endonuclease MutS2 [Megasphaera sp.]
Protein Classification
endonuclease MutS2( domain architecture ID 11439775)
endonuclease MutS2 is a dsDNA-specific endonuclease/ATPase involved in the suppression of homologous recombination; may play a role in the control of bacterial genetic diversity
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||
| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-787 | 0e+00 | |||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; : Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 951.51 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||||
| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-787 | 0e+00 | |||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 951.51 E-value: 0e+00
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
1-787 | 0e+00 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 677.70 E-value: 0e+00
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| mutS2 | TIGR01069 | MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
1-786 | 0e+00 | |||||||||||
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other] Pssm-ID: 130141 [Multi-domain] Cd Length: 771 Bit Score: 553.66 E-value: 0e+00
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| ABC_MutS2 | cd03280 | ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
300-497 | 4.08e-105 | |||||||||||
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 320.73 E-value: 4.08e-105
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
327-507 | 8.78e-67 | |||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 219.35 E-value: 8.78e-67
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
328-508 | 1.44e-32 | |||||||||||
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters. Pssm-ID: 425714 [Multi-domain] Cd Length: 188 Bit Score: 124.61 E-value: 1.44e-32
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| Name | Accession | Description | Interval | E-value | |||||||||||
| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-787 | 0e+00 | |||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 951.51 E-value: 0e+00
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
1-787 | 0e+00 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 677.70 E-value: 0e+00
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| mutS2 | TIGR01069 | MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
1-786 | 0e+00 | |||||||||||
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other] Pssm-ID: 130141 [Multi-domain] Cd Length: 771 Bit Score: 553.66 E-value: 0e+00
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| ABC_MutS2 | cd03280 | ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
300-497 | 4.08e-105 | |||||||||||
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 320.73 E-value: 4.08e-105
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
327-507 | 8.78e-67 | |||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 219.35 E-value: 8.78e-67
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| ABC_MutS_homologs | cd03243 | ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
300-497 | 1.83e-57 | |||||||||||
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 194.78 E-value: 1.83e-57
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| ABC_MSH4_euk | cd03282 | ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
301-464 | 1.39e-39 | |||||||||||
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213249 [Multi-domain] Cd Length: 204 Bit Score: 145.22 E-value: 1.39e-39
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| mutS1 | TIGR01070 | DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
246-577 | 9.08e-37 | |||||||||||
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 148.76 E-value: 9.08e-37
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| ABC_MSH6_euk | cd03286 | ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
303-505 | 1.78e-36 | |||||||||||
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 136.79 E-value: 1.78e-36
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| ABC_MSH3_euk | cd03287 | ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
299-505 | 9.35e-36 | |||||||||||
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213254 [Multi-domain] Cd Length: 222 Bit Score: 134.92 E-value: 9.35e-36
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| ABC_MSH2_euk | cd03285 | ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
301-506 | 5.55e-35 | |||||||||||
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213252 [Multi-domain] Cd Length: 222 Bit Score: 132.50 E-value: 5.55e-35
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| ABC_MSH5_euk | cd03281 | ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
300-496 | 7.76e-33 | |||||||||||
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213248 [Multi-domain] Cd Length: 213 Bit Score: 126.26 E-value: 7.76e-33
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
328-508 | 1.44e-32 | |||||||||||
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters. Pssm-ID: 425714 [Multi-domain] Cd Length: 188 Bit Score: 124.61 E-value: 1.44e-32
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| ABC_MutS1 | cd03284 | ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
300-508 | 3.37e-32 | |||||||||||
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213251 [Multi-domain] Cd Length: 216 Bit Score: 124.30 E-value: 3.37e-32
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| MutS | COG0249 | DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
244-544 | 4.55e-27 | |||||||||||
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 117.85 E-value: 4.55e-27
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| PRK05399 | PRK05399 | DNA mismatch repair protein MutS; Provisional |
243-554 | 1.51e-26 | |||||||||||
DNA mismatch repair protein MutS; Provisional Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 116.35 E-value: 1.51e-26
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| MUTSd | smart00533 | DNA-binding domain of DNA mismatch repair MUTS family; |
21-311 | 6.74e-24 | |||||||||||
DNA-binding domain of DNA mismatch repair MUTS family; Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 103.15 E-value: 6.74e-24
