|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09146 |
PRK09146 |
DNA polymerase III subunit epsilon; Validated |
13-222 |
2.02e-51 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236392 [Multi-domain] Cd Length: 239 Bit Score: 167.41 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 13 HPIGHW--RFCHRRQRAAQhaptGALRACLGSPLPSARQAVADCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLST 90
Cdd:PRK09146 8 QPALDWpaKFAQKAEQAKD----PRLKRFYAAGLVSPDTPLSEVPFVALDFETTGLDAEQDAIVSIGLVPFTLQRIRCRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 91 ADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDT 170
Cdd:PRK09146 84 ARHWVVKPRRPLEEESVVIHGITHSELQDAPDLERILDELLEALAGKVVVVHYRRIERDFLDQALRNRIGEGIEFPVIDT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174928096 171 LRLAERQLRR---------AGRPIPAdgMRLHTLRGRYNLPQYRAHDALFDALAAGELFAA 222
Cdd:PRK09146 164 MEIEARIQRKqagglwnrlKGKKPES--IRLADSRLRYGLPAYSPHHALTDAIATAELLQA 222
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
55-224 |
6.58e-48 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 155.72 E-value: 6.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 55 RFLAVDLETTGLDPEHDAILSIGWVAMDGVRIdlSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEAL 134
Cdd:COG0847 1 RFVVLDTETTGLDPAKDRIIEIGAVKVDDGRI--VETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 135 QGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRAGRpipadgMRLHTLRGRYNLPQYRAHDALFDAL 214
Cdd:COG0847 79 GGAVLVAHNAAFDLGFLNAELRRAGLPLPPFPVLDTLRLARRLLPGLPS------YSLDALCERLGIPFDERHRALADAE 152
|
170
....*....|
gi 1174928096 215 AAGELFAALV 224
Cdd:COG0847 153 ATAELFLALL 162
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
57-221 |
2.86e-46 |
|
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: 151.30 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 57 LAVDLETTGLDPEHDAILSIGWVAMDGvRIDLSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQG 136
Cdd:cd06127 1 VVFDTETTGLDPKKDRIIEIGAVKVDG-GIEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFLGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 137 RVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRAGRPIPADgmrlhTLRGRYNLPQYRAHDALFDALAA 216
Cdd:cd06127 80 RVLVAHNASFDLRFLNRELRRLGGPPLPNPWIDTLRLARRLLPGLRSHRLGL-----LLAERYGIPLEGAHRALADALAT 154
|
....*
gi 1174928096 217 GELFA 221
Cdd:cd06127 155 AELLL 159
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
55-227 |
4.37e-33 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 117.79 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 55 RFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLSTadQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEAL 134
Cdd:smart00479 1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGEIIEVF--DTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 135 QGRVLVAHH-AALELGFLEEACHRLYGVRPP-LPVVDTLRLAERQLRRAGRpipadgMRLHTLRGRYNLPQY-RAHDALF 211
Cdd:smart00479 79 RGRILVAGNsAHFDLRFLKLEHPRLGIKQPPkLPVIDTLKLARATNPGLPK------YSLKKLAKRLLLEVIqRAHRALD 152
|
170
....*....|....*.
gi 1174928096 212 DALAAGELFAALVSQL 227
Cdd:smart00479 153 DARATAKLFKKLLERL 168
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
57-220 |
1.89e-19 |
|
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: 82.01 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 57 LAVDLETTGLDPEHDAILSIGWVAMDG-VRIDLSTADQrLVRADCP--VPEQSAVIHRITDREAAGGTTVDSALDALFEA 133
Cdd:pfam00929 1 VVIDLETTGLDPEKDEIIEIAAVVIDGgENEIGETFHT-YVKPTRLpkLTDECTKFTGITQAMLDNKPSFEEVLEEFLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQ-GRVLVAHHAALELGFLEEACHRLYGVRPPL--PVVDTLRLAerQLRRAGRPipadGMRLHTLRGRYNLP-QYRAHDA 209
Cdd:pfam00929 80 LRkGNLLVAHNASFDVGFLRYDDKRFLKKPMPKlnPVIDTLILD--KATYKELP----GRSLDALAEKLGLEhIGRAHRA 153
|
170
....*....|.
