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Conserved domains on  [gi|340548424|gb|AEK52379|]
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recombinase A, partial [Aeromonas sp. Ae76(2011)]

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

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List of domain hits

Name Accession Description Interval E-value
recA super family cl35814
recombinase A; Provisional
1-187 9.20e-155

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 431.14  E-value: 9.20e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:PRK09354  21 QFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:PRK09354 101 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 180
                        170       180
                 ....*....|....*....|....*..
gi 340548424 161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:PRK09354 181 GNISKSNTTVIFINQIREKIGVMFGNP 207
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-187 9.20e-155

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 431.14  E-value: 9.20e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:PRK09354  21 QFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:PRK09354 101 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 180
                        170       180
                 ....*....|....*....|....*..
gi 340548424 161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:PRK09354 181 GNISKSNTTVIFINQIREKIGVMFGNP 207
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-187 8.36e-152

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 423.81  E-value: 8.36e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:COG0468   24 QFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHAL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:COG0468  104 DPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 183
                        170       180
                 ....*....|....*....|....*..
gi 340548424 161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:COG0468  184 GAISKSNTTVIFINQLREKIGVMFGNP 210
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-187 2.46e-136

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: 381.36  E-value: 2.46e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:pfam00154  13 QFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:pfam00154  93 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 172
                         170       180
                  ....*....|....*....|....*..
gi 340548424  161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:pfam00154 173 GSISKSNTTVIFINQIREKIGVMFGNP 199
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-187 5.55e-136

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: 382.49  E-value: 5.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:TIGR02012  16 QFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:TIGR02012  96 DPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 175
                         170       180
                  ....*....|....*....|....*..
gi 340548424  161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:TIGR02012 176 GALSKSNTTAIFINQIREKIGVMFGNP 202
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
17-187 6.54e-124

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: 348.78  E-value: 6.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  17 DIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLL 96
Cdd:cd00983    1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  97 ISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQI 176
Cdd:cd00983   81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
                        170
                 ....*....|.
gi 340548424 177 RMKIGVMFGSP 187
Cdd:cd00983  161 REKIGVMFGNP 171
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
40-181 6.07e-09

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: 52.38  E-value: 6.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    40 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAV 119
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340548424   120 DVIIVDSVAALTPKaeiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIG 181
Cdd:smart00382  80 DVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-187 9.20e-155

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 431.14  E-value: 9.20e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:PRK09354  21 QFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:PRK09354 101 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 180
                        170       180
                 ....*....|....*....|....*..
gi 340548424 161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:PRK09354 181 GNISKSNTTVIFINQIREKIGVMFGNP 207
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-187 8.36e-152

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 423.81  E-value: 8.36e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:COG0468   24 QFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHAL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:COG0468  104 DPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 183
                        170       180
                 ....*....|....*....|....*..
gi 340548424 161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:COG0468  184 GAISKSNTTVIFINQLREKIGVMFGNP 210
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-187 2.46e-136

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: 381.36  E-value: 2.46e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:pfam00154  13 QFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:pfam00154  93 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 172
                         170       180
                  ....*....|....*....|....*..
gi 340548424  161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:pfam00154 173 GSISKSNTTVIFINQIREKIGVMFGNP 199
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-187 5.55e-136

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: 382.49  E-value: 5.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    1 QFGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHAL 80
Cdd:TIGR02012  16 QFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   81 DPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:TIGR02012  96 DPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 175
                         170       180
                  ....*....|....*....|....*..
gi 340548424  161 ANIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:TIGR02012 176 GALSKSNTTAIFINQIREKIGVMFGNP 202
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
17-187 6.54e-124

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: 348.78  E-value: 6.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  17 DIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLL 96
Cdd:cd00983    1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  97 ISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQI 176
Cdd:cd00983   81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
                        170
                 ....*....|.
gi 340548424 177 RMKIGVMFGSP 187
Cdd:cd00983  161 REKIGVMFGNP 171
recA PRK09519
intein-containing recombinase RecA;
2-187 1.86e-91

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 283.14  E-value: 1.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   2 FGKGSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALD 81
Cdd:PRK09519  22 YGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  82 PIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTA 161
Cdd:PRK09519 102 PDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTG 181
                        170       180
                 ....*....|....*....|....*.
gi 340548424 162 NIKNANCLCIFINQIRMKIGVMFGSP 187
Cdd:PRK09519 182 ALNNSGTTAIFINQLRDKIGVMFGSP 207
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
40-186 1.93e-46

