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Conserved domains on  [gi|518681585|ref|WP_019843278|]
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MULTISPECIES: oligoribonuclease [Dickeya]

Protein Classification

oligoribonuclease( domain architecture ID 10792475)

oligoribonuclease 3'-5' exoribonuclease is responsible for degrading small oligoribonucleotides to mononucleotides

CATH:  3.30.420.10
EC:  3.1.15.-
Gene Ontology:  GO:0034611|GO:0003676|GO:0000175|GO:0046872
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05359 PRK05359
oligoribonuclease; Provisional
 3-180 4.61e-143

oligoribonuclease; Provisional


:

Pssm-ID: 235429  Cd Length: 181  Bit Score: 394.52  E-value: 4.61e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   3 NENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDED 82
Cdd:PRK05359   1 NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLIDRVRASTVSEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  83 AAQRETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNTHQALDD 162
Cdd:PRK05359  81 EAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWKPEILNGFKKQGTHRALAD 160

                        170
                 ....*....|....*...
gi 518681585 163 IRESVAELAYYREHFIQL 180
Cdd:PRK05359 161 IRESIAELKYYREHFFKL 178
 
Name Accession Description Interval E-value
PRK05359 PRK05359
oligoribonuclease; Provisional
 3-180 4.61e-143

oligoribonuclease; Provisional


Pssm-ID: 235429  Cd Length: 181  Bit Score: 394.52  E-value: 4.61e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   3 NENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDED 82
Cdd:PRK05359   1 NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLIDRVRASTVSEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  83 AAQRETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNTHQALDD 162
Cdd:PRK05359  81 EAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWKPEILNGFKKQGTHRALAD 160

                        170
                 ....*....|....*...
gi 518681585 163 IRESVAELAYYREHFIQL 180
Cdd:PRK05359 161 IRESIAELKYYREHFFKL 178
Orn COG1949
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
4-180 1.04e-135

Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];


Pssm-ID: 441552  Cd Length: 177  Bit Score: 375.98  E-value: 1.04e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   4 ENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDA 83
Cdd:COG1949    1 DDNLVWIDLEMTGLDPETDRIIEIATIVTDSDLNILAEGPVLVIHQSDEALDGMDDWNRRMHTKSGLIDRVRASTVTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  84 AQRETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNTHQALDDI 163
Cdd:COG1949   81 AEAQTLAFLKQHVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWYPEVLAGPKKKGGHRALADI 160

                        170
                 ....*....|....*..
gi 518681585 164 RESVAELAYYREHFIQL 180
Cdd:COG1949  161 RESIAELRYYREHFFVL 177
Orn cd06135
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ...
 7-178 6.22e-109

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: 308.32  E-value: 6.22e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   7 LIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDAAQR 86
Cdd:cd06135    1 LVWIDLEMTGLDPEKDRILEIACIITDGDLNIIAEGPELVIHQPDEVLDGMDEWCTEMHTKSGLTERVRASTVTLAQAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  87 ETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEIL-AGFKKRNTHQALDDIRE 165
Cdd:cd06135   81 ELLEFIKKYVPKGKSPLAGNSVHQDRRFLDKYMPELEEYLHYRILDVSSIKELARRWYPEIYrKAPKKKGTHRALDDIRE 160

                        170
                 ....*....|...
gi 518681585 166 SVAELAYYREHFI 178
Cdd:cd06135  161 SIAELKYYRENIF 173
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 8-170 4.84e-46

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: 148.65  E-value: 4.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585    8 IWIDLEMTGLDPERDRIIEIATLVTDANLNVlaEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDAAQRE 87
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGENE--IGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   88 TIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNT---HQALDDIR 164
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMPKLNPVIDTLILDKATYKELPGRSLDALAEKLGLEHIgraHRALDDAR 158


                  ....*.
gi 518681585  165 ESVAEL 170
Cdd:pfam00929 159 ATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 7-177 5.50e-22

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 86.97  E-value: 5.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585     7 LIWIDLEMTGLDPERDRIIEIATLVTDANLnvLAEGPTLAVHqPDSQlalMDDWNVRTHtasGLVERVKASRVDEDAAQR 86
Cdd:smart00479   2 LVVIDCETTGLDPGKDEIIEIAAVDVDGGE--IIEVFDTYVK-PDRP---ITDYATEIH---GITPEMLDDAPTFEEVLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585    87 EtiafLQQWVPaGKSPICGNSIGQDRRFLFRYMPELEA----------YFHYRYLDVS-----TLKELARRWKPEILAgf 151
Cdd:smart00479  73 E----LLEFLR-GRILVAGNSAHFDLRFLKLEHPRLGIkqppklpvidTLKLARATNPglpkySLKKLAKRLLLEVIQ-- 145

                          170       180
                   ....*....|....*....|....*.
gi 518681585   152 kkrNTHQALDDIRESVAELAYYREHF 177
Cdd:smart00479 146 ---RAHRALDDARATAKLFKKLLERL 168
 
