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Conserved domains on  [gi|117667658|gb|ABK55875|]
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recombinase A, partial [Streptomyces acrimycini]

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

CATH:  3.30.250.10|3.40.50.300
Gene Ontology:  GO:0005524|GO:0003697|GO:0006310|GO:0006281|GO:0140664|GO:0003684|GO:0016887
PubMed:  12045091|9187054

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
recA super family cl35814
recombinase A; Provisional
 1-168 9.54e-139

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 389.92  E-value: 9.54e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:PRK09354  49 DIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:PRK09354 129 IADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPE 208


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:PRK09354 209 TTTGGNAL 216
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-168 9.54e-139

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 389.92  E-value: 9.54e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:PRK09354  49 DIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:PRK09354 129 IADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPE 208


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:PRK09354 209 TTTGGNAL 216
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-168 1.25e-137

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 386.83  E-value: 1.25e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:COG0468   52 DIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:COG0468  132 IAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPE 211


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:COG0468  212 TTTGGNAL 219
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-168 1.90e-127

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: 356.87  E-value: 1.90e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:cd00983   13 DIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:cd00983   93 IADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPE 172


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:cd00983  173 TTTGGNAL 180
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-168 1.69e-125

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: 355.14  E-value: 1.69e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:TIGR02012  44 DLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:TIGR02012 124 IAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPE 203


                  ....*...
gi 117667658  161 TTTGGRAL 168
Cdd:TIGR02012 204 TTTGGNAL 211
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-168 5.60e-123

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: 346.69  E-value: 5.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:pfam00154  41 DIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:pfam00154 121 IADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPE 200


                  ....*...
gi 117667658  161 TTTGGRAL 168
Cdd:pfam00154 201 TTTGGRAL 208
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 11-153 2.13e-08

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: 50.45  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    11 RGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSqpDNGEQALEIVDMLVRSGA 90
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117667658    91 LDLIVIDSVAALVPRaeiegemgdshVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIG 153
Cdd:smart00382  79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-168 9.54e-139

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 389.92  E-value: 9.54e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:PRK09354  49 DIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:PRK09354 129 IADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPE 208


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:PRK09354 209 TTTGGNAL 216
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-168 1.25e-137

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 386.83  E-value: 1.25e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:COG0468   52 DIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:COG0468  132 IAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPE 211


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:COG0468  212 TTTGGNAL 219
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-168 1.90e-127

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: 356.87  E-value: 1.90e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:cd00983   13 DIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:cd00983   93 IADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPE 172


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:cd00983  173 TTTGGNAL 180
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-168 1.69e-125

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: 355.14  E-value: 1.69e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:TIGR02012  44 DLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:TIGR02012 124 IAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPE 203


                  ....*...
gi 117667658  161 TTTGGRAL 168
Cdd:TIGR02012 204 TTTGGNAL 211
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-168 5.60e-123

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: 346.69  E-value: 5.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:pfam00154  41 DIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:pfam00154 121 IADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPE 200


                  ....*...
gi 117667658  161 TTTGGRAL 168
Cdd:pfam00154 201 TTTGGRAL 208
recA PRK09519
intein-containing recombinase RecA;
1-168 8.98e-100

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 303.94  E-value: 8.98e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQALE 80
Cdd:PRK09519  49 DVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPE 160
Cdd:PRK09519 129 IADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPE 208


                 ....*...
gi 117667658 161 TTTGGRAL 168
Cdd:PRK09519 209 TTTGGKAL 216
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 12-168 2.36e-51

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: 162.52  E-value: 2.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  12 GRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYA-----------KKLGVDIDSLILSQPDNGEQALE 80
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  81 IVDMLVRSGA----LDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMF 156
Cdd:cd01393   81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160

                        170
                 ....*....|...
gi 117667658 157 G-SPETTTGGRAL 168
Cdd:cd01393  161 GaSLVPPALGNTW 173
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
 7-168 5.86e-16

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: 71.68  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    7 GGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEhALDPEYAKKLGVD-----IDSLILSQP---DNGEQA 78
Cdd:TIGR02237   7 GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfdfDEQGVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   79 LEIVDMLVRSGALDLIVIDSVAALVpRAEIEGEMGDSHVGL--QARLMSQALRKitsalnqSKTTAIFINQLREKIGVMF 156
Cdd:TIGR02237  86 IQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELarQLTLLLSLARK-------KNLAVVITNQVYTDVNNGT 157

