NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|385287421|gb|AFI58657|]
View 

recombinase A protein, partial [Exiguobacterium sp. E11_55]

Protein Classification

recombinase RecA family protein( domain architecture ID 1000164)

recombinase RecA catalyzes an ATP-dependent DNA strand-exchange reaction, which is a critical step in the repair of DNA double-strand breaks by homologous recombination

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
recA super family cl35814
recombinase A; Provisional
1-201 1.65e-164

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 456.56  E-value: 1.65e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:PRK09354  62 IVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:PRK09354 142 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYAS 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:PRK09354 222 VRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFD 262
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-201 1.65e-164

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 456.56  E-value: 1.65e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:PRK09354  62 IVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:PRK09354 142 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYAS 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:PRK09354 222 VRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFD 262
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-201 1.14e-160

RecA/RadA recombinase [Replication, recombination and repair];


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 446.92  E-value: 1.14e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:COG0468   65 IVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:COG0468  145 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYAS 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:COG0468  225 VRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFD 265
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
1-201 1.29e-149

recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange.


Pssm-ID: 410863 [Multi-domain]  Cd Length: 235  Bit Score: 414.26  E-value: 1.29e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:cd00983   26 IIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLIRSGAVDL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:cd00983  106 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPETTTGGNALKFYAS 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:cd00983  186 VRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFD 226
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-201 4.66e-148

recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA repair systems. RecA protein catalyzes an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination.


Pssm-ID: 425488 [Multi-domain]  Cd Length: 262  Bit Score: 411.41  E-value: 4.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:pfam00154  54 IIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:pfam00154 134 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYAS 213
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 385287421  161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:pfam00154 214 VRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFD 254
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-201 2.56e-146

protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization of homolgous regions of DNA. A segment of ssDNA can be hybridized to another ssDNA region, or to a dsDNA region. ATP is hydrolyzed in the process. Part of the SOS respones, it is regulated by LexA via autocatalytic cleavage. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 162659 [Multi-domain]  Cd Length: 321  Bit Score: 409.45  E-value: 2.56e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:TIGR02012  57 IIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:TIGR02012 137 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYAS 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 385287421  161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:TIGR02012 217 VRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFD 257
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1-169 2.17e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.31  E-value: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421     1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSqpDTGEQALEIAEALVRSGAVDI 80
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    81 LVVDSVAALVPKaeiegemgdshVGLQARLMSQALRKLSGATNKSKTIVIFINqirekigimfgNPETTPGGRALKFYSS 160
Cdd:smart00382  82 LILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRRRFD 139

                   ....*....
gi 385287421   161 VRLEVRRAE 169
Cdd:smart00382 140 RRIVLLLIL 148
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-201 1.65e-164

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 456.56  E-value: 1.65e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:PRK09354  62 IVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:PRK09354 142 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYAS 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:PRK09354 222 VRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFD 262
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-201 1.14e-160

RecA/RadA recombinase [Replication, recombination and repair];


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 446.92  E-value: 1.14e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:COG0468   65 IVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:COG0468  145 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYAS 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:COG0468  225 VRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFD 265
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
1-201 1.29e-149

recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange.


Pssm-ID: 410863 [Multi-domain]  Cd Length: 235  Bit Score: 414.26  E-value: 1.29e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:cd00983   26 IIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLIRSGAVDL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:cd00983  106 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPETTTGGNALKFYAS 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:cd00983  186 VRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFD 226
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-201 4.66e-148

recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA repair systems. RecA protein catalyzes an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination.


Pssm-ID: 425488 [Multi-domain]  Cd Length: 262  Bit Score: 411.41  E-value: 4.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:pfam00154  54 IIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:pfam00154 134 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYAS 213
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 385287421  161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:pfam00154 214 VRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFD 254
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-201 2.56e-146

protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization of homolgous regions of DNA. A segment of ssDNA can be hybridized to another ssDNA region, or to a dsDNA region. ATP is hydrolyzed in the process. Part of the SOS respones, it is regulated by LexA via autocatalytic cleavage. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 162659 [Multi-domain]  Cd Length: 321  Bit Score: 409.45  E-value: 2.56e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:TIGR02012  57 IIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:TIGR02012 137 IVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYAS 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 385287421  161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNKIAPPFKTAEVD 201
Cdd:TIGR02012 217 VRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFD 257
recA PRK09519
intein-containing recombinase RecA;
1-190 1.50e-101

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 310.10  E-value: 1.50e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDI 80
Cdd:PRK09519  62 VIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDI 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  81 LVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALKFYSS 160
Cdd:PRK09519 142 VVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYAS 221
                        170       180       190
                 ....*....|....*....|....*....|
gi 385287421 161 VRLEVRRAETLKQGQDMVGNRTKIKVVKNK 190
Cdd:PRK09519 222 VRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
1-167 2.06e-50

