MULTISPECIES: exonuclease subunit SbcD [Staphylococcus]
Protein Classification
exonuclease SbcCD subunit D( domain architecture ID 11417993)
exonuclease SbcCD subunit D is a component of SbcCD, which is involved in double-strand DNA break detection and repair by homologous recombination and non-homologous end joining of damaged DNA
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
1-266 | 4.14e-64 | |||||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; : Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 204.76 E-value: 4.14e-64
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| SbcD_C | pfam12320 | Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ... |
262-314 | 2.82e-04 | |||||
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria. : Pssm-ID: 463533 Cd Length: 100 Bit Score: 39.59 E-value: 2.82e-04
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| Name | Accession | Description | Interval | E-value | |||||
| SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
1-266 | 4.14e-64 | |||||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 204.76 E-value: 4.14e-64
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| sbcd | TIGR00619 | exonuclease SbcD; All proteins in this family for which functions are known are ... |
1-241 | 5.49e-47 | |||||
exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273178 [Multi-domain] Cd Length: 253 Bit Score: 160.66 E-value: 5.49e-47
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| MPP_Mre11_N | cd00840 | Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
2-234 | 6.95e-30 | |||||
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. Pssm-ID: 277319 [Multi-domain] Cd Length: 186 Bit Score: 113.13 E-value: 6.95e-30
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| PRK10966 | PRK10966 | exonuclease subunit SbcD; Provisional |
1-240 | 2.30e-21 | |||||
exonuclease subunit SbcD; Provisional Pssm-ID: 182871 [Multi-domain] Cd Length: 407 Bit Score: 94.62 E-value: 2.30e-21
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| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
1-131 | 1.40e-08 | |||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 52.22 E-value: 1.40e-08
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| SbcD_C | pfam12320 | Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ... |
262-314 | 2.82e-04 | |||||
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria. Pssm-ID: 463533 Cd Length: 100 Bit Score: 39.59 E-value: 2.82e-04
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| Name | Accession | Description | Interval | E-value | |||||
| SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
1-266 | 4.14e-64 | |||||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 204.76 E-value: 4.14e-64
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| sbcd | TIGR00619 | exonuclease SbcD; All proteins in this family for which functions are known are ... |
1-241 | 5.49e-47 | |||||
exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273178 [Multi-domain] Cd Length: 253 Bit Score: 160.66 E-value: 5.49e-47
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| MPP_Mre11_N | cd00840 | Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
2-234 | 6.95e-30 | |||||
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. Pssm-ID: 277319 [Multi-domain] Cd Length: 186 Bit Score: 113.13 E-value: 6.95e-30
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| PRK10966 | PRK10966 | exonuclease subunit SbcD; Provisional |
1-240 | 2.30e-21 | |||||
exonuclease subunit SbcD; Provisional Pssm-ID: 182871 [Multi-domain] Cd Length: 407 Bit Score: 94.62 E-value: 2.30e-21
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| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
1-131 | 1.40e-08 | |||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 52.22 E-value: 1.40e-08
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| CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
1-126 | 1.42e-07 | |||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 52.00 E-value: 1.42e-07
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| COG2129 | COG2129 | Predicted phosphoesterase, related to the Icc protein [General function prediction only]; |
2-172 | 2.29e-06 | |||||
Predicted phosphoesterase, related to the Icc protein [General function prediction only]; Pssm-ID: 441732 [Multi-domain] Cd Length: 211 Bit Score: 48.09 E-value: 2.29e-06
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| YaeI | COG1408 | Predicted phosphohydrolase, MPP superfamily [General function prediction only]; |
1-86 | 3.72e-05 | |||||
Predicted phosphohydrolase, MPP superfamily [General function prediction only]; Pssm-ID: 441018 [Multi-domain] Cd Length: 268 Bit Score: 44.79 E-value: 3.72e-05
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| SbcD_C | pfam12320 | Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ... |
262-314 | 2.82e-04 | |||||
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria. Pssm-ID: 463533 Cd Length: 100 Bit Score: 39.59 E-value: 2.82e-04
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| MPP_YkuE_C | cd07385 | Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ... |
2-98 | 1.84e-03 | |||||
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. Pssm-ID: 277331 [Multi-domain] Cd Length: 224 Bit Score: 39.19 E-value: 1.84e-03
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| MPP_DNA_pol_II_small_archeal_C | cd07386 | archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small ... |
7-86 | 5.80e-03 | |||||
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small subunit of the archeal DNA polymerase II contains a C-terminal metallophosphatase domain. This domain is thought to be functionally active because the active site residues required for phosphoesterase activity in other members of this superfamily are intact. The archeal replicative DNA polymerases are thought to possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. Pssm-ID: 277332 Cd Length: 243 Bit Score: 38.05 E-value: 5.80e-03
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| Blast search parameters | ||||
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