MULTISPECIES: endonuclease MutS2 [Staphylococcus]
Protein Classification
endonuclease MutS2( domain architecture ID 11478705)
endonuclease MutS2 is a dsDNA-specific endonuclease/ATPase involved in the suppression of homologous recombination; it plays a role in the control of bacterial genetic diversity
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||
| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
1-782 | 0e+00 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed : Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 1122.22 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||||
| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
1-782 | 0e+00 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 1122.22 E-value: 0e+00
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| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-782 | 0e+00 | |||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 1050.89 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 ... |
1-782 | 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: 659.20 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 ... |
304-501 | 1.78e-112 | |||||||||||
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: 339.61 E-value: 1.78e-112
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
332-512 | 2.38e-77 | |||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 247.47 E-value: 2.38e-77
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
332-510 | 1.93e-31 | |||||||||||
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: 121.15 E-value: 1.93e-31
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| Name | Accession | Description | Interval | E-value | |||||||||||
| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
1-782 | 0e+00 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 1122.22 E-value: 0e+00
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| MutS2 | COG1193 | dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-782 | 0e+00 | |||||||||||
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 1050.89 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 ... |
1-782 | 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: 659.20 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 ... |
304-501 | 1.78e-112 | |||||||||||
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: 339.61 E-value: 1.78e-112
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| MUTSac | smart00534 | ATPase domain of DNA mismatch repair MUTS family; |
332-512 | 2.38e-77 | |||||||||||
ATPase domain of DNA mismatch repair MUTS family; Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 247.47 E-value: 2.38e-77
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| ABC_MutS_homologs | cd03243 | ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
308-501 | 1.23e-52 | |||||||||||
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: 181.29 E-value: 1.23e-52
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| mutS1 | TIGR01070 | DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
246-549 | 1.42e-33 | |||||||||||
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 138.36 E-value: 1.42e-33
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| ABC_MSH4_euk | cd03282 | ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
310-485 | 2.96e-33 | |||||||||||
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: 127.12 E-value: 2.96e-33
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| ABC_MSH3_euk | cd03287 | ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
310-509 | 4.56e-33 | |||||||||||
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: 127.22 E-value: 4.56e-33
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| ABC_MSH2_euk | cd03285 | ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
304-510 | 9.30e-33 | |||||||||||
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: 126.34 E-value: 9.30e-33
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| ABC_MSH6_euk | cd03286 | ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
304-509 | 1.08e-31 | |||||||||||
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: 122.92 E-value: 1.08e-31
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| MutS_V | pfam00488 | MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
332-510 | 1.93e-31 | |||||||||||
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: 121.15 E-value: 1.93e-31
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| Smr | pfam01713 | Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
708-782 | 9.80e-28 | |||||||||||
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: 106.78 E-value: 9.80e-28
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| ABC_MSH5_euk | cd03281 | ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
308-501 | 4.62e-27 | |||||||||||
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: 109.70 E-value: 4.62e-27
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| ABC_MutS1 | cd03284 | ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
310-510 | 1.21e-26 | |||||||||||
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: 108.51 E-value: 1.21e-26
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| ABC_MutS-like | cd03283 | ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
309-501 | 2.78e-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: 98.14 E-value: 2.78e-23
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| PRK05399 | PRK05399 | DNA mismatch repair protein MutS; Provisional |
246-469 | 6.14e-21 | |||||||||||
DNA mismatch repair protein MutS; Provisional Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 98.24 E-value: 6.14e-21
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| MutS | COG0249 | DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
246-470 | 5.19e-19 | |||||||||||
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 92.05 E-value: 5.19e-19
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| SMR | smart00463 | Small MutS-related domain; |
704-782 | 1.01e-16 | |||||||||||
Small MutS-related domain; Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 75.41 E-value: 1.01e-16
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| ABC_Class2 | cd03227 | ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
333-456 | 1.78e-14 | |||||||||||
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: 71.62 E-value: 1.78e-14
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| MUTSd | smart00533 | DNA-binding domain of DNA mismatch repair MUTS family; |
63-314 | 4.53e-13 | |||||||||||
DNA-binding domain of DNA mismatch repair MUTS family; Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 70.79 E-value: 4.53e-13
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| MSSS | pfam20297 | MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
641-681 | 9.53e-12 | |||||||||||
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: 60.12 E-value: 9.53e-12
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
330-466 | 4.05e-07 | |||||||||||
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: 50.32 E-value: 4.05e-07
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| SmrA | COG2840 | DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
697-775 | 2.00e-06 | |||||||||||
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 48.75 E-value: 2.00e-06
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| BRE1 | pfam08647 | BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
540-614 | 9.47e-05 | |||||||||||
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions. Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 41.80 E-value: 9.47e-05
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| DivIVA | COG3599 | Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
503-601 | 2.82e-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: 2.82e-04
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
518-619 | 7.52e-04 | |||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.52e-04
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| 235kDa-fam | TIGR01612 | reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
495-587 | 9.43e-04 | |||||||||||
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii. Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 9.43e-04
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| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-665 | 2.17e-03 | |||||||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.17e-03
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
519-723 | 8.08e-03 | |||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 8.08e-03
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| Blast search parameters | ||||
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