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| ABC_MutS-like | cd03283 | ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
303-496 | 6.98e-23 | |||||||||||
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange. Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 96.99 E-value: 6.98e-23
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| Smr | pfam01713 | Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
714-787 | 2.32e-21 | |||||||||||
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2. This domain exhibits nicking endonuclease activity that might have a role in mismatch repair or genetic recombination. It shows no significant double strand cleavage or exonuclease activity. The full-length Swiss:Q86UW6 also has the polynucleotide kinase activity. Pssm-ID: 460303 [Multi-domain] Cd Length: 76 Bit Score: 88.29 E-value: 2.32e-21
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| ABC_Class2 | cd03227 | ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
300-454 | 3.38e-16 | |||||||||||
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins. Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 76.63 E-value: 3.38e-16
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| ATP-synt_Fo_b | cd06503 | F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
524-625 | 1.56e-07 | |||||||||||
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens. Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 50.90 E-value: 1.56e-07
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| SMR | smart00463 | Small MutS-related domain; |
712-787 | 2.76e-07 | |||||||||||
Small MutS-related domain; Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 48.83 E-value: 2.76e-07
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| SmrA | COG2840 | DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
708-786 | 3.92e-07 | |||||||||||
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 50.68 E-value: 3.92e-07
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| AtpF | COG0711 | FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
519-625 | 5.82e-06 | |||||||||||
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 46.70 E-value: 5.82e-06
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| ATP-synt_B | pfam00430 | ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
529-625 | 1.80e-05 | |||||||||||
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006 Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 45.00 E-value: 1.80e-05
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
326-454 | 4.15e-05 | |||||||||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 44.54 E-value: 4.15e-05
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| DivIVA | COG3599 | Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
521-618 | 2.43e-04 | |||||||||||
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 41.38 E-value: 2.43e-04
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| PRK13460 | PRK13460 | F0F1 ATP synthase subunit B; Provisional |
518-625 | 5.84e-04 | |||||||||||
F0F1 ATP synthase subunit B; Provisional Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 41.55 E-value: 5.84e-04
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
503-625 | 1.22e-03 | |||||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.22e-03
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| ClyA_Cry6Aa-like | cd22656 | Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
448-618 | 1.23e-03 | |||||||||||
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices. Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 1.23e-03
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| COG1340 | COG1340 | Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
500-625 | 1.23e-03 | |||||||||||
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.23e-03
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| OmpH | smart00935 | Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
516-618 | 1.24e-03 | |||||||||||
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery. Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 1.24e-03
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| Borrelia_P83 | pfam05262 | Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
546-642 | 2.45e-03 | |||||||||||
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.14 E-value: 2.45e-03
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| MSSS | pfam20297 | MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
638-677 | 3.21e-03 | |||||||||||
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ABC ATPase and Smr domains. It has been predicted to play a role in lesion recognition or alternatively in mediating contacts with RNA primers or misincorporated ribonucleotides during DNA repair or interacting with the ribosome at the intersection between DNA repair and ribosome rescue. Pssm-ID: 466447 [Multi-domain] Cd Length: 42 Bit Score: 35.85 E-value: 3.21e-03
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| PRK08475 | PRK08475 | F0F1 ATP synthase subunit B; Validated |
525-606 | 4.52e-03 | |||||||||||
F0F1 ATP synthase subunit B; Validated Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 38.84 E-value: 4.52e-03
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| PRK04950 | PRK04950 | ProP expression regulator; Provisional |
582-673 | 4.69e-03 | |||||||||||
ProP expression regulator; Provisional Pssm-ID: 235322 [Multi-domain] Cd Length: 213 Bit Score: 39.14 E-value: 4.69e-03
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| Borrelia_P83 | pfam05262 | Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
505-603 | 4.97e-03 | |||||||||||
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.37 E-value: 4.97e-03
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| rad50 | TIGR00606 | rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
490-643 | 6.26e-03 | |||||||||||
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.26e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
503-618 | 6.34e-03 | |||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 6.34e-03
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