gi 1174928096 210 LFDALAAGELF 220
Cdd:pfam00929 154 LDDARATAKLF 164
|
|
| dnaq |
TIGR00573 |
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ... |
56-225 |
1.95e-14 |
|
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: 69.79 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 56 FLAVDLETTGLDPEHDaILSIGWVAMDGVRIdlsTADQRLVRA--DCPVPEQSAVIHRITDREAAGGTTVDSALDALFEA 133
Cdd:TIGR00573 9 ETTGDNETTGLYAGHD-IIEIGAVEIINRRI---TGNKFHTYIkpDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQGRVLVAHHAALELGFLEEACHRLYGVRPPL-PVVDTLRLAE--RQLRRAGRpipadgMRLHTLRGRYNLPQYR--AHD 208
Cdd:TIGR00573 85 IRGAELVIHNASFDVGFLNYEFSKLYKVEPKTnDVIDTTDTLQyaRPEFPGKR------NTLDALCKRYEITNSHraLHG 158
|
170
....*....|....*..
gi 1174928096 209 ALFDALAAGELFAALVS 225
Cdd:TIGR00573 159 ALADAFILAKLYLVMTG 175
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09146 |
PRK09146 |
DNA polymerase III subunit epsilon; Validated |
13-222 |
2.02e-51 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236392 [Multi-domain] Cd Length: 239 Bit Score: 167.41 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 13 HPIGHW--RFCHRRQRAAQhaptGALRACLGSPLPSARQAVADCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLST 90
Cdd:PRK09146 8 QPALDWpaKFAQKAEQAKD----PRLKRFYAAGLVSPDTPLSEVPFVALDFETTGLDAEQDAIVSIGLVPFTLQRIRCRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 91 ADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDT 170
Cdd:PRK09146 84 ARHWVVKPRRPLEEESVVIHGITHSELQDAPDLERILDELLEALAGKVVVVHYRRIERDFLDQALRNRIGEGIEFPVIDT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174928096 171 LRLAERQLRR---------AGRPIPAdgMRLHTLRGRYNLPQYRAHDALFDALAAGELFAA 222
Cdd:PRK09146 164 MEIEARIQRKqagglwnrlKGKKPES--IRLADSRLRYGLPAYSPHHALTDAIATAELLQA 222
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
55-224 |
6.58e-48 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 155.72 E-value: 6.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 55 RFLAVDLETTGLDPEHDAILSIGWVAMDGVRIdlSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEAL 134
Cdd:COG0847 1 RFVVLDTETTGLDPAKDRIIEIGAVKVDDGRI--VETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 135 QGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRAGRpipadgMRLHTLRGRYNLPQYRAHDALFDAL 214
Cdd:COG0847 79 GGAVLVAHNAAFDLGFLNAELRRAGLPLPPFPVLDTLRLARRLLPGLPS------YSLDALCERLGIPFDERHRALADAE 152
|
170
....*....|
gi 1174928096 215 AAGELFAALV 224
Cdd:COG0847 153 ATAELFLALL 162
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
57-221 |
2.86e-46 |
|
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: 151.30 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 57 LAVDLETTGLDPEHDAILSIGWVAMDGvRIDLSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQG 136
Cdd:cd06127 1 VVFDTETTGLDPKKDRIIEIGAVKVDG-GIEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFLGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 137 RVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRAGRPIPADgmrlhTLRGRYNLPQYRAHDALFDALAA 216
Cdd:cd06127 80 RVLVAHNASFDLRFLNRELRRLGGPPLPNPWIDTLRLARRLLPGLRSHRLGL-----LLAERYGIPLEGAHRALADALAT 154
|
....*
gi 1174928096 217 GELFA 221
Cdd:cd06127 155 AELLL 159
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
53-227 |
1.86e-45 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 149.91 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 53 DCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRIdlstAD--QRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDAL 130
Cdd:COG2176 7 DLTYVVFDLETTGLSPKKDEIIEIGAVKVENGEI----VDrfSTLVNPGRPIPPFITELTGITDEMVADAPPFEEVLPEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 131 FEALQGRVLVAHHAALELGFLEEACHRLyGVRPPLPVVDTLRLAERQLRRAGRPipadgmRLHTLRGRYNLPQYRAHDAL 210
Cdd:COG2176 83 LEFLGDAVLVAHNASFDLGFLNAALKRL-GLPFDNPVLDTLELARRLLPELKSY------KLDTLAERLGIPLEDRHRAL 155
|
170
....*....|....*..