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: 150.58  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  40 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYA-----------AKLGVNVDDLLISQPDTGEQALE 108
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424 109 ICDMLVRSNA----VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMF 184
Cdd:cd01393   81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160

                 ..
gi 340548424 185 GS 186
Cdd:cd01393  161 GA 162
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
21-181 8.10e-18

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: 77.35  E-value: 8.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDP-----IYAAKLGVNVDDL 95
Cdd:cd01394    1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  96 LISQP-DTGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEiegEMGDShvGLQARLMSQaLRKLTANIKNANCLCIF 172
Cdd:cd01394   79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151

                 ....*....
gi 340548424 173 INQIRMKIG 181
Cdd:cd01394  152 TNQVYSDID 160
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
21-178 1.06e-14

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 69.17  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPI--YAAKLGVNVDDLL-- 96
Cdd:COG0467    2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  97 ----ISQPDTGEQALEICDML------VRSNAVDVIIVDSVAALtpkaeiEGEMGDShvglqaRLMSQALRKLTANIKNA 166
Cdd:COG0467   81 gllrIIDLSPEELGLDLEELLarlreaVEEFGAKRVVIDSLSGL------LLALPDP------ERLREFLHRLLRYLKKR 148
                        170
                 ....*....|..
gi 340548424 167 NCLCIFINQIRM 178
Cdd:COG0467  149 GVTTLLTSETGG 160
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
28-181 3.24e-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: 65.13  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   28 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDP-----IYAAKLGVNVDDLLISQP-D 101
Cdd:TIGR02237   1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkqIAEDRPERALSNFIVFEVfD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  102 TGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEIEGEMGDSHVGLQARLmsQALRKLTANIKNAnclCIFINQIRMK 179
Cdd:TIGR02237  79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLARKKNLA---VVITNQVYTD 152

                  ..
gi 340548424  180 IG 181
Cdd:TIGR02237 153 VN 154
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
20-134 2.26e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 63.02  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  20 AISTGSLSLDVALGIGGLPCGRIVEIYGPE-SSGKTTLTLQVIAEAQKKGKVCAFIDAEHALdpiYA---AKLGVNVDDL 95
Cdd:COG4544   28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 340548424  96 LISQPDTGEQALEICDMLVRSNAVDVIIVDsVAALTPKA 134
Cdd:COG4544  105 LLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
radB PRK09361
DNA repair and recombination protein RadB; Provisional
18-130 2.81e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 59.88  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  18 IEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDPIYAAKL-GVNVDDLL 96
Cdd:PRK09361   2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 340548424  97 ----ISQP-DTGEQALEICDM--LVRSNaVDVIIVDSVAAL 130
Cdd:PRK09361  80 sniiIFEPsSFEEQSEAIRKAekLAKEN-VGLIVLDSATSL 119
radA PRK04301
DNA repair and recombination protein RadA; Validated
16-187 1.29e-10

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 58.74  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  16 MDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK------KGKVCAFIDAE------------ 77
Cdd:PRK04301  79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEgtfrperieqma 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  78 --------HALDPIYAAKlGVNVDD--LLIsqpdtgEQALEICDmlvRSNAVDVIIVDSVAALTpKAEiegemgdsHVGL 147
Cdd:PRK04301 158 ealgldpdEVLDNIHVAR-AYNSDHqmLLA------EKAEELIK---EGENIKLVIVDSLTAHF-RAE--------YVGR 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 340548424 148 ------QARLMSQ--ALRKLtANIKnaNCLCIFINQIRMKIGVMFGSP 187
Cdd:PRK04301 219 gnlaerQQKLNKHlhDLLRL-ADLY--NAAVVVTNQVMARPDAFFGDP 263
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
29-181 3.74e-10

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: 56.94  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  29 DVALGiGGLPCGRIVEIYGPESSGKT----TLTLQVIAEAQKKGK--VCAFIDAEHALDP-----IYAAKLGVN------ 91
Cdd:cd19493    1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLdgGVLYIDTESKFSAerlaeIAEARFPEAfsgfme 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  92 --------VDDLLISQPDTGEQALEICDML---VRSNAVDVIIVDSVAALTPKaeiegEMGDSHVGLQARlmSQALRKLT 160
Cdd:cd19493   80 eneraeemLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
                        170       180
                 ....*....|....*....|....*
gi 340548424 161 ANIKN-ANCLCIFI---NQIRMKIG 181
Cdd:cd19493  153 SSLKRlAEEFRIAVlvtNQATTHFG 177
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
21-130 1.24e-09

homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.