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 161.37  E-value: 2.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQ-----------NLGVNIDELLLSQPDTGEQALEIA 69
Cdd:cd01393    3 ITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLLAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  70 EALVRSGA----VDILVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFG- 144
Cdd:cd01393   83 DSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGSGa 162
                        170       180
                 ....*....|....*....|...
gi 385287421 145 NPETTPGGRALKFYSSVRLEVRR 167
Cdd:cd01393  163 SLVPPALGNTWEHSVSTRLLLYR 185
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
1-172 1.13e-15

archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 72.35  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEhALDP-KYAQNLGVNIDELL----LSQP-DTGEQALEI--AEAL 72
Cdd:cd01394   21 ITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPeRFQQIAGERFESIAsniiVFEPySFDEQGVAIqeAEKL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  73 VRSGAVDILVVDSVAALVpKAEiegEMGDShvGLQARLMSQaLRKLSGATNKSKTIVIFINQIREKigimFGNPETTP-G 151
Cdd:cd01394  100 LKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVITNQVYSD----IDDDRLKPvG 168
                        170       180
                 ....*....|....*....|.
gi 385287421 152 GRALKFYSSVRLEVRRAETLK 172
Cdd:cd01394  169 GTLLEHWSKAIIRLEKSPPGL 189
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
1-191 3.23e-13

DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).


Pssm-ID: 274047 [Multi-domain]  Cd Length: 209  Bit Score: 65.52  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEhALDPKYAQNLGVNIDELLLSQP--------DTGEQALEIAEAL 72
Cdd:TIGR02237  14 ITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNFivfevfdfDEQGVAIQKTSKF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   73 VRSGAVDILVVDSVAALVpKAEIEGEMGDSHVGLQARlmsqaLRKLSGATNKSKTIVIFINQIREKIgimfGNPETTP-G 151
Cdd:TIGR02237  93 IDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTDV----NNGTLRPlG 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 385287421  152 GRALKFYSS--VRLE----VRRAETLKQGQDMVGNRTKIKVVKNKI 191
Cdd:TIGR02237 163 GHLLEHWSKviLRLEkfrgRRLATLEKHRSRPEGESVYFRITDDGI 208
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1-169 2.17e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.31  E-value: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421     1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPKYAQNLGVNIDELLLSqpDTGEQALEIAEALVRSGAVDI 80
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    81 LVVDSVAALVPKaeiegemgdshVGLQARLMSQALRKLSGATNKSKTIVIFINqirekigimfgNPETTPGGRALKFYSS 160
Cdd:smart00382  82 LILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRRRFD 139

                   ....*....
gi 385287421   161 VRLEVRRAE 169
Cdd:smart00382 140 RRIVLLLIL 148
radB PRK09361
DNA repair and recombination protein RadB; Provisional
1-168 6.38e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 59.49  E-value: 6.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEhALDP-KYAQNLGVNIDELL----LSQP-DTGEQ--ALEIAEAL 72
Cdd:PRK09361  25 ITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPeRFKQIAGEDFEELLsniiIFEPsSFEEQseAIRKAEKL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  73 VRSGaVDILVVDSVAALVpKAEIEGEMGDShvGLQARLMSQaLRKLSGATNKSKTIVIFINQIREKIgimfGNPETTP-G 151
Cdd:PRK09361 104 AKEN-VGLIVLDSATSLY-RLELEDEEDNS--KLNRELGRQ-LTHLLKLARKHDLAVVITNQVYSDI----DSDGLRPlG 174
                        170       180
                 ....*....|....*....|....
gi 385287421 152 GRALKFYSS--VRLE-----VRRA 168
Cdd:PRK09361 175 GHTLEHWSKtiLRLEkfrngKRRA 198
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
1-167 2.36e-06

recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .


Pssm-ID: 410868 [Multi-domain]  Cd Length: 234  Bit Score: 46.37  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVAlHAIA-------EVQKRGGQAAFVDAEHALDPK----YAQNLGVNIDELLLS-------QPDTG 62
Cdd:cd01123   21 ITEMFGEFRTGKTQLC-HTLAvtcqlpiDRGGGEGKAIYIDTEGTFRPErlraIAQRFGLDPDDVLDNvayarafNSDHQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  63 EQALEIAEALVRSGAVDILVVDSVAALVpKAEIEGEmGDshvgLQARLM--SQALRKLSGATNKSKTIVIFINQIREKIG 140
Cdd:cd01123  100 TQLLDQAAAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQRLADEFGVAVVVTNQVVAQVD 173
                        170       180       190
                 ....*....|....*....|....*....|
gi 385287421 141 ---IMFGNPETTPGGRALKFYSSVRLEVRR 167
Cdd:cd01123  174 gamMFAADPKKPIGGNILAHASTTRLYLRK 203
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
1-167 2.52e-06

archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a homolog of Rad51. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR)