gi 1174928096 211 FDALAAGELFAALVSQL 227
Cdd:COG2176 156 GDAEATAELFLKLLEKL 172
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
55-227 |
4.37e-33 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 117.79 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 55 RFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLSTadQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEAL 134
Cdd:smart00479 1 TLVVIDCETTGLDPGKDEIIEIAAVDVDGGEIIEVF--DTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 135 QGRVLVAHH-AALELGFLEEACHRLYGVRPP-LPVVDTLRLAERQLRRAGRpipadgMRLHTLRGRYNLPQY-RAHDALF 211
Cdd:smart00479 79 RGRILVAGNsAHFDLRFLKLEHPRLGIKQPPkLPVIDTLKLARATNPGLPK------YSLKKLAKRLLLEVIqRAHRALD 152
|
170
....*....|....*.
gi 1174928096 212 DALAAGELFAALVSQL 227
Cdd:smart00479 153 DARATAKLFKKLLERL 168
|
|
| PRK09145 |
PRK09145 |
3'-5' exonuclease; |
56-223 |
2.99e-25 |
|
3'-5' exonuclease;
Pssm-ID: 236391 [Multi-domain] Cd Length: 202 Bit Score: 98.44 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 56 FLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQ 135
Cdd:PRK09145 31 WVALDCETTGLDPRRAEIVSIAAVKIRGNRILTSERLELLVRPPQSLSAESIKIHRLRHQDLEDGLSEEEALRQLLAFIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 136 GRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRaGRPIPADGMRLHTLRGRYNLPQYRAHDALFDALA 215
Cdd:PRK09145 111 NRPLVGYYLEFDVAMLNRYVRPLLGIPLPNPLIEVSALYYDKKER-HLPDAYIDLRFDAILKHLDLPVLGRHDALNDAIM 189
|
....*...
gi 1174928096 216 AGELFAAL 223
Cdd:PRK09145 190 AALIFLRL 197
|
|
| PRK07883 |
PRK07883 |
DEDD exonuclease domain-containing protein; |
40-229 |
1.22e-20 |
|
DEDD exonuclease domain-containing protein;
Pssm-ID: 236123 [Multi-domain] Cd Length: 557 Bit Score: 90.36 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 40 LGSPLpsarqavADCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRI--DLSTadqrLVRADCPVPEQSAVIHRITDREA 117
Cdd:PRK07883 8 LGTPL-------RDVTFVVVDLETTGGSPAGDAITEIGAVKVRGGEVlgEFAT----LVNPGRPIPPFITVLTGITTAMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 118 AGGTTVDSALDALFEALQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRAGRPipadGMRLHTLRG 197
Cdd:PRK07883 77 AGAPPIEEVLPAFLEFARGAVLVAHNAPFDIGFLRAAAARCGYPWPGPPVLCTVRLARRVLPRDEAP----NVRLSTLAR 152
|
170 180 190
....*....|....*....|....*....|..
gi 1174928096 198 RYNLPQYRAHDALFDALAAGELFAALVSQLSP 229
Cdd:PRK07883 153 LFGATTTPTHRALDDARATVDVLHGLIERLGN 184
|
|
| PRK07740 |
PRK07740 |
hypothetical protein; Provisional |
17-224 |
3.38e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236085 [Multi-domain] Cd Length: 244 Bit Score: 86.26 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 17 HWRFCHRRQRAAQHAPTgalracLGSPLpsarqavADCRFLAVDLETTGLDPEH-DAILSIGWVAMDGVRIDLSTAdQRL 95
Cdd:PRK07740 35 QEAWIRSIQKEAKRDDV------LDIPL-------TDLPFVVFDLETTGFSPQQgDEILSIGAVKTKGGEVETDTF-YSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 96 VRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAE 175
Cdd:PRK07740 101 VKPKRPIPEHILELTGITAEDVAFAPPLAEVLHRFYAFIGAGVLVAHHAGHDKAFLRHALWRTYRQPFTHRLIDTMFLTK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1174928096 176 RQlrragrPIPADGMRLHTLRGRYNLPQYRAHDALFDALAAGELFAALV 224
Cdd:PRK07740 181 LL------AHERDFPTLDDALAYYGIPIPRRHHALGDALMTAKLWAILL 223
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
57-220 |
1.89e-19 |
|
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: 82.01 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 57 LAVDLETTGLDPEHDAILSIGWVAMDG-VRIDLSTADQrLVRADCP--VPEQSAVIHRITDREAAGGTTVDSALDALFEA 133
Cdd:pfam00929 1 VVIDLETTGLDPEKDEIIEIAAVVIDGgENEIGETFHT-YVKPTRLpkLTDECTKFTGITQAMLDNKPSFEEVLEEFLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQ-GRVLVAHHAALELGFLEEACHRLYGVRPPL--PVVDTLRLAerQLRRAGRPipadGMRLHTLRGRYNLP-QYRAHDA 209
Cdd:pfam00929 80 LRkGNLLVAHNASFDVGFLRYDDKRFLKKPMPKlnPVIDTLILD--KATYKELP----GRSLDALAEKLGLEhIGRAHRA 153
|
170
....*....|.