Pssm-ID: 410922 [Multi-domain]  Cd Length: 236  Bit Score: 55.44  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKK-----GKVCaFIDAEHALDP----IYAAKLG 89
Cdd:cd19514    1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 340548424  90 VN----VDDLLISQPDTGEQALEICDMLVRSNAVD----VIIVDSVAAL 130
Cdd:cd19514   79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMAL 127
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
21-130 1.76e-09

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: 55.39  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQK-----KGKvCAFIDAEHALDPI----YAAKLG 89
Cdd:pfam08423  19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLemgggEGK-ALYIDTEGTFRPErlvaIAERYG 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 340548424   90 VNVDDLLISQP-------DTGEQALEICDMLVRSNAVDVIIVDSVAAL 130
Cdd:pfam08423  97 LDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATAL 144
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
40-181 6.07e-09

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: 52.38  E-value: 6.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424    40 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAV 119
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340548424   120 DVIIVDSVAALTPKaeiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIG 181
Cdd:smart00382  80 DVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
21-177 1.07e-08

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 52.65  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVD----- 93
Cdd:cd01124    1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemede 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  94 -DLLISQPDTGEQALEICDML-------VRSNAVDVIIVDSVAALTPKAEiegemgdshvglQARLMSQALRKLTANIKN 165
Cdd:cd01124   80 gKLIIVDAPPTEAGRFSLDELlsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
                        170
                 ....*....|..
gi 340548424 166 ANCLCIFINQIR 177
Cdd:cd01124  148 AGVTTIFTSEMR 159
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
21-187 2.03e-08

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: 51.98  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK-------KGKVcAFIDAEHALDP----IYAAKLG 89
Cdd:cd19515    1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeegglNGKA-VYIDTENTFRPerimQMAKALG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  90 VNVDDLL-----ISQPDTGEQAL---EICDMLVRSNAVDVIIVDSVAALTpKAEI--EGEMGDSHVGLqARLMSQALRkl 159
Cdd:cd19515   79 LDPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR-- 154
                        170       180
                 ....*....|....*....|....*....
gi 340548424 160 TANIKNAnclCIFI-NQIRMKIGVMFGSP 187
Cdd:cd19515  155 LADLYNI---AVLVtNQVMAKPDAFFGDP 180
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
17-160 3.79e-08

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 52.04  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  17 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDP----IYA 85
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVtcqlpLDQGGGEGK-AMYIDTEGTFRPqrliQIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  86 AKLGVNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAALTpKAEIEGEmGDshvgLQAR--LMSQA 155
Cdd:PLN03186 179 ERFGLNGADVLenvayARAYNTDHQSellLEAASMMAETR-FALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKF 251

                 ....*
gi 340548424 156 LRKLT 160
Cdd:PLN03186 252 LRSLQ 256
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
21-178 3.83e-08

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 51.48  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   21 ISTGSLSLDvALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAE-AQKKGKVCAFIDA-EHALDPIYAAK-LGVNVDDLL- 96
Cdd:pfam06745   1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLRENARsFGWDLEKLEe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   97 --------ISQPDTGEQALEICDML----------VRSNAVDVIIVDSVAALtpkAEIEGEMgdshvglQARlmsQALRK 158
Cdd:pfam06745  80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
                         170       180
                  ....*....|....*....|
gi 340548424  159 LTANIKNANCLCIFINQIRM 178
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPS 166
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
28-176 7.38e-08

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: 50.75  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  28 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ------KKGKVCAFIDAEHAL----------------DPIYA 85
Cdd:cd19491    1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  86 AKLGVNVddLLISQPDTgeQALEICDM-----LVRSNAVDVIIVDSVAALtpkAEIEGEMGDSHVGLQARLMSQALRKLT 160
Cdd:cd19491   80 KNFLDNI--FVEHVADL--ETLEHCLNyqlpaLLERGPIRLVVIDSIAAL---FRSEFDTSRSDLVERAKYLRRLADHLK 152
                        170
                 ....*....|....*.
gi 340548424 161 ANIKNANCLCIFINQI 176
Cdd:cd19491  153 RLADKYNLAVVVVNQV 168
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
21-130 7.73e-08

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: 50.61  E-value: 7.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDPI----YAAKLG 89
Cdd:cd01123    1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVtcqlpIDRGGGEGK-AIYIDTEGTFRPErlraIAQRFG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 340548424  90 VNVDDLL----ISQPDTGEQALEICD----MLVRSnAVDVIIVDSVAAL 130
Cdd:cd01123   79 LDPDDVLdnvaYARAFNSDHQTQLLDqaaaMMVES-RFKLLIVDSATAL 126
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
8-127 4.14e-07

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 48.68  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   8 MRLGDSKTMDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAE-AQKKGKVcAFIDAEHALDPI--Y 84
Cdd:cd01121   51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARlAQRGGKV-LYVSGEESLSQIklR 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 340548424  85 AAKLGVNVDDLLIsqpdTGEQALE-ICDMLVRSNAvDVIIVDSV 127
Cdd:cd01121  129 AERLGLGSDNLYL----LAETNLEaILAEIEELKP-SLVVIDSI 167
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
21-130 1.57e-06

meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.