                         170
                  ....*....|..
gi 117667658  157 GSPettTGGRAL 168
Cdd:TIGR02237 158 LRP---LGGHLL 166
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 1-129 2.38e-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: 70.42  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEhALDPEYAKKL-----GVDIDSLILSQP-DN 74
Cdd:cd01394    9 DSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPERFQQIagerfESIASNIIVFEPySF 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 117667658  75 GEQALEIVDM--LVRSGALDLIVIDSVAALVpRAEiegEMGDSHVGLQ-ARLMSQALR 129
Cdd:cd01394   87 DEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDSEANRElSRQMSKLLS 140
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 7-111 5.83e-12

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 61.42  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEhALDPEYAKKL-GVDIDSL----ILSQP---DNGEQA 78
Cdd:PRK09361  18 GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELlsniIIFEPssfEEQSEA 96

                         90       100       110
                 ....*....|....*....|....*....|...
gi 117667658  79 LEIVDMLVRSGAlDLIVIDSVAALVpRAEIEGE 111
Cdd:PRK09361  97 IRKAEKLAKENV-GLIVLDSATSLY-RLELEDE 127
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
1-160 1.28e-11

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 60.31  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDP--EYAKKLGVDIDSLI---------- 68
Cdd:COG0467   10 DELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIesgllriidl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  69 ---LSQPDNGEQALEIVDMLVRSGAlDLIVIDSVAALVPRAEIEGEmgdshvglqARLMsqaLRKITSALNQSKTTAIFI 145
Cdd:COG0467   89 speELGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKKRGVTTLLT 155

                        170
                 ....*....|....*
gi 117667658 146 NQLREKIGVMFGSPE 160
Cdd:COG0467  156 SETGGLEDEATEGGL 170
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 7-151 2.12e-10

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: 56.89  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDP--EYAKKLGVDID------SLILSQPDNGEQA 78
Cdd:cd01124   14 GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERllRNAKSFGWDFDemedegKLIIVDAPPTEAG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  79 LEIVDML-------VRSGALDLIVIDSVAALvpRAEIEGEMgdshvglQARlmsQALRKITSALNQSKTTAIFINQLREK 151
Cdd:cd01124   94 RFSLDELlsrilsiIKSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRAAGVTTIFTSEMRSF 161
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
1-97 4.24e-10

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 56.48  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGVGGLPRGRVVEVYGPE-SSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNGEQAL 79
Cdd:COG4544   37 DAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRARRPADAL 116

                         90
                 ....*....|....*...
gi 117667658  80 EIVDMLVRSGALDLIVID 97
Cdd:COG4544  117 WAAEEALRSGACGAVVAW 134
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 1-153 2.36e-09

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: 54.25  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANA---QKLGGS---VAFIDAEHALDPE---------YAKKLGVDID 65
Cdd:cd19493    1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampARKGGLdggVLYIDTESKFSAErlaeiaearFPEAFSGFME 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  66 S-----------LILSQPDNGE-----QALE--IVDMLVRsgaldLIVIDSVAALVpRAEIEGEMGDshvgLQARlmSQA 127
Cdd:cd19493   80 EneraeemlkrvAVVRVTTLAQllerlPNLEehILSSGVR-----LVVIDSIAALV-RREFGGSDGE----VTER--HNA 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 117667658 128 LRKITSAL----NQSKTTAIFINQLREKIG 153
Cdd:cd19493  148 LAREASSLkrlaEEFRIAVLVTNQATTHFG 177
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 7-150 6.65e-09

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: 53.02  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    7 GGLPRGRVVEVYGPESSGKTTLTLH-AVANAQKLGGSVAFIDA-EHALD-PEYAKKLGVDIDSLI--------------- 68
Cdd:pfam06745  14 GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLEKLEeegklaiidastsgi 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   69 ----LSQPDNGEQALEIVDMLVRSGALDLIVIDSVAALvprAEIEGEMgdshvglQARlmsQALRKITSALNQSKTTAIF 144
Cdd:pfam06745  94 giaeVEDRFDLEELIERLREAIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRRLKRVLKGLGVTAIF 160


                  ....*.
gi 117667658  145 INQLRE 150
Cdd:pfam06745 161 TSEKPS 166
radA PRK04301
DNA repair and recombination protein RadA; Validated
 7-165 1.29e-08

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 52.57  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTLTLHAVANAQK------LGGSVAFIDAEHALDPE----YAKKLGVDIDSLIlsqpDN-- 74
Cdd:PRK04301  97 GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRPErieqMAEALGLDPDEVL----DNih 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  75 -------------GEQALEIV--DMLVRsgaldLIVIDSVAALVpRAEiegemgdsHVGL------QARLMSQ--ALRKI 131
Cdd:PRK04301 173 varaynsdhqmllAEKAEELIkeGENIK-----LVIVDSLTAHF-RAE--------YVGRgnlaerQQKLNKHlhDLLRL 238

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 117667658 132 TSALNqsktTAIFI-NQLREKIGVMFGSPETTTGG 165
Cdd:PRK04301 239 ADLYN----AAVVVtNQVMARPDAFFGDPTQPIGG 269
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 11-153 2.13e-08

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: 50.45  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    11 RGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEYAKKLGVDIDSLILSqpDNGEQALEIVDMLVRSGA 90
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117667658    91 LDLIVIDSVAALVPRaeiegemgdshVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIG 153
Cdd:smart00382  79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 1-168 3.30e-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: 51.21  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANAQK------LGGSVAFIDAEHALDPE----YAKKLGVDIDSLIls 70
Cdd:cd19515    9 DKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRPErimqMAKALGLDPDEVL-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  71 qpDN---------GEQAL---EIVDMLVRSGALDLIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQaLRKITSALN 136
Cdd:cd19515   86 --DNiyvaraynsNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHD-LHRLADLYN 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 117667658 137 qsktTAIFI-NQLREKIGVMFGSPETTTGGRAL 168
Cdd:cd19515  161 ----IAVLVtNQVMAKPDAFFGDPTQAIGGHIL 189
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
 1-168 3.81e-08

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: 50.82  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTlHAVANAQKL-------GGSVAFIDAEHALDPE----YAKKLGVD----ID 65
Cdd:cd19514    9 DKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLCVTAQLpgsmgggGGKVAYIDTEGTFRPDrirpIAERFGVDhdavLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  66 SLILSQPDNGEQALEIVDML----VRSGALDLIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQaLRKITSALNqsk 139
Cdd:cd19514   87 NILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKISEEYN--- 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 117667658 140 tTAIFI-NQLREKIG--VMFGS-PETTTGGRAL 168
Cdd:cd19514  161 -VAVFItNQVTADPGaaMTFQAdPKKPIGGHIL 192
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
 1-153 1.70e-07

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: 49.21  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANAQ------KLGGSVAFIDAEHAL----------------DPEYAK 58
Cdd:cd19491    2 DELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  59 KLGVDIDSLILSQPDNGEQAL-EIVDMLVRSGALDLIVIDSVAALVpRAeiegEMGDSHVGLQARlmSQALRKITSALNQ 137
Cdd:cd19491   81 NFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RS----EFDTSRSDLVER--AKYLRRLADHLKR 153

                        170       180
                 ....*....|....*....|
gi 117667658 138 --SK--TTAIFINQLREKIG 153
Cdd:cd19491  154 laDKynLAVVVVNQVTDRFD 173
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 12-147 1.76e-07

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: 48.88  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  12 GRVVEVYGPESSGKTTLTLHAVANA--------QKLGG---SVAFIDAEHALD-----------------PEYAKKLGVD 63
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCilpsswggVPLGGleaAVVFIDTDGRFDilrlrsileariraaiqAANSSDDEED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  64 IDSLILS--------QPDNGEQALEIVDML-------VRSGALDLIVIDSVAALVPRAEIEGEMGdshvGLQARLMSQAL 128
Cdd:cd19490   81 VEEIAREclqrlhifRCHSSLQLLATLLSLenyllslSANPELGLLLIDSISAFYWQDRFSAELA----RAAPLLQEAAL 156