gi 1174928096 210 LFDALAAGELF 220
Cdd:pfam00929 154 LDDARATAKLF 164
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
53-227 |
1.11e-17 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 81.81 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 53 DCRFLAVDLETTGLDPEHDAILSIGWVAM-DGVRIDlstADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALF 131
Cdd:PRK00448 418 DATYVVFDVETTGLSAVYDEIIEIGAVKIkNGEIID---KFEFFIKPGHPLSAFTTELTGITDDMVKDAPSIEEVLPKFK 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 132 EALQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAerqlrRAGRPIpADGMRLHTLRGRYNLPQYRAHDALF 211
Cdd:PRK00448 495 EFCGDSILVAHNASFDVGFINTNYEKLGLEKIKNPVIDTLELS-----RFLYPE-LKSHRLNTLAKKFGVELEHHHRADY 568
|
170
....*....|....*.
gi 1174928096 212 DALAAGELFAALVSQL 227
Cdd:PRK00448 569 DAEATAYLLIKFLKDL 584
|
|
| PRK06310 |
PRK06310 |
DNA polymerase III subunit epsilon; Validated |
53-242 |
1.35e-16 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180525 [Multi-domain] Cd Length: 250 Bit Score: 76.41 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 53 DCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLSTadQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFE 132
Cdd:PRK06310 6 DTEFVCLDCETTGLDVKKDRIIEFAAIRFTFDEVIDSV--EFLINPERVVSAESQRIHHISDAMLRDKPKIAEVFPQIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 133 AL-QGRVLVAHHAALELGFLEEACHRLyGVRPPL---PVVDTLRLAerqlRRAG-RPIPAdgmrLHTLRGRYNLPQYRAH 207
Cdd:PRK06310 84 FFkEGDYIVGHSVGFDLQVLSQESERI-GETFLSkhyYIIDTLRLA----KEYGdSPNNS----LEALAVHFNVPYDGNH 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1174928096 208 DALFDALAAGELFAALVSQLSPEAQvpLERVLFRP 242
Cdd:PRK06310 155 RAMKDVEINIKVFKHLCKRFRTLEQ--LKQILSKP 187
|
|
| PRK08074 |
PRK08074 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
55-236 |
6.18e-15 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236148 [Multi-domain] Cd Length: 928 Bit Score: 73.83 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 55 RFLAVDLETTGLDPEH-DAILSIGWVAM-DGVRID-LSTadqrLVRADCPVPeqsAVIHR---ITDREAAGGTTVDSALD 128
Cdd:PRK08074 4 RFVVVDLETTGNSPKKgDKIIQIAAVVVeDGEILErFSS----FVNPERPIP---PFITEltgISEEMVKQAPLFEDVAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 129 ALFEALQGRVLVAHHAALELGFLEEACHRLyGVRPPL-PVVDTLRLAeRQLrragrpIP-ADGMRLHTLRGRYNLPQYRA 206
Cdd:PRK08074 77 EIVELLEGAYFVAHNVHFDLNFLNEELERA-GYTEIHcPKLDTVELA-RIL------LPtAESYKLRDLSEELGLEHDQP 148
|
170 180 190
....*....|....*....|....*....|
gi 1174928096 207 HDALFDALAAGELFAALVSQLSpeaQVPLE 236
Cdd:PRK08074 149 HRADSDAEVTAELFLQLLNKLE---RLPLV 175
|
|
| dnaq |
TIGR00573 |
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ... |
56-225 |
1.95e-14 |
|
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: 69.79 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 56 FLAVDLETTGLDPEHDaILSIGWVAMDGVRIdlsTADQRLVRA--DCPVPEQSAVIHRITDREAAGGTTVDSALDALFEA 133
Cdd:TIGR00573 9 ETTGDNETTGLYAGHD-IIEIGAVEIINRRI---TGNKFHTYIkpDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQGRVLVAHHAALELGFLEEACHRLYGVRPPL-PVVDTLRLAE--RQLRRAGRpipadgMRLHTLRGRYNLPQYR--AHD 208
Cdd:TIGR00573 85 IRGAELVIHNASFDVGFLNYEFSKLYKVEPKTnDVIDTTDTLQyaRPEFPGKR------NTLDALCKRYEITNSHraLHG 158
|
170
....*....|....*..