Pssm-ID: 131292 [Multi-domain]  Cd Length: 313  Bit Score: 47.08  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKK-----GKVCaFIDAEHALDP----IYAAKLG 89
Cdd:TIGR02238  78 ITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREmgggnGKVA-YIDTEGTFRPdrirAIAERFG 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 340548424   90 VN----VDDLLISQPDTGEQALEICDMLVRSNAVD---VIIVDSVAAL 130
Cdd:TIGR02238 156 VDpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMAL 203
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
21-113 2.53e-06

N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410896 [Multi-domain]  Cd Length: 225  Bit Score: 46.19  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVDDLLI- 97
Cdd:cd19488    1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRavALSHGWSLDGIHIf 79
                         90
                 ....*....|....*...
gi 340548424  98 --SQPDTGEQALEICDML 113
Cdd:cd19488   80 elSPSESALDAAQQYTIL 97
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
21-130 2.71e-06

RAD51D recombinase; RAD51 recombinase plays an essential 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. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.


Pssm-ID: 410921 [Multi-domain]  Cd Length: 235  Bit Score: 46.16  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDP----IYAAKLG 89
Cdd:cd19513    1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPerllAIAERYG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 340548424  90 VNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAAL 130
Cdd:cd19513   79 LNGEDVLdnvayARAYNTDHQMqllIQASAMMAESR-YALLIVDSATAL 126
PTZ00035 PTZ00035
Rad51 protein; Provisional
21-130 4.51e-06

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 45.76  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAE-----AQKKGKVCaFIDAEHALDP-----IyAAKL 88
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGKVL-YIDTEGTFRPerivqI-AERF 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 340548424  89 GVN----VDDLLISQPDTGEQALE----ICDMLVRSNAVdVIIVDSVAAL 130
Cdd:PTZ00035 177 GLDpedvLDNIAYARAYNHEHQMQllsqAAAKMAEERFA-LLIVDSATAL 225
FlaH COG2874
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
21-131 1.41e-05

Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];


Pssm-ID: 442121  Cd Length: 230  Bit Score: 44.05  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHA----LDPIYAakLGVNVDDLL 96
Cdd:COG2874    3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTtkefIKQMKS--LSYDISDYL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340548424  97 IS--------QPDTGE----QALEICDMLVRSNA-----VDVIIVDSVAALT 131
Cdd:COG2874   80 LRgrllflpvHPLGFEwnskQRKDLLKRLMKYIAsnlweADVIIIDSLSALL 131
recomb_RAD51 TIGR02239
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ...
17-130 1.52e-05

DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).


Pssm-ID: 274048 [Multi-domain]  Cd Length: 316  Bit Score: 44.33  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   17 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDPI----YA 85
Cdd:TIGR02239  74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIA 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 340548424   86 AKLGVNVDDLLIS-------QPDTGEQALEICDMLVRSNAVDVIIVDSVAAL 130
Cdd:TIGR02239 152 ERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATAL 203
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
40-181 3.94e-05

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: 42.72  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  40 GRIVEIYGPESSGKTTLTLQVIAEA-----------QKKGKVCAFIDAEHALDP-----IYAAKLGVNVDDLLISQPDTG 103
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCilpsswggvplGGLEAAVVFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424 104 -EQALEIC-----------------------DMLVRSNA---VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQAL 156
Cdd:cd19490   81 vEEIAREClqrlhifrchsslqllatllsleNYLLSLSAnpeLGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAIL 160
                        170       180
                 ....*....|....*....|....*
gi 340548424 157 RKLTANIKNANCLCIFINQIRMKIG 181
Cdd:cd19490  161 RELRRLRRRFQLVVIATKQALFPGK 185
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
17-130 4.70e-05

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 42.84  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  17 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKVcAFIDAEHALDP----IYA 85
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVttqlpTEMGGGNGKV-AYIDTEGTFRPdrivPIA 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340548424  86 AKLGVN----VDDLLISQPDTGEQ---ALEICDMLVRSNAVDVIIVDSVAAL 130
Cdd:PLN03187 182 ERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIAL 233
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
35-64 9.09e-05

