DNA mismatch repair protein MutS [Geopsychrobacter electrodiphilus]
Protein Classification
DNA mismatch repair protein MutS( domain architecture ID 11415631)
DNA mismatch repair protein MutS, binds to DNA with mismatched base pairs and initiates repair
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||||
| MutS | COG0249 | DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
1-871 | 0e+00 | |||||||||||||
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; : Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 1360.89 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||||||
| MutS | COG0249 | DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
1-871 | 0e+00 | |||||||||||||
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 1360.89 E-value: 0e+00
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| PRK05399 | PRK05399 | DNA mismatch repair protein MutS; Provisional |
1-871 | 0e+00 | |||||||||||||
DNA mismatch repair protein MutS; Provisional Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 1350.91 E-value: 0e+00
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| mutS1 | TIGR01070 | DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
5-869 | 0e+00 | |||||||||||||
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 949.21 E-value: 0e+00
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| ABC_MutS1 | cd03284 | ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
585-802 | 4.58e-137 | |||||||||||||
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: 406.27 E-value: 4.58e-137
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
617-806 | 2.33e-114 | |||||||||||||
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: 346.49 E-value: 2.33e-114
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
616-802 | 1.26e-100 | |||||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 310.64 E-value: 1.26e-100
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| Name | Accession | Description | Interval | E-value | |||||||||||||
| MutS | COG0249 | DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
1-871 | 0e+00 | |||||||||||||
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 1360.89 E-value: 0e+00
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| PRK05399 | PRK05399 | DNA mismatch repair protein MutS; Provisional |
1-871 | 0e+00 | |||||||||||||
DNA mismatch repair protein MutS; Provisional Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 1350.91 E-value: 0e+00
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| mutS1 | TIGR01070 | DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
5-869 | 0e+00 | |||||||||||||
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 949.21 E-value: 0e+00
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| ABC_MutS1 | cd03284 | ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
585-802 | 4.58e-137 | |||||||||||||
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: 406.27 E-value: 4.58e-137
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
617-806 | 2.33e-114 | |||||||||||||
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: 346.49 E-value: 2.33e-114
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
616-802 | 1.26e-100 | |||||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 310.64 E-value: 1.26e-100
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| MutS_III | pfam05192 | MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
273-556 | 3.68e-93 | |||||||||||||
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam01624 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 III, which is central to the structure of Thermus aquaticus MutS as characterized in. Pssm-ID: 461579 [Multi-domain] Cd Length: 291 Bit Score: 295.08 E-value: 3.68e-93
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| ABC_MSH2_euk | cd03285 | ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
584-806 | 1.43e-87 | |||||||||||||
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: 277.72 E-value: 1.43e-87
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| ABC_MutS_homologs | cd03243 | ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
584-790 | 4.01e-86 | |||||||||||||
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: 272.97 E-value: 4.01e-86
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| MUTSd | smart00533 | DNA-binding domain of DNA mismatch repair MUTS family; |
290-595 | 1.01e-85 | |||||||||||||
DNA-binding domain of DNA mismatch repair MUTS family; Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 276.10 E-value: 1.01e-85
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| ABC_MSH6_euk | cd03286 | ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
585-798 | 1.92e-83 | |||||||||||||
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: 266.60 E-value: 1.92e-83
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| ABC_MSH3_euk | cd03287 | ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
583-798 | 3.47e-78 | |||||||||||||
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: 252.79 E-value: 3.47e-78
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| ABC_MSH5_euk | cd03281 | ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
585-790 | 2.76e-62 | |||||||||||||
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: 209.47 E-value: 2.76e-62
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| ABC_MSH4_euk | cd03282 | ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
585-788 | 1.24e-49 | |||||||||||||
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: 173.73 E-value: 1.24e-49
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| MutS_I | pfam01624 | MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
5-117 | 9.87e-47 | |||||||||||||
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, 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 globular domain I, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in. Pssm-ID: 426350 [Multi-domain] Cd Length: 113 Bit Score: 162.37 E-value: 9.87e-47
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| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
298-802 | 2.18e-41 | |||||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 163.00 E-value: 2.18e-41
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| ABC_MutS-like | cd03283 | ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
584-790 | 1.22e-38 | |||||||||||||
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: 142.44 E-value: 1.22e-38
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| ABC_MutS2 | cd03280 | ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
585-790 | 2.97e-36 | |||||||||||||
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: 135.84 E-value: 2.97e-36
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| MutS_II | pfam05188 | MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
125-257 | 6.17e-31 | |||||||||||||
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam01624, 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. This domain corresponds to domain II in Thermus aquaticus MutS as characterized in, and has similarity resembles RNAse-H-like domains (see pfam00075). Pssm-ID: 398728 [Multi-domain] Cd Length: 133 Bit Score: 118.22 E-value: 6.17e-31
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| MutS_IV | pfam05190 | MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ... |
433-524 | 8.18e-31 | |||||||||||||
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam00488. 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 in part with globular domain IV, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in. Pssm-ID: 398730 [Multi-domain] Cd Length: 92 Bit Score: 116.17 E-value: 8.18e-31
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| ABC_Class2 | cd03227 | ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
584-752 | 1.39e-28 | |||||||||||||
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: 112.45 E-value: 1.39e-28
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
571-802 | 3.02e-27 | |||||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 118.78 E-value: 3.02e-27
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
599-748 | 9.70e-12 | |||||||||||||
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: 63.80 E-value: 9.70e-12
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| znuC | PRK09544 | high-affinity zinc transporter ATPase; Reviewed |
603-657 | 9.32e-04 | |||||||||||||
high-affinity zinc transporter ATPase; Reviewed Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.02 E-value: 9.32e-04
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| ABC_Class3 | cd03229 | ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
602-657 | 4.04e-03 | |||||||||||||
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 39.09 E-value: 4.04e-03
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| ABC_DR_subfamily_A | cd03230 | ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
605-745 | 4.19e-03 | |||||||||||||
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 38.92 E-value: 4.19e-03
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
605-715 | 4.59e-03 | |||||||||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 38.40 E-value: 4.59e-03
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| COG4559 | COG4559 | ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
605-632 | 5.05e-03 | |||||||||||||
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 39.71 E-value: 5.05e-03
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| ABC_Iron-Siderophores_B12_Hemin | cd03214 | ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
605-668 | 5.79e-03 | |||||||||||||
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters. Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 38.57 E-value: 5.79e-03
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| CcmA | COG4133 | ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
606-635 | 8.13e-03 | |||||||||||||
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 38.61 E-value: 8.13e-03
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| ZnuC | COG1121 | ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
588-632 | 8.38e-03 | |||||||||||||
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 38.92 E-value: 8.38e-03
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