                        170       180
                 ....*....|....*....|...
gi 117667658 129 RKITSAL----NQSKTTAIFINQ 147
Cdd:cd19490  157 RAILRELrrlrRRFQLVVIATKQ 179
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 15-168 3.71e-07

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: 46.34  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  15 VEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDaehALDpeyakklgvDIDSLILSQPDNgeqaleivdmlvrsGALDLI 94
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFIS---FLD---------TILEAIEDLIEE--------------KKLDII 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117667658  95 VIDSVAALVPRAEiegemgdshvGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPETTTGGRAL 168
Cdd:cd01120   55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSL 118
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
 1-168 4.64e-07

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: 47.91  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTlHAVANAQKL-------GGSVAFIDAEHALDPE----YAKKLGVD----ID 65
Cdd:cd01123    9 DKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLAVTCQLpidrgggEGKAIYIDTEGTFRPErlraIAQRFGLDpddvLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658  66 SLILSQPDNGEQALEIVD----MLVRSgALDLIVIDSVAALVpRAEIEGEmGDshvgLQARLM--SQALRKITSALNQSK 139
Cdd:cd01123   87 NVAYARAFNSDHQTQLLDqaaaMMVES-RFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQRLADEFG 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 117667658 140 TTAIFINQLREKIG---VMFGSPETTTGGRAL 168
Cdd:cd01123  160 VAVVVTNQVVAQVDgamMFAADPKKPIGGNIL 191
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
9-136 1.67e-06

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 46.43  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   9 LPRGRVVEVYGPESSGKTTLTLH---AVANAQKL------GGSVAFIDAE----------------HALDPEYAKKlGVD 63
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAGGPWlgrrvpPGKVLYLAAEddrgelrrrlkalgadLGLPFADLDG-RLR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117667658  64 IDSLILSQPDNGeqALEIVDMLVRSGALDLIVIDSVAALVPraeiegemGDSHVGLQARLMSQALRKITSALN 136
Cdd:COG3598   89 LLSLAGDLDDTD--DLEALERAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLAERTG 151
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
 1-168 2.33e-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: 46.31  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGvGGLPRGRVVEVYGPESSGKTTLTlHAVANAQKL-------GGSVAFIDAEHALDPE----YAKKLGVD----ID 65
Cdd:TIGR02238  86 DGILG-GGIESMSITEVFGEFRCGKTQLS-HTLCVTAQLpremgggNGKVAYIDTEGTFRPDriraIAERFGVDpdavLD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   66 SLILSQPDNGEQALEIVDML---VRSGALDLIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQaLRKITSALNqskt 140
Cdd:TIGR02238 164 NILYARAYTSEHQMELLDYLaakFSEEPFRLLIVDSIMALF-RVDFsgRGELSERQQKL-AQMLSR-LNKISEEFN---- 236

                         170       180       190
                  ....*....|....*....|....*....|..
gi 117667658  141 TAIFI-NQLREKIG--VMFGS-PETTTGGRAL 168
Cdd:TIGR02238 237 VAVFVtNQVQADPGatMTFIAdPKKPIGGHVL 268
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
 17-103 3.83e-06

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: 45.00  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   17 VYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDPEY----------AKKLGVDIDSLILSQPDNGEQALEIVDMLV 86
Cdd:pfam01637  25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKldrfeevrrlAEALGIAVPKAELEESKLAFLAIELLLEAL 104

                          90
                  ....*....|....*...
gi 117667658   87 -RSGALDLIVIDSVAALV 103
Cdd:pfam01637 105 kRRGKKIAIIIDEVQQAI 122
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 7-103 1.68e-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: 43.01  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTLTLHAVAN-AQKLGGSVAFIDAEHALdpeYAKKLGVDIDSLILSQpDNGEQAL------ 79
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANvASRSGQNVLYIDTKSSF---SARRLAQILKSRAQDA-EEIDKALqrirvv 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 117667658  80 -------------EIVDML-----VRSGALDLIVIDSVAALV 103
Cdd:cd19489   78 rvfdpyelldlleELRNTLsqqqeNLYSRLKLVIIDSLSALI 119
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 1-165 3.45e-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: 42.67  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    1 DVALGvGGLPRGRVVEVYGPESSGKTTLTlHAVANAQKLG-------GSVAFIDAEHALDPE----YAKKLGVD----ID 65
Cdd:pfam08423  27 DKLLG-GGIETGSITEIFGEFRTGKTQLC-HTLCVTCQLPlemgggeGKALYIDTEGTFRPErlvaIAERYGLDpedvLD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   66 SLILSQPDNGEQALEIVDML---VRSGALDLIVIDSVAALVpRAEIE--GEMGDSHVGLqARLMSqALRKITSALNqskt 140
Cdd:pfam08423 105 NVAYARAYNSEHQMQLLQQAaamMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-TLQRLADEFG---- 177

