sujigwak/NVAR huggingface dataset:
UniProt ID: P93825
Variant: D -> E at position 38-38
Variant annotation: in strain: cv. El-0, Gy-0 and Kn-0
Protein function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Reference sequence:
MLKTLLVQWLVFFFFFLIGSVVTAAEDDGSLSLCNCDDEDSLFSYETILNSQKVGDFLIAIAYFSIPIELVYFVSRTNVPSPYNWVVCEFIAFIVLCGMTHLLAGFTYGPHWPWVMTAVTVFKMLTGIVSFLTALSLVTLLPLLLKAKVREFMLSKKTRELDREVGIIMKQTETSLHVRMLTTKIRTSLDRHTILYTTLVELSKTLGLKNCAVWIPNEIKTEMNLTHELRPRIDDENENEHFGGYAGFSIPISESDVVRIKRSEEVNMLSPGSVLASVTSRGKSGPTVGIRVPMLRVCNFKGGTPEAIHMCYAILVCVLPLRQPQAWTYQELEIVKVVADQVAVAISHAVILEESQLMREKLAEQNRALQVARENALRANQAKAAFEQMMSDAMRCPVRSILGLLPLILQDGKLPENQTVIVDAMRRTSELLVQLVNNAGDINNGTIRAAETHYFSLHSVVKESACVARCLCMANGFGFSAEVYRALPDYVVGDDRKVFQAILHMLGVLMNRKIKGNVTFWVFPESGNSDVSERKDIQEAVWRHCYSKEYMEVRFGFEVTAEGEESSSSSSGSNLEEEEENPSLNACQNIVKYMQGNIRVVEDGLGLVKSVSVVFRFQLRRSMMSRGGGYSGETFRTSTPPSTSH
UniProt ID: P93825
Variant: I -> V at position 61-61
Variant annotation: in strain: cv. Gu-0 and cv. Ove-0
Protein function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Reference sequence:
MLKTLLVQWLVFFFFFLIGSVVTAAEDDGSLSLCNCDDEDSLFSYETILNSQKVGDFLIAIAYFSIPIELVYFVSRTNVPSPYNWVVCEFIAFIVLCGMTHLLAGFTYGPHWPWVMTAVTVFKMLTGIVSFLTALSLVTLLPLLLKAKVREFMLSKKTRELDREVGIIMKQTETSLHVRMLTTKIRTSLDRHTILYTTLVELSKTLGLKNCAVWIPNEIKTEMNLTHELRPRIDDENENEHFGGYAGFSIPISESDVVRIKRSEEVNMLSPGSVLASVTSRGKSGPTVGIRVPMLRVCNFKGGTPEAIHMCYAILVCVLPLRQPQAWTYQELEIVKVVADQVAVAISHAVILEESQLMREKLAEQNRALQVARENALRANQAKAAFEQMMSDAMRCPVRSILGLLPLILQDGKLPENQTVIVDAMRRTSELLVQLVNNAGDINNGTIRAAETHYFSLHSVVKESACVARCLCMANGFGFSAEVYRALPDYVVGDDRKVFQAILHMLGVLMNRKIKGNVTFWVFPESGNSDVSERKDIQEAVWRHCYSKEYMEVRFGFEVTAEGEESSSSSSGSNLEEEEENPSLNACQNIVKYMQGNIRVVEDGLGLVKSVSVVFRFQLRRSMMSRGGGYSGETFRTSTPPSTSH
UniProt ID: P93825
Variant: G -> V at position 244-244
Variant annotation: in strain: cv. Se-0
Protein function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Reference sequence:
MLKTLLVQWLVFFFFFLIGSVVTAAEDDGSLSLCNCDDEDSLFSYETILNSQKVGDFLIAIAYFSIPIELVYFVSRTNVPSPYNWVVCEFIAFIVLCGMTHLLAGFTYGPHWPWVMTAVTVFKMLTGIVSFLTALSLVTLLPLLLKAKVREFMLSKKTRELDREVGIIMKQTETSLHVRMLTTKIRTSLDRHTILYTTLVELSKTLGLKNCAVWIPNEIKTEMNLTHELRPRIDDENENEHFGGYAGFSIPISESDVVRIKRSEEVNMLSPGSVLASVTSRGKSGPTVGIRVPMLRVCNFKGGTPEAIHMCYAILVCVLPLRQPQAWTYQELEIVKVVADQVAVAISHAVILEESQLMREKLAEQNRALQVARENALRANQAKAAFEQMMSDAMRCPVRSILGLLPLILQDGKLPENQTVIVDAMRRTSELLVQLVNNAGDINNGTIRAAETHYFSLHSVVKESACVARCLCMANGFGFSAEVYRALPDYVVGDDRKVFQAILHMLGVLMNRKIKGNVTFWVFPESGNSDVSERKDIQEAVWRHCYSKEYMEVRFGFEVTAEGEESSSSSSGSNLEEEEENPSLNACQNIVKYMQGNIRVVEDGLGLVKSVSVVFRFQLRRSMMSRGGGYSGETFRTSTPPSTSH
UniProt ID: P93835
Variant: E -> K at position 127-127
Variant annotation: in strain: cv. Cvi-1
Protein function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Reference sequence:
MNSFSAFSEMFGSDYEPQGGDYCPTLATSCPKKPAGRKKFRETRHPIYRGVRQRNSGKWVSEVREPNKKTRIWLGTFQTAEMAARAHDVAALALRGRSACLNFADSAWRLRIPESTCAKDIQKAAAEAALAFQDETCDTTTTNHGLDMEETMVEAIYTPEQSEGAFYMDEETMFGMPTLLDNMAEGMLLPPPSVQWNHNYDGEGDGDVSLWSY