Name Accession Description Interval E-value
PRK05359 PRK05359
oligoribonuclease; Provisional
 3-180 4.61e-143

oligoribonuclease; Provisional


Pssm-ID: 235429  Cd Length: 181  Bit Score: 394.52  E-value: 4.61e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   3 NENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDED 82
Cdd:PRK05359   1 NEDNLIWIDLEMTGLDPERDRIIEIATIVTDADLNILAEGPVIAIHQSDEALAAMDEWNTRTHTRSGLIDRVRASTVSEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  83 AAQRETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNTHQALDD 162
Cdd:PRK05359  81 EAEAQTLEFLKQWVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWKPEILNGFKKQGTHRALAD 160

                        170
                 ....*....|....*...
gi 518681585 163 IRESVAELAYYREHFIQL 180
Cdd:PRK05359 161 IRESIAELKYYREHFFKL 178
Orn COG1949
Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];
4-180 1.04e-135

Oligoribonuclease (3'-5' exoribonuclease) [RNA processing and modification];


Pssm-ID: 441552  Cd Length: 177  Bit Score: 375.98  E-value: 1.04e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   4 ENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDA 83
Cdd:COG1949    1 DDNLVWIDLEMTGLDPETDRIIEIATIVTDSDLNILAEGPVLVIHQSDEALDGMDDWNRRMHTKSGLIDRVRASTVTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  84 AQRETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNTHQALDDI 163
Cdd:COG1949   81 AEAQTLAFLKQHVPAGKSPLCGNSIGQDRRFLARYMPELEAYFHYRNLDVSTLKELARRWYPEVLAGPKKKGGHRALADI 160

                        170
                 ....*....|....*..
gi 518681585 164 RESVAELAYYREHFIQL 180
Cdd:COG1949  161 RESIAELRYYREHFFVL 177
Orn cd06135
DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins; Oligoribonuclease ...
 7-178 6.22e-109

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: 308.32  E-value: 6.22e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   7 LIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDAAQR 86
Cdd:cd06135    1 LVWIDLEMTGLDPEKDRILEIACIITDGDLNIIAEGPELVIHQPDEVLDGMDEWCTEMHTKSGLTERVRASTVTLAQAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  87 ETIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEIL-AGFKKRNTHQALDDIRE 165
Cdd:cd06135   81 ELLEFIKKYVPKGKSPLAGNSVHQDRRFLDKYMPELEEYLHYRILDVSSIKELARRWYPEIYrKAPKKKGTHRALDDIRE 160

                        170
                 ....*....|...
gi 518681585 166 SVAELAYYREHFI 178
Cdd:cd06135  161 SIAELKYYRENIF 173
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
 8-170 4.84e-46

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: 148.65  E-value: 4.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585    8 IWIDLEMTGLDPERDRIIEIATLVTDANLNVlaEGPTLAVHQPDSQLALMDDWNVRTHTASGLVERVKASRVDEDAAQRE 87
Cdd:pfam00929   1 VVIDLETTGLDPEKDEIIEIAAVVIDGGENE--IGETFHTYVKPTRLPKLTDECTKFTGITQAMLDNKPSFEEVLEEFLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   88 TIAFLQQWVPAGKSPICGNSIGQDRRFLFRYMPELEAYFHYRYLDVSTLKELARRWKPEILAGFKKRNT---HQALDDIR 164
Cdd:pfam00929  79 FLRKGNLLVAHNASFDVGFLRYDDKRFLKKPMPKLNPVIDTLILDKATYKELPGRSLDALAEKLGLEHIgraHRALDDAR 158


                  ....*.
gi 518681585  165 ESVAEL 170
Cdd:pfam00929 159 ATAKLF 164
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
 7-177 5.50e-22

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


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 86.97  E-value: 5.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585     7 LIWIDLEMTGLDPERDRIIEIATLVTDANLnvLAEGPTLAVHqPDSQlalMDDWNVRTHtasGLVERVKASRVDEDAAQR 86
Cdd:smart00479   2 LVVIDCETTGLDPGKDEIIEIAAVDVDGGE--IIEVFDTYVK-PDRP---ITDYATEIH---GITPEMLDDAPTFEEVLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585    87 EtiafLQQWVPaGKSPICGNSIGQDRRFLFRYMPELEA----------YFHYRYLDVS-----TLKELARRWKPEILAgf 151
Cdd:smart00479  73 E----LLEFLR-GRILVAGNSAHFDLRFLKLEHPRLGIkqppklpvidTLKLARATNPglpkySLKKLAKRLLLEVIQ-- 145