                         170       180       190
                  ....*....|....*....|....*....|
gi 117667658  141 TAIFI-NQLREKIG---VMF-GSPETTTGG 165
Cdd:pfam08423 178 VAVVItNQVVAQVDgaaGMFsGDPKKPIGG 207
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
 7-132 2.34e-04

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 40.49  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTL--TLHA---VANAQKLG-GSVAFIDAEHALDPE----YAKKLGVD----IDSLILSQP 72
Cdd:PLN03186 118 GGIETGSITEIYGEFRTGKTQLchTLCVtcqLPLDQGGGeGKAMYIDTEGTFRPQrliqIAERFGLNgadvLENVAYARA 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117667658  73 DNGEQALEIV----DMLVRSgALDLIVIDSVAALVpRAEIEGEmGDshvgLQAR--LMSQALRKIT 132
Cdd:PLN03186 198 YNTDHQSELLleaaSMMAET-RFALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKFLRSLQ 256
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 9-107 1.11e-03

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


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 37.75  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658    9 LPRGRVVEVYGPESSGKTTLTLH-AVANAQKL----------GGSVAFIDAE--------------HALDPEYAKKLGVD 63
Cdd:pfam13481  30 LPAGGLGLLAGAPGTGKTTLALDlAAAVATGKpwlggprvpeQGKVLYVSAEgpadelrrrlraagADLDLPARLLFLSL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 117667658   64 IDSLILSQPDNGEQAL-----EIVDMLVRSGALDLIVIDSVAALVPRAE 107
Cdd:pfam13481 110 VESLPLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALGGDE 158
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 7-85 3.39e-03

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: 36.56  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   7 GGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDP--EYAKKLGVDIDSLI---LSQPDNGEQALEI 81
Cdd:cd19488   14 GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQElrAVALSHGWSLDGIHifeLSPSESALDAAQQ 93


                 ....
gi 117667658  82 VDML 85
Cdd:cd19488   94 YTIL 97
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 11-99 3.49e-03

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


Pssm-ID: 433243  Cd Length: 199  Bit Score: 36.54  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   11 RGRVVEVYGPESSGKTTLTLHAvanaqklgGSVAFIDAEHALDPEYAKKLGVDIDSLILSQPDNgeqalEIVDMLVRSGA 90
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPDIVIRDSWQDFLD-----AIDELTAAELA 67

                          90
                  ....*....|
gi 117667658   91 L-DLIVIDSV 99
Cdd:pfam13479  68 DyKTIVIDTV 77
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
 10-48 3.55e-03

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


Pssm-ID: 440952  Cd Length: 353  Bit Score: 36.92  E-value: 3.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 117667658  10 PRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDA 48
Cdd:COG1341   33 SGPGRIMVLGPVDSGKSTLTTLLANKLLAEGLKVAIIDA 71
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 13-57 4.09e-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: 35.95  E-value: 4.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 117667658  13 RVVeVYGPESSGKTTLTlHAVANAqkLGGSVAfidaehaldPEYA 57
Cdd:COG3172   10 KIV-LLGAESTGKTTLA-RALAAH--YNTPWV---------PEYG 41
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 1-99 5.94e-03

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: 35.97  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117667658   1 DVALGvGGLPRGRVVEVYGPESSGKTTLTLHAVANAQKLGGSVAFIDAEHALDP--EYAKKLGVDIDSL-ILSqpdngEQ 77
Cdd:cd01121   72 DRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQikLRAERLGLGSDNLyLLA-----ET 145

                         90       100
                 ....*....|....*....|..
gi 117667658  78 ALEIVDMLVRSGALDLIVIDSV 99
Cdd:cd01121  146 NLEAILAEIEELKPSLVVIDSI 167
 
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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