UniProt ID: P93835
Variant: T -> S at position 178-178
Variant annotation: in strain: cv. Cvi-1
Protein function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Reference sequence:
MNSFSAFSEMFGSDYEPQGGDYCPTLATSCPKKPAGRKKFRETRHPIYRGVRQRNSGKWVSEVREPNKKTRIWLGTFQTAEMAARAHDVAALALRGRSACLNFADSAWRLRIPESTCAKDIQKAAAEAALAFQDETCDTTTTNHGLDMEETMVEAIYTPEQSEGAFYMDEETMFGMPTLLDNMAEGMLLPPPSVQWNHNYDGEGDGDVSLWSY
UniProt ID: P94281
Variant: G -> S at position 124-124
Variant annotation: in coumermycin A1 mutant
Protein function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Reference sequence:
MSNDNKDLFSVLNHAQSRIDRKENTQYTSAHSEIVVPAVPLSSPHHHKEDSTYNASSIRILEGLEPVRLRPGMYIGGTDSKALHHLFSEIIDNAMDEAVAGYADLIDITLDSNNYLTVTDNGRGIPIENHPQIPDKSTLEVIMTHLHSGGKFDGKAYQTSGGLHGVGISVVNALSDDMEVEVARERKLYRQRFSRGIPQSGLEELGDVYNRRGTRVCFHPDSQIFGENTAFDPEKIYKIARSKAYLFNGVKIRWNCDPAALKDAKNIPEKDVFYFPDGLKDYLSLSLKNKHLVTAEIFSGKTQQLSGHGSVEWAIAWHNGDAYIQSYCNTIPTEEGGTHETGLRQTLLRGLKAYAELIGNKRASIITSDDVMASTVVMLSVFIKDPQFVGQTKDRLATTEAQRIVENAIRDPFDHWLANSPHEATKLLNWVIERAEERLKRRQDREINRKTAVRKLRLPGKLADCSQNSAAGAELFIVEGDSAGGSAKQARNRTNQAILPLRGKILNVASAAREKMSSSQTIADLILALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFFQEIPDLIRAGHLYLAVPPLYRISQGGKVAYARDDSHKDELLKTEFTGKGKIEIGRFKGLGEMRAEQLKETTMNPKKRTLLRVSIDTFEMQETKETVQNLMGTKPEERFRFIQESSTFANNLDI
UniProt ID: P94281
Variant: R -> Q at position 184-184
Variant annotation: in coumermycin A1 mutant
Protein function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Reference sequence:
MSNDNKDLFSVLNHAQSRIDRKENTQYTSAHSEIVVPAVPLSSPHHHKEDSTYNASSIRILEGLEPVRLRPGMYIGGTDSKALHHLFSEIIDNAMDEAVAGYADLIDITLDSNNYLTVTDNGRGIPIENHPQIPDKSTLEVIMTHLHSGGKFDGKAYQTSGGLHGVGISVVNALSDDMEVEVARERKLYRQRFSRGIPQSGLEELGDVYNRRGTRVCFHPDSQIFGENTAFDPEKIYKIARSKAYLFNGVKIRWNCDPAALKDAKNIPEKDVFYFPDGLKDYLSLSLKNKHLVTAEIFSGKTQQLSGHGSVEWAIAWHNGDAYIQSYCNTIPTEEGGTHETGLRQTLLRGLKAYAELIGNKRASIITSDDVMASTVVMLSVFIKDPQFVGQTKDRLATTEAQRIVENAIRDPFDHWLANSPHEATKLLNWVIERAEERLKRRQDREINRKTAVRKLRLPGKLADCSQNSAAGAELFIVEGDSAGGSAKQARNRTNQAILPLRGKILNVASAAREKMSSSQTIADLILALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFFQEIPDLIRAGHLYLAVPPLYRISQGGKVAYARDDSHKDELLKTEFTGKGKIEIGRFKGLGEMRAEQLKETTMNPKKRTLLRVSIDTFEMQETKETVQNLMGTKPEERFRFIQESSTFANNLDI
UniProt ID: P94281
Variant: T -> A at position 214-214
Variant annotation: in coumermycin A1 mutant
Protein function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Reference sequence:
MSNDNKDLFSVLNHAQSRIDRKENTQYTSAHSEIVVPAVPLSSPHHHKEDSTYNASSIRILEGLEPVRLRPGMYIGGTDSKALHHLFSEIIDNAMDEAVAGYADLIDITLDSNNYLTVTDNGRGIPIENHPQIPDKSTLEVIMTHLHSGGKFDGKAYQTSGGLHGVGISVVNALSDDMEVEVARERKLYRQRFSRGIPQSGLEELGDVYNRRGTRVCFHPDSQIFGENTAFDPEKIYKIARSKAYLFNGVKIRWNCDPAALKDAKNIPEKDVFYFPDGLKDYLSLSLKNKHLVTAEIFSGKTQQLSGHGSVEWAIAWHNGDAYIQSYCNTIPTEEGGTHETGLRQTLLRGLKAYAELIGNKRASIITSDDVMASTVVMLSVFIKDPQFVGQTKDRLATTEAQRIVENAIRDPFDHWLANSPHEATKLLNWVIERAEERLKRRQDREINRKTAVRKLRLPGKLADCSQNSAAGAELFIVEGDSAGGSAKQARNRTNQAILPLRGKILNVASAAREKMSSSQTIADLILALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFFQEIPDLIRAGHLYLAVPPLYRISQGGKVAYARDDSHKDELLKTEFTGKGKIEIGRFKGLGEMRAEQLKETTMNPKKRTLLRVSIDTFEMQETKETVQNLMGTKPEERFRFIQESSTFANNLDI
UniProt ID: P94281
Variant: T -> I at position 214-214
Variant annotation: in coumermycin A1 mutant
Protein function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Reference sequence:
MSNDNKDLFSVLNHAQSRIDRKENTQYTSAHSEIVVPAVPLSSPHHHKEDSTYNASSIRILEGLEPVRLRPGMYIGGTDSKALHHLFSEIIDNAMDEAVAGYADLIDITLDSNNYLTVTDNGRGIPIENHPQIPDKSTLEVIMTHLHSGGKFDGKAYQTSGGLHGVGISVVNALSDDMEVEVARERKLYRQRFSRGIPQSGLEELGDVYNRRGTRVCFHPDSQIFGENTAFDPEKIYKIARSKAYLFNGVKIRWNCDPAALKDAKNIPEKDVFYFPDGLKDYLSLSLKNKHLVTAEIFSGKTQQLSGHGSVEWAIAWHNGDAYIQSYCNTIPTEEGGTHETGLRQTLLRGLKAYAELIGNKRASIITSDDVMASTVVMLSVFIKDPQFVGQTKDRLATTEAQRIVENAIRDPFDHWLANSPHEATKLLNWVIERAEERLKRRQDREINRKTAVRKLRLPGKLADCSQNSAAGAELFIVEGDSAGGSAKQARNRTNQAILPLRGKILNVASAAREKMSSSQTIADLILALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFFQEIPDLIRAGHLYLAVPPLYRISQGGKVAYARDDSHKDELLKTEFTGKGKIEIGRFKGLGEMRAEQLKETTMNPKKRTLLRVSIDTFEMQETKETVQNLMGTKPEERFRFIQESSTFANNLDI
UniProt ID: P94846
Variant: A -> T at position 59-59
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: K -> R at position 231-231
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: I -> V at position 259-259
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: N -> T at position 376-376
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: K -> Q at position 407-407
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: L -> S at position 443-443
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: A -> V at position 475-475
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: I -> V at position 501-501
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: R -> K at position 607-607
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P94846
Variant: CT -> HA at position 636-637
Variant annotation: in strain: 84-183
Protein function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Reference sequence:
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPALIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRATGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARGERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECTKNLDFEEAMRLRDEIAQLRTL
UniProt ID: P95361
Variant: A -> V at position 85-85
Variant annotation: in strain: FA19
Protein function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Reference sequence:
MHALPRYAVFGNPAAHSKSPQIHQQFALQEGVDIEYGRICADIGGFAQAVSTFFETGGCGANVTVPFKQEAFHLADEHSDRALAAGAVNTLVWLEDGRIRGDNTDGIGLANDITQVKNIAIEGKTILLLGAGGAVRGVIPVLKEHRPARIVIANRTRAKAEELARLFGIEAVPMADVNGGFDIIINGTSGGLSGQLPAVSPKIFRDCRLAYDMVYREAAKPFLDFARQSGAKKTADGLGMLVGQAAASYALWRGFKPDIRPVIEHMKAL