Exonuclease mut-7 [Caenorhabditis elegans]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| mut-7_like_exo | cd06146 | DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ... |
404-602 | 6.37e-77 | ||||
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. : Pssm-ID: 176655 Cd Length: 193 Bit Score: 248.75 E-value: 6.37e-77
|
||||||||
| PIN_Mut7-C-like | cd18772 | Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the ... |
667-756 | 3.41e-26 | ||||
Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related proteins; This Mut7-C-like subgroup of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. : Pssm-ID: 350854 Cd Length: 81 Bit Score: 102.82 E-value: 3.41e-26
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| mut-7_like_exo | cd06146 | DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ... |
404-602 | 6.37e-77 | ||||
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Pssm-ID: 176655 Cd Length: 193 Bit Score: 248.75 E-value: 6.37e-77
|
||||||||
| DNA_pol_A_exo1 | pfam01612 | 3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ... |
404-605 | 2.06e-41 | ||||
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome. Pssm-ID: 396266 [Multi-domain] Cd Length: 173 Bit Score: 149.37 E-value: 2.06e-41
|
||||||||
| PIN_Mut7-C-like | cd18772 | Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the ... |
667-756 | 3.41e-26 | ||||
Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related proteins; This Mut7-C-like subgroup of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Pssm-ID: 350854 Cd Length: 81 Bit Score: 102.82 E-value: 3.41e-26
|
||||||||
| 35EXOc | smart00474 | 3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ... |
430-605 | 7.63e-23 | ||||
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes Pssm-ID: 214681 [Multi-domain] Cd Length: 172 Bit Score: 96.27 E-value: 7.63e-23
|
||||||||
| Rnd | COG0349 | Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
450-589 | 1.74e-10 | ||||
Ribonuclease D [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 63.74 E-value: 1.74e-10
|
||||||||
| Mut7-C | pfam01927 | Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C ... |
665-775 | 4.25e-08 | ||||
Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus. Pssm-ID: 426515 Cd Length: 146 Bit Score: 53.03 E-value: 4.25e-08
|
||||||||
| Mut7-C | COG1656 | Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function ... |
668-776 | 4.47e-05 | ||||
Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function prediction only]; Pssm-ID: 441262 Cd Length: 155 Bit Score: 44.47 E-value: 4.47e-05
|
||||||||
| rnd | TIGR01388 | ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ... |
560-643 | 6.16e-04 | ||||
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing] Pssm-ID: 130455 [Multi-domain] Cd Length: 367 Bit Score: 43.22 E-value: 6.16e-04
|
||||||||
| PRK10829 | PRK10829 | ribonuclease D; Provisional |
560-589 | 4.05e-03 | ||||
ribonuclease D; Provisional Pssm-ID: 236771 [Multi-domain] Cd Length: 373 Bit Score: 40.37 E-value: 4.05e-03
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| mut-7_like_exo | cd06146 | DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ... |
404-602 | 6.37e-77 | ||||
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Pssm-ID: 176655 Cd Length: 193 Bit Score: 248.75 E-value: 6.37e-77
|
||||||||
| DNA_pol_A_exo1 | pfam01612 | 3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ... |
404-605 | 2.06e-41 | ||||
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome. Pssm-ID: 396266 [Multi-domain] Cd Length: 173 Bit Score: 149.37 E-value: 2.06e-41
|
||||||||
| PIN_Mut7-C-like | cd18772 | Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the ... |
667-756 | 3.41e-26 | ||||
Mut7-C-like family of the PIN domain superfamily similar to the PIN domain found at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related proteins; This Mut7-C-like subgroup of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Pssm-ID: 350854 Cd Length: 81 Bit Score: 102.82 E-value: 3.41e-26
|
||||||||
| 35EXOc | smart00474 | 3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ... |
430-605 | 7.63e-23 | ||||
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes Pssm-ID: 214681 [Multi-domain] Cd Length: 172 Bit Score: 96.27 E-value: 7.63e-23
|
||||||||
| WRN_exo | cd06141 | DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ... |
407-601 | 5.81e-21 | ||||
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability. Pssm-ID: 176653 [Multi-domain] Cd Length: 170 Bit Score: 90.72 E-value: 5.81e-21
|
||||||||
| PIN_Mut7-C-like | cd18670 | PIN domain at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related domains; ... |
667-756 | 1.15e-17 | ||||