Pssm-ID: 410923 [Multi-domain]  Cd Length: 233  Bit Score: 46.59  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVAlHAIA-EVQKR------GGQAAFVDAEHALDPK----YAQNLGVNIDELL-----LSQPDTGEQ 64
Cdd:cd19515   21 ITEVFGEFGSGKTQLC-HQLAvNVQLPpeegglNGKAVYIDTENTFRPErimqMAKALGLDPDEVLdniyvARAYNSNHQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  65 AL--EIAEALVRSG-AVDILVVDSVAALVpKAEIegeMGDSHVGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGI 141
Cdd:cd19515  100 MLlvEKAEDLIKEGnNIKLLIVDSLTSHF-RAEY---VGRGTLAERQQKLNKHLHDLHRLADLYNIAVLVTNQVMAKPDA 175
                        170       180
                 ....*....|....*....|....*.
gi 385287421 142 MFGNPETTPGGRALKFYSSVRLEVRR 167
Cdd:cd19515  176 FFGDPTQAIGGHILGHAATFRVYLRK 201
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
1-154 3.34e-06

XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.


Pssm-ID: 410898 [Multi-domain]  Cd Length: 226  Bit Score: 45.80  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIA---------EVQKRGGQAA--FVDAEHALDP----KYAQNLGVNIDELLLSQPDTGEQA 65
Cdd:cd19490    3 VIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrSILEARIRAAIQAANSSDDEEDVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  66 LEIAEALVR----------------------------SGAVDILVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRK 117
Cdd:cd19490   83 EIARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAILRE 162
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 385287421 118 LSGATNKSKTIVIFINQirekiGIMFGNPETTPGGRA 154
Cdd:cd19490  163 LRRLRRRFQLVVIATKQ-----ALFPGKSASTDNPAA 194
radA PRK04301
DNA repair and recombination protein RadA; Validated
1-168 9.04e-06

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 45.25  E-value: 9.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKR------GGQAAFVDAEHALDP----KYAQNLGVNIDELL-----LSQPDTGEQA 65
Cdd:PRK04301 104 ITEFYGEFGSGKTQICHQLAVNVQLPeekgglEGKAVYIDTEGTFRPerieQMAEALGLDPDEVLdnihvARAYNSDHQM 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  66 L--EIAEALVRSG-AVDILVVDSVAALVpKAEiegemgdsHVGL------QARLMSQ--ALRKLSGATNkskTIVIFINQ 134
Cdd:PRK04301 184 LlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLNKHlhDLLRLADLYN---AAVVVTNQ 251
                        170       180       190
                 ....*....|....*....|....*....|....
gi 385287421 135 IREKIGIMFGNPETTPGGRALKFYSSVRLEVRRA 168
Cdd:PRK04301 252 VMARPDAFFGDPTQPIGGHILGHTATFRIYLRKS 285
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
2-156 1.69e-05

RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.49  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   2 IEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAehaldpkyaqnlgvnidelllsqPDTgeqALEIAEALVRSGAVDIL 81
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF-----------------------LDT---ILEAIEDLIEEKKLDII 54
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385287421  82 VVDSVAALVPKAEiegemgdshvGLQARLMSQALRKLSGATNKSKTIVIFINQIREKIGIMFGNPETTPGGRALK 156
Cdd:cd01120   55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
3-167 2.01e-05

Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.


Pssm-ID: 462471 [Multi-domain]  Cd Length: 255  Bit Score: 43.83  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    3 EVYGPESSGKT----TVALHAIAEVQKRG--GQAAFVDAEHALDPK----YAQNLGVNIDELLLSQP-------DTGEQA 65
Cdd:pfam08423  41 EIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFRPErlvaIAERYGLDPEDVLDNVAyaraynsEHQMQL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   66 LEIAEALVRSGAVDILVVDSVAALVpKAEIEGEmGDshvgLQARLM--SQALRKLSGATNKSKTIVIFINQIREKIG--- 140
Cdd:pfam08423 121 LQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQRLADEFGVAVVITNQVVAQVDgaa 194
                         170       180
                  ....*....|....*....|....*...
gi 385287421  141 IMF-GNPETTPGGRALKFYSSVRLEVRR 167
Cdd:pfam08423 195 GMFsGDPKKPIGGHIMAHASTTRLSLRK 222
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
1-140 3.85e-05