gi 1174928096 209 ALFDALAAGELFAALVS 225
Cdd:TIGR00573 159 ALADAFILAKLYLVMTG 175
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
59-244 |
9.93e-14 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 69.34 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 59 VDLETTGLDPEHDAILSIGWVAMDgvriDLSTADQRLVRADCPVPEQSAV-IHRITDREAAGGTTVDSALDALFEALQGR 137
Cdd:PRK06063 20 VDVETSGFRPGQARIISLAVLGLD----ADGNVEQSVVTLLNPGVDPGPThVHGLTAEMLEGQPQFADIAGEVAELLRGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 138 VLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAerqlRRAGRPIPadGMRLHTLRGRYNLPQYRAHDALFDALA-A 216
Cdd:PRK06063 96 TLVAHNVAFDYSFLAAEAERAGAELPVDQVMCTVELA----RRLGLGLP--NLRLETLAAHWGVPQQRPHDALDDARVlA 169
|
170 180
....*....|....*....|....*...
gi 1174928096 217 GELFAALVSQLSPEAQVPLERVlFRPGW 244
Cdd:PRK06063 170 GILRPSLERARERDVWLPLHPV-TRRRW 196
|
|
| PRK06309 |
PRK06309 |
DNA polymerase III subunit epsilon; Validated |
60-242 |
1.15e-13 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180524 [Multi-domain] Cd Length: 232 Bit Score: 67.91 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 60 DLETTGLDPEHDAILSIGwvAMDGVRidlSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQGR-V 138
Cdd:PRK06309 8 DTETTGTQIDKDRIIEIA--AYNGVT---SESFQTLVNPEIPIPAEASKIHGITTDEVADAPKFPEAYQKFIEFCGTDnI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 139 LVAHHA-ALELGFLEEACHRlYGVRPP-LPVVDTLRLAERQlrragRP-IPADGmrLHTLRGRYNLPQYRAHDALFDALA 215
Cdd:PRK06309 83 LVAHNNdAFDFPLLRKECRR-HGLEPPtLRTIDSLKWAQKY-----RPdLPKHN--LQYLRQVYGFEENQAHRALDDVIT 154
|
170 180
....*....|....*....|....*..
gi 1174928096 216 AGELFAALVSQLSPEAQVPLERVLFRP 242
Cdd:PRK06309 155 LHRVFSALVGDLSPQQVYDLLNESCHP 181
|
|
| DNA_pol_III_epsilon_like |
cd06130 |
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with ... |
56-222 |
2.26e-13 |
|
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: 65.61 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 56 FLAVDLETTglDPEHDAILSIGWVAM-DGVRIDLSTadqRLVRadcPVPEQSAV---IHRITDREAAGGTTVDSALDALF 131
Cdd:cd06130 1 FVAIDFETA--NADRASACSIGLVKVrDGQIVDTFY---TLIR---PPTRFDPFniaIHGITPEDVADAPTFPEVWPEIK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 132 EALQGRVLVAHHAALELGFLeEACHRLYGV-RPPLPVVDTLRLAerqlRRAGRPIPadGMRLHTLRGRYNLPqYRAHDAL 210
Cdd:cd06130 73 PFLGGSLVVAHNASFDRSVL-RAALEAYGLpPPPYQYLCTVRLA----RRVWPLLP--NHKLNTVAEHLGIE-LNHHDAL 144
|
170
....*....|..