RAD51D recombinase; RAD51D 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. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410897 [Multi-domain]  Cd Length: 209  Bit Score: 41.47  E-value: 9.09e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 340548424  35 GGLPCGRIVEIYGPESSGKTTLTLQVIAEA 64
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANV 31
PRK06067 PRK06067
flagellar accessory protein FlaH; Validated
17-137 1.20e-04

flagellar accessory protein FlaH; Validated


Pssm-ID: 180381  Cd Length: 234  Bit Score: 41.11  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  17 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPiYAAK---LGVNVD 93
Cdd:PRK06067   3 KKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKS-YLKQmesVKIDIS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 340548424  94 DLLIS---------------QPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIE 137
Cdd:PRK06067  81 DFFLWgylrifplntegfewNSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
42-76 4.23e-04

ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.


Pssm-ID: 376582 [Multi-domain]  Cd Length: 222  Bit Score: 39.61  E-value: 4.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 340548424   42 IVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDA 76
Cdd:pfam01637  22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDP 56
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
37-159 5.54e-04

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 39.50  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  37 LPCGRIVEIYGPESSGKTTLTLQV---IAEAQ-------KKGKVcAFIDAEHALDPI------YAAKLGVNVDDL----- 95
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQLaaaVAAGGpwlgrrvPPGKV-LYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlr 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 340548424  96 LIS-----QPDTGEQALEicdMLVRSNAVDVIIVDSVAALTPkaeiegemGDSHVGLQARLMSQALRKL 159
Cdd:COG3598   89 LLSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL 146
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
41-127 6.76e-04

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 38.85  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424   41 RIVeIYGPESSGKTTLtlqvIAEAQKKgkvcAFIDAEHALDPIYAAKLGVnvddllISQPDTGEQALEICDMLVRSNAV- 119
Cdd:pfam13479   4 KIL-IYGPSGIGKTTF----AKTLPKP----LFLDTEKGSKALDGDRFPD------IVIRDSWQDFLDAIDELTAAELAd 68

                  ....*....
gi 340548424  120 -DVIIVDSV 127
Cdd:pfam13479  69 yKTIVIDTV 77
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
29-71 1.39e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 38.53  E-value: 1.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 340548424  29 DVALGIgglPCGRIVEIYGPESSGKTTLtLQVIA--EAQKKGKVC 71
Cdd:PRK10851  20 DISLDI---PSGQMVALLGPSGSGKTTL-LRIIAglEHQTSGHIR 60
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
34-76 1.65e-03

Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440952  Cd Length: 353  Bit Score: 38.08  E-value: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 340548424  34 IGGLPCGRIVeIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDA 76
Cdd:COG1341   30 ILSSGPGRIM-VLGPVDSGKSTLTTLLANKLLAEGLKVAIIDA 71
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
21-72 3.09e-03

C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410895 [Multi-domain]  Cd Length: 219  Bit Score: 36.89  E-value: 3.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340548424  21 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCA 72
Cdd:cd19487    1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSV 51
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
41-59 4.92e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 36.34  E-value: 4.92e-03
                         10
                 ....*....|....*....
gi 340548424  41 RIVeIYGPESSGKTTLTLQ 59
Cdd:COG3172   10 KIV-LLGAESTGKTTLARA 27
Tdk COG1435
Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the ...
40-125 7.58e-03

Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441044  Cd Length: 192  Bit Score: 35.85  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  40 GRIVEIYGPESSGKTTLTLQVI--AEAQKKgKVCAFIdaeHALDPIYAAK-----LGVNVDDLLISQPDtgeqalEICDM 112
Cdd:COG1435    4 GKLEFIYGPMFSGKSEELLRRAhnYEEAGQ-KVLLFK---PAIDDRYGEGkivsrIGLSREAIPVDDDT------DILEL 73
                         90
                 ....*....|...
gi 340548424 113 LVRSNAVDVIIVD 125
Cdd:COG1435   74 VREGPDVDVVLID 86
KaiC_C cd19484
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ...
21-131 8.09e-03

C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410892 [Multi-domain]  Cd Length: 218  Bit Score: 35.77  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340548424  21 ISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVDDLLIS 98
Cdd:cd19484    1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 340548424  99 Q---------PDTG-EQALEICDMLVRSNAVDVIIVDSVAALT 131
Cdd:cd19484   81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSALA 123
 
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.
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