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 42.69  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALH----AIAEVQKRGGQAA--FVDAEHALDPK-------------YAQNLGVNIDELLLSQ--- 58
Cdd:cd19493   13 ITEITGASGSGKTQFALTlassAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFMEENERAEEMLKrva 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  59 ---PDTGEQALEIAEAL---VRSGAVDILVVDSVAALVPKA--EIEGEMGDSHVGLqARLMSqALRKLSgatNKSKTIVI 130
Cdd:cd19493   93 vvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS-SLKRLA---EEFRIAVL 167
                        170
                 ....*....|
gi 385287421 131 FINQIREKIG 140
Cdd:cd19493  168 VTNQATTHFG 177
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
4-137 1.39e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 41.05  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   4 VYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDP--KYAQNLGVNIDELL-------------LSQPDTGEQALEI 68
Cdd:COG0467   25 LSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIesgllriidlspeELGLDLEELLARL 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385287421  69 AEALVRSGAvDILVVDSVAALVpkAEIEGEMgdshvglQARLMsqaLRKLSGATNKSKTIVIFINQIRE 137
Cdd:COG0467  105 REAVEEFGA-KRVVIDSLSGLL--LALPDPE-------RLREF---LHRLLRYLKKRGVTTLLTSETGG 160
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
10-82 2.81e-04

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 40.21  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  10 SGKTTVALHAIAEVQKRGGQAAF-----VDAE-HALD-PKYAQNLGVNIDelLLSQPDTGEQALEIAEALvRSGAVDILV 82
Cdd:cd17992   77 SGKTVVAALAMLAAVENGYQVALmapteILAEqHYDSlKKLLEPLGIRVA--LLTGSTKAKEKREILEKI-ASGEIDIVI 153
DEXHc_priA cd17929
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ...
4-41 5.13e-04

DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350687 [Multi-domain]  Cd Length: 178  Bit Score: 39.11  E-value: 5.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 385287421   4 VYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDP 41
Cdd:cd17929   20 LHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTP 57
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
1-140 1.58e-03

XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410899 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   1 VIEVYGPESSGKTTVALHAIAEVQKR------GGQAAFVDAEHAL----------------DPKYAQNLGVNIDELLLSQ 58
Cdd:cd19491   14 ITEIAGESGAGKTQLCLQLALTVQLPrelgglGGGAVYICTESSFpskrlqqlasslpkryHLEKAKNFLDNIFVEHVAD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  59 PDTGEQAL-EIAEALVRSGAVDILVVDSVAALVpKAEIEGEMGDShvGLQARLMSQALRKLSGATNKSKTIVIFINQIRE 137
Cdd:cd19491   94 LETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSDL--VERAKYLRRLADHLKRLADKYNLAVVVVNQVTD 170

                 ...
gi 385287421 138 KIG 140
Cdd:cd19491  171 RFD 173
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
10-82 2.85e-03

RecG-like helicase [Replication, recombination and repair];


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 38.11  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  10 SGKTTVALHAIAEVQKRGGQAAF-----VDAE-HA--LDpKYAQNLGVNIdELLLSQpDTGEQALEIAEALvRSGAVDIL 81
Cdd:COG1200  291 SGKTVVALLAMLAAVEAGYQAALmapteILAEqHYrsLS-KLLEPLGIRV-ALLTGS-TKAKERREILAAL-ASGEADIV 366

                 .
gi 385287421  82 V 82
Cdd:COG1200  367 V 367
AAA_22 pfam13401
AAA domain;
1-93 4.89e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.78  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421    1 VIEVYGPESSGKTTVALHAIAEVQKRGGQAAFVDAEHALDPK-YAQNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVD 79
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKdLLRALLRALGLPLSGRLSKEELLAALQQLLLALAVAV 86
                          90
                  ....*....|....
gi 385287421   80 ILVVDSVAALVPKA 93
Cdd:pfam13401  87 VLIIDEAQHLSLEA 100
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
10-82 8.56e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 36.67  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421  10 SGKTTVALHAIAEVQKRGGQAAF-----VDAE-HALD-PKYAQNLGVNIDelLLSQPDTGEQALEIAEALvRSGAVDILV 82
Cdd:PRK10917 293 SGKTVVAALAALAAIEAGYQAALmapteILAEqHYENlKKLLEPLGIRVA--LLTGSLKGKERREILEAI-ASGEADIVI 369
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
4-132 9.97e-03

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 36.03  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385287421   4 VYGPESSGKTTVALHAIAEV---------QKRGGQAAFVDAE---HALDP---KYAQNLGVNIDEL-----LLSQPDTGE 63
Cdd:COG3598   18 LAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEddrGELRRrlkALGADLGLPFADLdgrlrLLSLAGDLD 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385287421  64 --QALEIAEALVRSGAVDILVVDSVAALVPkaeiegemGDSHVGLQARLMSQALRKLSGATNKSktiVIFI 132
Cdd:COG3598   98 dtDDLEALERAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLAERTGAA---VLLV 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH