|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05359 |
PRK05359 |
oligoribonuclease; Provisional |
4-181 |
1.74e-141 |
|
oligoribonuclease; Provisional
Pssm-ID: 235429 Cd Length: 181 Bit Score: 390.67 E-value: 1.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 4 DENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDR 83
Cdd:PRK05359 1 NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLIDRVRASTVSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 84 EAELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGTHQAMDD 163
Cdd:PRK05359 81 EAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWKPEILNGFKKQGTHRALAD 160
|
170
....*....|....*...
gi 578181814 164 IRESVAELSYYRENFIKL 181
Cdd:PRK05359 161 IRESIAELKYYREHFFKL 178
|
|
| Orn |
COG1949 |
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification]; |
5-181 |
3.94e-134 |
|
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
Pssm-ID: 441552 Cd Length: 177 Bit Score: 372.13 E-value: 3.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 5 ENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDRE 84
Cdd:COG1949 1 DDNLVWIDLEMTGLDPETDRIIEIATIVTDSDLNILAEGPVLVIHQSDEALDGMDDWNRRMHTKSGLIDRVRASTVTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 85 AELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGTHQAMDDI 164
Cdd:COG1949 81 AEAQTLAFLKQHVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWYPEVLAGPKKKGGHRALADI 160
|
170
....*....|....*..
gi 578181814 165 RESVAELSYYRENFIKL 181
Cdd:COG1949 161 RESIAELRYYREHFFVL 177
|
|
| Orn |
cd06135 |
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ... |
8-179 |
1.78e-108 |
|
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. 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. Orn is essential for Escherichia coli survival. The human homolog, also called Sfn (small fragment nuclease), is able to hydrolyze short single-stranded RNA and DNA oligomers. It plays a role in cellular nucleotide recycling.
Pssm-ID: 99838 [Multi-domain] Cd Length: 173 Bit Score: 307.17 E-value: 1.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 8 LIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDREAEL 87
Cdd:cd06135 1 LVWIDLEMTGLDPEKDRILEIACIITDGDLNIIAEGPELVIHQPDEVLDGMDEWCTEMHTKSGLTERVRASTVTLAQAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 88 ATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILD-GFKKQGTHQAMDDIRE 166
Cdd:cd06135 81 ELLEFIKKYVPKGKSPLAGNSVHQDRRFLDKYMPELEEYLHYRILDVSSIKELARRWYPEIYRkAPKKKGTHRALDDIRE 160
|
170
....*....|...
gi 578181814 167 SVAELSYYRENFI 179
Cdd:cd06135 161 SIAELKYYRENIF 173
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
9-171 |
5.57e-48 |
|
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: 153.66 E-value: 5.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 9 IWIDLEMTGLDPERDRIIEIATLVTDANLNilAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDREAELA 88
Cdd:pfam00929 1 VVIDLETTGLDPEKDEIIEIAAVVIDGGEN--EIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 89 TLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGT---HQAMDDIR 165
Cdd:pfam00929 79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMPKLNPVIDTLILDKATYKELPGRSLDALAEKLGLEHIgraHRALDDAR 158
|
....*.
gi 578181814 166 ESVAEL 171
Cdd:pfam00929 159 ATAKLF 164
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
8-178 |
2.44e-20 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 82.73 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 8 LIWIDLEMTGLDPERDRIIEIATLVTDanlnilaeGPTIAVHQSD--DQLALMDEWNVRTHtgsGLVER--VKASTFGDr 83
Cdd:smart00479 2 LVVIDCETTGLDPGKDEIIEIAAVDVD--------GGEIIEVFDTyvKPDRPITDYATEIH---GITPEmlDDAPTFEE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 84 eaelaTLEFLKQWVPaGKSPICGNSIGQDRRFLFKYMPELES----------YFHYRYLDVS-----TLKELARRWKPEI 148
Cdd:smart00479 70 -----VLEELLEFLR-GRILVAGNSAHFDLRFLKLEHPRLGIkqppklpvidTLKLARATNPglpkySLKKLAKRLLLEV 143
|
170 180 190
....*....|....*....|....*....|
gi 578181814 149 LdgfkkQGTHQAMDDIRESVAELSYYRENF 178
Cdd:smart00479 144 I-----QRAHRALDDARATAKLFKKLLERL 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05359 |
PRK05359 |
oligoribonuclease; Provisional |
4-181 |
1.74e-141 |
|
oligoribonuclease; Provisional
Pssm-ID: 235429 Cd Length: 181 Bit Score: 390.67 E-value: 1.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 4 DENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDR 83
Cdd:PRK05359 1 NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLIDRVRASTVSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 84 EAELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGTHQAMDD 163
Cdd:PRK05359 81 EAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWKPEILNGFKKQGTHRALAD 160
|
170
....*....|....*...
gi 578181814 164 IRESVAELSYYRENFIKL 181
Cdd:PRK05359 161 IRESIAELKYYREHFFKL 178
|
|
| Orn |
COG1949 |
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification]; |
5-181 |
3.94e-134 |
|
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
Pssm-ID: 441552 Cd Length: 177 Bit Score: 372.13 E-value: 3.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 5 ENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDRE 84
Cdd:COG1949 1 DDNLVWIDLEMTGLDPETDRIIEIATIVTDSDLNILAEGPVLVIHQSDEALDGMDDWNRRMHTKSGLIDRVRASTVTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 85 AELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGTHQAMDDI 164
Cdd:COG1949 81 AEAQTLAFLKQHVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWYPEVLAGPKKKGGHRALADI 160
|
170
....*....|....*..
gi 578181814 165 RESVAELSYYRENFIKL 181
Cdd:COG1949 161 RESIAELRYYREHFFVL 177
|
|
| Orn |
cd06135 |
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ... |
8-179 |
1.78e-108 |
|
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. 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. Orn is essential for Escherichia coli survival. The human homolog, also called Sfn (small fragment nuclease), is able to hydrolyze short single-stranded RNA and DNA oligomers. It plays a role in cellular nucleotide recycling.
Pssm-ID: 99838 [Multi-domain] Cd Length: 173 Bit Score: 307.17 E-value: 1.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 8 LIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDREAEL 87
Cdd:cd06135 1 LVWIDLEMTGLDPEKDRILEIACIITDGDLNIIAEGPELVIHQPDEVLDGMDEWCTEMHTKSGLTERVRASTVTLAQAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 88 ATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILD-GFKKQGTHQAMDDIRE 166
Cdd:cd06135 81 ELLEFIKKYVPKGKSPLAGNSVHQDRRFLDKYMPELEEYLHYRILDVSSIKELARRWYPEIYRkAPKKKGTHRALDDIRE 160
|
170
....*....|...
gi 578181814 167 SVAELSYYRENFI 179
Cdd:cd06135 161 SIAELKYYRENIF 173
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
9-171 |
5.57e-48 |
|
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: 153.66 E-value: 5.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 9 IWIDLEMTGLDPERDRIIEIATLVTDANLNilAEGPTIAVHQSDDQLALMDEWNVRTHTGSGLVERVKASTFGDREAELA 88
Cdd:pfam00929 1 VVIDLETTGLDPEKDEIIEIAAVVIDGGEN--EIGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 89 TLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELESYFHYRYLDVSTLKELARRWKPEILDGFKKQGT---HQAMDDIR 165
Cdd:pfam00929 79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMPKLNPVIDTLILDKATYKELPGRSLDALAEKLGLEHIgraHRALDDAR 158
|
....*.
gi 578181814 166 ESVAEL 171
Cdd:pfam00929 159 ATAKLF 164
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
8-178 |
2.44e-20 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 82.73 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 8 LIWIDLEMTGLDPERDRIIEIATLVTDanlnilaeGPTIAVHQSD--DQLALMDEWNVRTHtgsGLVER--VKASTFGDr 83
Cdd:smart00479 2 LVVIDCETTGLDPGKDEIIEIAAVDVD--------GGEIIEVFDTyvKPDRPITDYATEIH---GITPEmlDDAPTFEE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 84 eaelaTLEFLKQWVPaGKSPICGNSIGQDRRFLFKYMPELES----------YFHYRYLDVS-----TLKELARRWKPEI 148
Cdd:smart00479 70 -----VLEELLEFLR-GRILVAGNSAHFDLRFLKLEHPRLGIkqppklpvidTLKLARATNPglpkySLKKLAKRLLLEV 143
|
170 180 190
....*....|....*....|....*....|
gi 578181814 149 LdgfkkQGTHQAMDDIRESVAELSYYRENF 178
Cdd:smart00479 144 I-----QRAHRALDDARATAKLFKKLLERL 168
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
9-165 |
2.50e-13 |
|
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: 64.24 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 9 IWIDLEMTGLDPERDRIIEIATLVTDANLNILAEG-----PTIAVHQSddqlalmdewnVRTHTGSGLVERVKASTFgdR 83
Cdd:cd06127 1 VVFDTETTGLDPKKDRIIEIGAVKVDGGIEIVERFetlvnPGRPIPPE-----------ATAIHGITDEMLADAPPF--E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 84 EAELATLEFLKQwvpagkSPICGNSIGQDRRFLFKYMPELESY-FHYRYLDVSTL-KELARRWKPEILD-------GFKK 154
Cdd:cd06127 68 EVLPEFLEFLGG------RVLVAHNASFDLRFLNRELRRLGGPpLPNPWIDTLRLaRRLLPGLRSHRLGlllaeryGIPL 141
|
170
....*....|.
gi 578181814 155 QGTHQAMDDIR 165
Cdd:cd06127 142 EGAHRALADAL 152
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
1-29 |
2.56e-06 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 45.52 E-value: 2.56e-06
10 20 30
....*....|....*....|....*....|.
gi 578181814 1 MSADENNLIW--IDLEMTGLDPERDRIIEIA 29
Cdd:COG2176 1 MSLDLEDLTYvvFDLETTGLSPKKDEIIEIG 31
|
|
| ExoI_N |
cd06138 |
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar ... |
9-40 |
2.69e-06 |
|
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar proteins; This subfamily is composed of the N-terminal domain of Escherichia coli exonuclease I (ExoI) and similar proteins. ExoI is a monomeric enzyme that hydrolyzes single stranded DNA in the 3' to 5' direction. It plays a role in DNA recombination and repair. It primarily functions in repairing frameshift mutations. The N-terminal domain of ExoI is a DEDDh-type DnaQ-like 3'-5 exonuclease 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. The ExoI structure is unique among DnaQ family enzymes in that there is a large distance between the two metal ions required for catalysis and the catalytic histidine is oriented away from the active site.
Pssm-ID: 99841 [Multi-domain] Cd Length: 183 Bit Score: 45.33 E-value: 2.69e-06
10 20 30
....*....|....*....|....*....|..
gi 578181814 9 IWIDLEMTGLDPERDRIIEIATLVTDANLNIL 40
Cdd:cd06138 1 LFYDYETFGLNPSFDQILQFAAIRTDENFNEI 32
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
11-165 |
1.51e-05 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 43.24 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 11 IDLEMTGLDPERDRIIEIA-------TLVTDANLNILAEGP----TIAVHQ-SDDQLAlmdewnvrthtgsglvervKAS 78
Cdd:COG0847 5 LDTETTGLDPAKDRIIEIGavkvddgRIVETFHTLVNPERPippeATAIHGiTDEDVA-------------------DAP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578181814 79 TFGDREAELatLEFLKqwvpagKSPICGNSIGQDRRFLFKYMPEL-ESYFHYRYLDvsTLKeLARRWKPEI----LD--- 150
Cdd:COG0847 66 PFAEVLPEL--LEFLG------GAVLVAHNAAFDLGFLNAELRRAgLPLPPFPVLD--TLR-LARRLLPGLpsysLDalc 134
|
170
....*....|....*...
gi 578181814 151 ---GFKKQGTHQAMDDIR 165
Cdd:COG0847 135 erlGIPFDERHRALADAE 152
|
|
| sbcB |
PRK11779 |
exonuclease I; Provisional |
1-55 |
2.23e-05 |
|
exonuclease I; Provisional
Pssm-ID: 236979 [Multi-domain] Cd Length: 476 Bit Score: 43.67 E-value: 2.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578181814 1 MSADENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQL 55
Cdd:PRK11779 1 DKKMQPTFLWHDYETFGANPALDRPAQFAGIRTDADLNIIGEPLVFYCKPADDYL 55
|
|
| SbcB |
COG2925 |
Exonuclease I (degrades ssDNA) [Replication, recombination and repair]; |
10-55 |
8.00e-05 |
|
Exonuclease I (degrades ssDNA) [Replication, recombination and repair];
Pssm-ID: 442169 [Multi-domain] Cd Length: 474 Bit Score: 42.04 E-value: 8.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578181814 10 WIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDDQL 55
Cdd:COG2925 6 WHDYETFGADPRRDRPAQFAGIRTDADLNIIGEPLVLYCKPADDYL 51
|
|
| PRK06310 |
PRK06310 |
DNA polymerase III subunit epsilon; Validated |
5-31 |
4.95e-04 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180525 [Multi-domain] Cd Length: 250 Bit Score: 39.43 E-value: 4.95e-04
10 20
....*....|....*....|....*..
gi 578181814 5 ENNLIWIDLEMTGLDPERDRIIEIATL 31
Cdd:PRK06310 6 DTEFVCLDCETTGLDVKKDRIIEFAAI 32
|
|
| PRK09182 |
PRK09182 |
DNA polymerase III subunit epsilon; Validated |
9-29 |
5.23e-03 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236397 [Multi-domain] Cd Length: 294 Bit Score: 36.49 E-value: 5.23e-03
|
| PRK09145 |
PRK09145 |
3'-5' exonuclease; |
5-50 |
7.24e-03 |
|
3'-5' exonuclease;
Pssm-ID: 236391 [Multi-domain] Cd Length: 202 Bit Score: 35.65 E-value: 7.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578181814 5 ENNLIWIDLEMTGLDPERDRIIEIAT-------LVTDANLNILAEGP------TIAVHQ 50
Cdd:PRK09145 28 PDEWVALDCETTGLDPRRAEIVSIAAvkirgnrILTSERLELLVRPPqslsaeSIKIHR 86
|
|
| PRK07942 |
PRK07942 |
DNA polymerase III subunit epsilon; Provisional |
1-36 |
9.69e-03 |
|
DNA polymerase III subunit epsilon; Provisional
Pssm-ID: 181176 [Multi-domain] Cd Length: 232 Bit Score: 35.34 E-value: 9.69e-03
10 20 30
....*....|....*....|....*....|....*.
gi 578181814 1 MSADENNLIWIDLEMTGLDPERDRIIEIATLVTDAN 36
Cdd:PRK07942 1 MSWHPGPLAAFDLETTGVDPETARIVTAALVVVDAD 36
|
|
| |