                          170       180
                   ....*....|....*....|....*.
gi 518681585   152 kkrNTHQALDDIRESVAELAYYREHF 177
Cdd:smart00479 146 ---RAHRALDDARATAKLFKKLLERL 168
DEDDh cd06127
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ...
 8-164 6.38e-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: 63.09  E-value: 6.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   8 IWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLaVHQPDSQLAlmddwnvRTHTASGLVERVKASRVDEDAAQRE 87
Cdd:cd06127    1 VVFDTETTGLDPKKDRIIEIGAVKVDGGIEIVERFETL-VNPGRPIPP-------EATAIHGITDEMLADAPPFEEVLPE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585  88 TIAFLqqwvpaGKSPICGNSIGQDRRFLFRYMPELEAY-FHYRYLDVStlkELARRWKPEI-----------LAGFKKRN 155
Cdd:cd06127   73 FLEFL------GGRVLVAHNASFDLRFLNRELRRLGGPpLPNPWIDTL---RLARRLLPGLrshrlglllaeRYGIPLEG 143


                 ....*....
gi 518681585 156 THQALDDIR 164
Cdd:cd06127  144 AHRALADAL 152
ExoI_N cd06138
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar ...
 8-39 3.97e-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: 44.95  E-value: 3.97e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 518681585   8 IWIDLEMTGLDPERDRIIEIATLVTDANLNVL 39
Cdd:cd06138    1 LFYDYETFGLNPSFDQILQFAAIRTDENFNEI 32
PolC COG2176
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ...
 10-28 3.36e-05

DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];


Pssm-ID: 441779 [Multi-domain]  Cd Length: 181  Bit Score: 42.44  E-value: 3.36e-05
                         10
                 ....*....|....*....
gi 518681585  10 IDLEMTGLDPERDRIIEIA 28
Cdd:COG2176   13 FDLETTGLSPKKDEIIEIG 31
DnaQ COG0847
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ...
 10-28 9.95e-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: 40.93  E-value: 9.95e-05
                         10
                 ....*....|....*....
gi 518681585  10 IDLEMTGLDPERDRIIEIA 28
Cdd:COG0847    5 LDTETTGLDPAKDRIIEIG 23
PRK09145 PRK09145
3'-5' exonuclease;
3-136 3.88e-04

3'-5' exonuclease;


Pssm-ID: 236391 [Multi-domain]  Cd Length: 202  Bit Score: 39.50  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518681585   3 NENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAEGPTLAVHQPDSqlalMDDWNVRTHtasGLVERVKASRVDED 82
Cdd:PRK09145  27 PPDEWVALDCETTGLDPRRAEIVSIAAVKIRGNRILTSERLELLVRPPQS----LSAESIKIH---RLRHQDLEDGLSEE 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518681585  83 AAQRETIAFLqqwvpaGKSPICGNSIGQDRRFLFRYM-PELEAYFHYRYLDVSTL 136
Cdd:PRK09145 100 EALRQLLAFI------GNRPLVGYYLEFDVAMLNRYVrPLLGIPLPNPLIEVSAL 148
PRK06310 PRK06310
DNA polymerase III subunit epsilon; Validated
 1-30 3.96e-04

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180525 [Multi-domain]  Cd Length: 250  Bit Score: 39.81  E-value: 3.96e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 518681585   1 MVNENNLIWIDLEMTGLDPERDRIIEIATL 30
Cdd:PRK06310   3 LLKDTEFVCLDCETTGLDVKKDRIIEFAAI 32
SbcB COG2925
Exonuclease I (degrades ssDNA) [Replication, recombination and repair];
9-41 5.98e-04

Exonuclease I (degrades ssDNA) [Replication, recombination and repair];


Pssm-ID: 442169 [Multi-domain]  Cd Length: 474  Bit Score: 39.34  E-value: 5.98e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 518681585   9 WIDLEMTGLDPERDRIIEIATLVTDANLNVLAE 41
Cdd:COG2925    6 WHDYETFGADPRRDRPAQFAGIRTDADLNIIGE 38
sbcB PRK11779
exonuclease I; Provisional
 1-41 7.86e-04

exonuclease I; Provisional


Pssm-ID: 236979 [Multi-domain]  Cd Length: 476  Bit Score: 39.05  E-value: 7.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 518681585   1 MVNENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNVLAE 41
Cdd:PRK11779   2 KKMQPTFLWHDYETFGANPALDRPAQFAGIRTDADLNIIGE 42
PRK09182 PRK09182
DNA polymerase III subunit epsilon; Validated
 8-28 6.51e-03

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 236397 [Multi-domain]  Cd Length: 294  Bit Score: 36.11  E-value: 6.51e-03
                         10        20
                 ....*....|....*....|.
gi 518681585   8 IWIDLEMTGLDPERDRIIEIA 28
Cdd:PRK09182  40 VILDTETTGLDPRKDEIIEIG 60
PRK06063 PRK06063
DEDDh family exonuclease;
10-38 7.40e-03

DEDDh family exonuclease;


Pssm-ID: 180377 [Multi-domain]  Cd Length: 313  Bit Score: 36.22  E-value: 7.40e-03
                         10        20
                 ....*....|....*....|....*....
gi 518681585  10 IDLEMTGLDPERDRIIEIATLVTDANLNV 38
Cdd:PRK06063  20 VDVETSGFRPGQARIISLAVLGLDADGNV 48
 
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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