gi 1174928096 211 FDALAAGELFAA 222
Cdd:cd06130 145 EDARACAEILLA 156
|
|
| PRK07942 |
PRK07942 |
DNA polymerase III subunit epsilon; Provisional |
57-236 |
6.44e-11 |
|
DNA polymerase III subunit epsilon; Provisional
Pssm-ID: 181176 [Multi-domain] Cd Length: 232 Bit Score: 60.38 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 57 LAVDLETTGLDPEHDAILS--IGWVAMDGVRIDLSTAdqrLVRADCPVPEQSAVIHRI-TDREAAGGTTVDSALDALFEA 133
Cdd:PRK07942 9 AAFDLETTGVDPETARIVTaaLVVVDADGEVVESREW---LADPGVEIPEEASAVHGItTEYARAHGRPAAEVLAEIADA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQ-----GRVLVAHHAALELGFLEEACHRlYGVRP--PLPVVDTLRLaERQLRRAGRpipadGMR-LHTLRGRYNLPQYR 205
Cdd:PRK07942 86 LReawarGVPVVVFNAPYDLTVLDRELRR-HGLPSlvPGPVIDPYVI-DKAVDRYRK-----GKRtLTALCEHYGVRLDN 158
|
170 180 190
....*....|....*....|....*....|.
gi 1174928096 206 AHDALFDALAAGELFAALVSQLSPEAQVPLE 236
Cdd:PRK07942 159 AHEATADALAAARVAWALARRFPELAALSPA 189
|
|
| DNA_pol_III_epsilon_Ecoli_like |
cd06131 |
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III ... |
60-223 |
1.62e-10 |
|
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: 57.93 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 60 DLETTGLDPEH-DAILSIGWVAMDGVRIDLSTAdQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEALQGRV 138
Cdd:cd06131 5 DTETTGLDPREgHRIIEIGCVELINRRLTGNTF-HVYINPERDIPEEAFKVHGITDEFLADKPKFAEIADEFLDFIRGAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 139 LVAHHAALELGFLEEACHRLYGVRPPLP---VVDTLRLAERqlRRAGRPIPADGmrlhtLRGRYNLP--QYRAHDALFDA 213
Cdd:cd06131 84 LVIHNASFDVGFLNAELSLLGLGKKIIDfcrVIDTLALARK--KFPGKPNSLDA-----LCKRFGIDnsHRTLHGALLDA 156
|
170
....*....|
gi 1174928096 214 LAAGELFAAL 223
Cdd:cd06131 157 ELLAEVYLEL 166
|
|
| PRK06807 |
PRK06807 |
3'-5' exonuclease; |
56-220 |
7.58e-10 |
|
3'-5' exonuclease;
Pssm-ID: 235864 [Multi-domain] Cd Length: 313 Bit Score: 57.90 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 56 FLAVDLETTGLDPEHDAILSIGWVAMDGVRIdlstADQ--RLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEA 133
Cdd:PRK06807 10 YVVIDFETTGFNPYNDKIIQVAAVKYRNHEL----VDQfvSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLPLFLAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 134 LQGRVLVAHHAALELGFLEEACHRLYGVRPPLPVVDTLRLAERQLRRagrpipADGMRLHTLRgRYNLPQYRAHDALFDA 213
Cdd:PRK06807 86 LHTNVIVAHNASFDMRFLKSNVNMLGLPEPKNKVIDTVFLAKKYMKH------APNHKLETLK-RMLGIRLSSHNAFDDC 158
|
....*..
gi 1174928096 214 LAAGELF 220
Cdd:PRK06807 159 ITCAAVY 165
|
|
| PRK08517 |
PRK08517 |
3'-5' exonuclease; |
44-220 |
1.47e-08 |
|
3'-5' exonuclease;
Pssm-ID: 236281 [Multi-domain] Cd Length: 257 Bit Score: 53.87 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 44 LPSARQAVADCRFLAVDLETTGLDPEHDAILSIGWVAM-DGVRIDlstADQRLVRADcPVPEQSAVIHRITDREAAGGTT 122
Cdd:PRK08517 58 LKTRFTPIKDQVFCFVDIETNGSKPKKHQIIEIGAVKVkNGEIID---RFESFVKAK-EVPEYITELTGITYEDLENAPS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 123 VDSALDALFEALQGRVLVAHHAALELGFLEEACHRlYGVRPPL-PVVDTLRLAERQlrragrpIPADGMRLHTLRGRYNL 201
Cdd:PRK08517 134 LKEVLEEFRLFLGDSVFVAHNVNFDYNFISRSLEE-IGLGPLLnRKLCTIDLAKRT-------IESPRYGLSFLKELLGI 205
|
170
....*....|....*....