PIN domain at the C-terminus of Caenorhabditis elegans exonuclease Mut-7 and related domains; The Mut7-C-like family of the PIN domain superfamily includes the C-terminal domain of Caenorhabditis elegans Mut-7 (also known as exonuclease 3'-5' domain-containing protein 3 homolog). Mut-7 is involved in RNA interference (RNAi) and transposon silencing in C. elegans. The Mut7-C PIN domain family is recognized as a genuine PIN domain, however it is not included it in the CDD PIN domain superfamily hierarchical model as it is lacks a core strand and helix (H3 and S3). The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Other PIN domain families are: the FEN-like PIN domain family which includes the PIN domains of Flap endonuclease-1 (FEN1), Exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and, rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. Matelska et al. recently classified PIN-like domains into distinct groups, this family includes some sequences belonging to two of these, PIN _10 and PIN_16. Pssm-ID: 350850 Cd Length: 65 Bit Score: 78.00 E-value: 1.15e-17
|
||||||||
| RNaseD_exo | cd06142 | DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ... |
450-611 | 1.19e-14 | ||||
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D is a bacterial enzyme involved in the maturation of small stable RNAs and the 3' maturation of tRNA. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. In vivo, RNase D only becomes essential upon removal of other ribonucleases. Eukaryotic RNase D homologs include yeast Rrp6p, human PM/Scl-100, and the Drosophila melanogaster egalitarian protein. Pssm-ID: 176654 [Multi-domain] Cd Length: 178 Bit Score: 72.95 E-value: 1.19e-14
|
||||||||
| RNaseD_like | cd06129 | DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ... |
412-600 | 3.11e-14 | ||||
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group is composed of RNase D, WRN, and similar proteins. They contain a DEDDy-type, DnaQ-like, 3'-5' exonuclease domain that contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase D is involved in the 3'-end processing of tRNA precursors. RNase D-like proteins in eukaryotes include yeast Rrp6p, human PM/Scl-100 and Drosophila melanogaster egalitarian (Egl) protein. WRN is a unique DNA helicase possessing exonuclease activity. Mutation in the WRN gene is implicated in Werner syndrome, a disease associated with premature aging and increased predisposition to cancer. Yeast Rrp6p and the human Polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100) are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Egl is a component of an mRNA-binding complex which is required for oocyte specification. The Egl subfamily does not possess a completely conserved YX(3)D pattern at the ExoIII motif. Pssm-ID: 176650 [Multi-domain] Cd Length: 161 Bit Score: 71.39 E-value: 3.11e-14
|
||||||||
| Rnd | COG0349 | Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
450-589 | 1.74e-10 | ||||
Ribonuclease D [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 63.74 E-value: 1.74e-10
|
||||||||
| Mut7-C | pfam01927 | Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C ... |
665-775 | 4.25e-08 | ||||
Mut7-C RNAse domain; RNAse domain of the PIN fold with an inserted Zinc Ribbon at the C terminus. Pssm-ID: 426515 Cd Length: 146 Bit Score: 53.03 E-value: 4.25e-08
|
||||||||
| DEDDy_polA_RNaseD_like_exo | cd09018 | DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ... |
432-600 | 3.66e-06 | ||||
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; DEDDy 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. They contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDy exonucleases are classified as such because of the presence of a specific YX(3)D pattern at ExoIII. The four conserved acidic residues serve as ligands for the two metal ions required for catalysis. This family of DEDDy exonucleases includes the proofreading domains of family A DNA polymerases, as well as RNases such as RNase D and yeast Rrp6p. The Egalitarian (Egl) and Bacillus-like DNA Polymerase I subfamilies do not possess a completely conserved YX(3)D pattern at the ExoIII motif. In addition, the Bacillus-like DNA polymerase I subfamily has inactive 3'-5' exonuclease domains which do not possess the metal-binding residues necessary for activity. Pssm-ID: 176656 [Multi-domain] Cd Length: 150 Bit Score: 47.62 E-value: 3.66e-06
|
||||||||
| Mut7-C | COG1656 | Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function ... |
668-776 | 4.47e-05 | ||||
Uncharacterized conserved protein, contains PIN-related Mut7-C RNAse domain [General function prediction only]; Pssm-ID: 441262 Cd Length: 155 Bit Score: 44.47 E-value: 4.47e-05
|
||||||||
| rnd | TIGR01388 | ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA ... |
560-643 | 6.16e-04 | ||||
ribonuclease D; This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing] Pssm-ID: 130455 [Multi-domain] Cd Length: 367 Bit Score: 43.22 E-value: 6.16e-04
|
||||||||
| PRK10829 | PRK10829 | ribonuclease D; Provisional |
560-589 | 4.05e-03 | ||||
ribonuclease D; Provisional Pssm-ID: 236771 [Multi-domain] Cd Length: 373 Bit Score: 40.37 E-value: 4.05e-03
|
||||||||
| Blast search parameters | ||||
|
