYEELFE-HTP------------------SLQFAVEQLGLTWEgKQHRALA 165
Cdd:PRK07246 92 -------HNV---------KFDANLLAEALFLEGYElRTPrvdtvelaqvffptlekySLSHLSRELNIDLA-DAHTAIA 154
|
170
....*....|.
gi 872545819 166 DAENTANILLK 176
Cdd:PRK07246 155 DARATAELFLK 165
|
|
| dnaq |
TIGR00573 |
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ... |
27-178 |
6.01e-06 |
|
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, Degradation of DNA]
Pssm-ID: 129663 [Multi-domain] Cd Length: 217 Bit Score: 46.29 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 27 IVDIGAVKIeASTMKVIGEFSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFIQFIGEDSIFVSWGREDYRFLS 106
Cdd:TIGR00573 25 IIEIGAVEI-INRRITGNKFHTYIKPDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADYIRGAELVIHNASFDVGFLN 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872545819 107 HDCTLhgvECPSMEKERKF-DLQKFVFQAYEELFEHTPSLQFAVEQLGLTwegKQHRALADAENTANILLKVY 178
Cdd:TIGR00573 104 YEFSK---LYKVEPKTNDViDTTDTLQYARPEFPGKRNTLDALCKRYEIT---NSHRALHGALADAFILAKLY 170
|
|
| PRK06807 |
PRK06807 |
3'-5' exonuclease; |
7-194 |
3.60e-05 |
|
3'-5' exonuclease;
Pssm-ID: 235864 [Multi-domain] Cd Length: 313 Bit Score: 44.42 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERN-FRPYKSddpsEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITK---KDLMGIEEfpqIIE 82
Cdd:PRK06807 10 YVVIDFETTgFNPYND----KIIQVAAVKYRNH--ELVDQFVSYVNPERPIPDRITSLTGITNyrvSDAPTIEE---VLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 83 KFIQFIGEDSIFVSWGREDYRFLSHDCTLHGVECPsmeKERKFDlqkfVFQAYEELFEHTPSLQFAVEQLGLTWEGKQHR 162
Cdd:PRK06807 81 LFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLPEP---KNKVID----TVFLAKKYMKHAPNHKLETLKRMLGIRLSSHN 153
|
170 180 190
....*....|....*....|....*....|...
gi 872545819 163 ALADAENTANILLK-VYSERDIHKRYKRHGELE 194
Cdd:PRK06807 154 AFDDCITCAAVYQKcASIEEEAKRKSNKEVLDE 186
|
|
| PTZ00315 |
PTZ00315 |
2'-phosphotransferase; Provisional |
7-174 |
6.07e-05 |
|
2'-phosphotransferase; Provisional
Pssm-ID: 240356 [Multi-domain] Cd Length: 582 Bit Score: 44.11 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 7 FIVFDIERNFRPYKSDDPSEIVDIGAVKIEASTMKVIGEFSELVKP--GARLTRHTTKLTGITKKDLMGIEEFPQIIEKF 84
Cdd:PTZ00315 58 YVVLDFEATCEADRRIEDAEVIEFPMVLVDARTATPVAEFQRYVRPvkNPVLSRFCTELTGITQSMVSRADPFPVVYCEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 85 IQFIGEDSI----------FVSWGREDYR-FLSHDCTLHGVECPSMEKERKFDLQKFVFQ-----AYEELFEHTPSLQFA 148
Cdd:PTZ00315 138 LQFLAEAGLgdapplrsycVVTCGDWDLKtMLPSQMRVSGQQGTPLSFQRWCNLKKYMSQlgfgnGSGCGGGATPPLGPS 217
|
170 180 190
....*....|....*....|....*....|.
gi 872545819 149 -----VEQLGLTWEGKQHRALADAENTANIL 174
Cdd:PTZ00315 218 dmpdmLQMLGLPLQGRHHSGIDDCRNIAAVL 248
|
|
| DNA_pol_III_epsilon_Ecoli_like |
cd06131 |
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III ... |
8-178 |
3.22e-04 |
|
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III and similar proteins; This subfamily is composed of the epsilon subunit of Escherichia coli DNA polymerase III (Pol III) and similar proteins. Pol III is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. It is a holoenzyme complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains 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. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.
Pssm-ID: 99835 [Multi-domain] Cd Length: 167 Bit Score: 40.59 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 8 IVFDIERN-FRPYKSDdpsEIVDIGAVkiEASTMKVIGE-FSELVKPGARLTRHTTKLTGITKKDLMGIEEFPQIIEKFI 85
Cdd:cd06131 2 IVLDTETTgLDPREGH---RIIEIGCV--ELINRRLTGNtFHVYINPERDIPEEAFKVHGITDEFLADKPKFAEIADEFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872545819 86 QFIGEDSIFVSWGREDYRFLSHDCTLHGVECPSMEKERKFDLQKFVfqayEELFEHTP-SLQFAVEQLGLTWEGKQ-HRA 163
Cdd:cd06131 77 DFIRGAELVIHNASFDVGFLNAELSLLGLGKKIIDFCRVIDTLALA----RKKFPGKPnSLDALCKRFGIDNSHRTlHGA 152
|
170
....*....|....*
gi 872545819 164 LADAEntanILLKVY 178
Cdd:cd06131 153 LLDAE----LLAEVY 163
|
|
| |