gi 1174928096 202 PQYRAHDALFDALAAGELF 220
Cdd:PRK08517 206 EIEVHHRAYADALAAYEIF 224
|
|
| PRK09182 |
PRK09182 |
DNA polymerase III subunit epsilon; Validated |
59-152 |
9.60e-07 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236397 [Multi-domain] Cd Length: 294 Bit Score: 48.82 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 59 VDLETTGLDPEHDAILSIGWVAM----DGVRIDLSTADQRLVRADCPVPEQSAVIHRITDREAAGGTTVDSALDALFEAL 134
Cdd:PRK09182 42 LDTETTGLDPRKDEIIEIGMVAFeyddDGRIGDVLDTFGGLQQPSRPIPPEITRLTGITDEMVAGQTIDPAAVDALIAPA 121
|
90
....*....|....*...
gi 1174928096 135 QgrVLVAHHAALELGFLE 152
Cdd:PRK09182 122 D--LIIAHNAGFDRPFLE 137
|
|
| PRK05711 |
PRK05711 |
DNA polymerase III subunit epsilon; Provisional |
60-176 |
2.09e-06 |
|
DNA polymerase III subunit epsilon; Provisional
Pssm-ID: 235574 [Multi-domain] Cd Length: 240 Bit Score: 47.16 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 60 DLETTGLDPEH-DAILSIGWVAMdgvridlstADQRL--------VRADCPVPEQSAVIHRITDREAAGGTTVDSALDAL 130
Cdd:PRK05711 10 DTETTGLNQREgHRIIEIGAVEL---------INRRLtgrnfhvyIKPDRLVDPEALAVHGITDEFLADKPTFAEVADEF 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1174928096 131 FEALQGRVLVAHHAALELGFLEEACHRLYGVRPPLP----VVDTLRLAER 176
Cdd:PRK05711 81 LDFIRGAELIIHNAPFDIGFMDYEFALLGRDIPKTNtfckVTDTLAMARR 130
|
|
| Orn |
COG1949 |
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification]; |
59-98 |
3.22e-04 |
|
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
Pssm-ID: 441552 Cd Length: 177 Bit Score: 40.09 E-value: 3.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1174928096 59 VDLETTGLDPEHDAILSIGWVAMDGvriDLSTADQRLVRA 98
Cdd:COG1949 7 IDLEMTGLDPETDRIIEIATIVTDS---DLNILAEGPVLV 43
|
|
| Orn |
cd06135 |
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ... |
59-83 |
8.80e-04 |
|
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: 39.07 E-value: 8.80e-04
10 20
....*....|....*....|....*
gi 1174928096 59 VDLETTGLDPEHDAILSIGWVAMDG 83
Cdd:cd06135 4 IDLEMTGLDPEKDRILEIACIITDG 28
|
|
| PRK05359 |
PRK05359 |
oligoribonuclease; Provisional |
59-76 |
3.91e-03 |
|
oligoribonuclease; Provisional
Pssm-ID: 235429 Cd Length: 181 Bit Score: 37.06 E-value: 3.91e-03
|
| PRK05601 |
PRK05601 |
DNA polymerase III subunit epsilon; Validated |
49-151 |
6.10e-03 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235529 [Multi-domain] Cd Length: 377 Bit Score: 37.50 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174928096 49 QAVADCRFLAVDLETTGLDPEHDAILSIGWVAMDGVRIDLSTADQRLVRADCPVPEQsavIHRITDREAAGGTTVDSALD 128
Cdd:PRK05601 41 EAIEAAPFVAVSIQTSGIHPSTSRLITIDAVTLTADGEEVEHFHAVLNPGEDPGPFH---LHGLSAEEFAQGKRFSQILK 117
|
90 100
....*....|....*....|...
gi 1174928096 129 ALFEALQGRVLVAHHAALELGFL 151
Cdd:PRK05601 118 PLDRLIDGRTLILHNAPRTWGFI 140
|
|
| CAF1 |
pfam04857 |
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ... |
44-74 |
7.05e-03 |
|
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.
Pssm-ID: 461457 Cd Length: 375 Bit Score: 37.01 E-value: 7.05e-03
10 20 30
....*....|....*....|....*....|.
gi 1174928096 44 LPSARQAVADCRFLAVDLETTGLDPEHDAIL 74
Cdd:pfam04857 10 LPEILKAIKEADFVAIDLEFTGLGSPWRKSS 40
|
|
|