NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|25991843|gb|AAN76962|]
View 

RecA, partial [Burkholderia vietnamiensis]

Protein Classification

DNA recombination/repair protein RecA( domain architecture ID 1000164)

DNA recombination/repair protein 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

Gene Ontology:  GO:0005524|GO:0006310|GO:0006281
PubMed:  31100988

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
recA super family cl35814
recombinase A; Provisional
 1-169 6.32e-127

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 359.88  E-value: 6.32e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09354  10 ALEAALKQIEKQFGKGSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09354  89 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 168


                 ....*....
gi 25991843  161 ARLMSQALR 169
Cdd:PRK09354 169 ARLMSQALR 177
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-169 6.32e-127

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 359.88  E-value: 6.32e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09354  10 ALEAALKQIEKQFGKGSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09354  89 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 168


                 ....*....
gi 25991843  161 ARLMSQALR 169
Cdd:PRK09354 169 ARLMSQALR 177
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-169 1.11e-122

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 349.08  E-value: 1.11e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:COG0468  13 ALEAALSQIEKQFGKGSIMRLGD-KARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:COG0468  92 GIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 171


                ....*....
gi 25991843 161 ARLMSQALR 169
Cdd:COG0468 172 ARLMSQALR 180
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-169 4.65e-112

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: 318.96  E-value: 4.65e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     1 ALAAALAQIEKQFGKGSIMRMGDGDvKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:pfam00154   2 ALEAALKQIEKQFGKGSIMKLGDEK-KLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:pfam00154  81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160


                  ....*....
gi 25991843   161 ARLMSQALR 169
Cdd:pfam00154 161 ARLMSQALR 169
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-169 5.44e-111

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: 318.55  E-value: 5.44e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:TIGR02012   5 ALEAALAQIEKQFGKGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:TIGR02012  84 GTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQ 163


                  ....*....
gi 25991843   161 ARLMSQALR 169
Cdd:TIGR02012 164 ARLMSQALR 172
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 29-169 5.84e-97

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: 279.83  E-value: 5.84e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  29 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL 108
Cdd:cd00983   1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25991843 109 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALR 169
Cdd:cd00983  81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALR 141
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 51-152 1.20e-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: 51.22  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     51 RGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELLISqpDTGEQALEITDALVRSGS 130
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 25991843    131 IDMIVIDSVAALVPKAEIEGEM 152
Cdd:smart00382  79 PDVLILDEITSLLDAEQEALLL 100
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-169 6.32e-127

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 359.88  E-value: 6.32e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09354  10 ALEAALKQIEKQFGKGSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09354  89 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 168


                 ....*....
gi 25991843  161 ARLMSQALR 169
Cdd:PRK09354 169 ARLMSQALR 177
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-169 1.11e-122

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 349.08  E-value: 1.11e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:COG0468  13 ALEAALSQIEKQFGKGSIMRLGD-KARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:COG0468  92 GIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 171


                ....*....
gi 25991843 161 ARLMSQALR 169
Cdd:COG0468 172 ARLMSQALR 180
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-169 4.65e-112

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: 318.96  E-value: 4.65e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     1 ALAAALAQIEKQFGKGSIMRMGDGDvKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:pfam00154   2 ALEAALKQIEKQFGKGSIMKLGDEK-KLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:pfam00154  81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160


                  ....*....
gi 25991843   161 ARLMSQALR 169
Cdd:pfam00154 161 ARLMSQALR 169
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-169 5.44e-111

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: 318.55  E-value: 5.44e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:TIGR02012   5 ALEAALAQIEKQFGKGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:TIGR02012  84 GTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQ 163


                  ....*....
gi 25991843   161 ARLMSQALR 169
Cdd:TIGR02012 164 ARLMSQALR 172
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 29-169 5.84e-97

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: 279.83  E-value: 5.84e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  29 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL 108
Cdd:cd00983   1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25991843 109 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALR 169
Cdd:cd00983  81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALR 141
recA PRK09519
intein-containing recombinase RecA;
1-169 2.39e-78

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 247.70  E-value: 2.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09519  10 ALELAVAQIEKSYGKGSVMRLGD-EARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09519  89 GVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQ 168


                 ....*....
gi 25991843  161 ARLMSQALR 169
Cdd:PRK09519 169 ARLMSQALR 177
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 52-169 1.30e-32

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: 114.37  E-value: 1.30e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  52 GRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPE-----------LLISQPDTGEQALE 120
Cdd:cd01393   1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSselelaealsrLLYFRPPDTLAHLL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 25991843 121 ITDALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALR 169
Cdd:cd01393  81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLAR 133
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 33-142 2.90e-16

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


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 72.73  E-value: 2.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL---- 108
Cdd:cd01394   1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERFESIAsnii 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 25991843 109 ISQP-DTGEQALEITDA--LVRSGSIDMIVIDSVAAL 142
Cdd:cd01394  80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATAL 116
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
33-142 6.29e-13

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 63.78  E-value: 6.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPELL-- 108
Cdd:COG0467   2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 25991843 109 -----------ISQPDTGEQALEITDAlVRSGSIDMIVIDSVAAL 142
Cdd:COG0467  81 gllriidlspeELGLDLEELLARLREA-VEEFGAKRVVIDSLSGL 124
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 30-142 1.89e-12

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 62.57  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   30 IQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKL-GVNVPELL 108
Cdd:PRK09361   2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 25991843  109 ----ISQP-DTGEQALEITDA--LVRSgSIDMIVIDSVAAL 142
Cdd:PRK09361  80 sniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSL 119
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
 40-163 1.31e-11

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: 60.12  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    40 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKLGVNVPELLISQ------PD 113
Cdd:TIGR02237   1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25991843   114 TGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARL 163
Cdd:TIGR02237  79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL 129
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
22-137 4.16e-10

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 56.48  E-value: 4.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  22 GDGDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKL 100
Cdd:COG4544  18 GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAA 97

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 25991843 101 GVNVPELLISQPDTGEQALEITDALVRSGSIDMIVID 137
Cdd:COG4544  98 GLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 41-162 3.36e-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: 53.86  E-value: 3.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  41 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVIAELQKLGGTAA--FIDAEHALDVQ-------------YAAKLG 101
Cdd:cd19493   1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843 102 VNVPELLISQ------PDTGEQALEITDAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQAR 162
Cdd:cd19493  80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER 144
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 27-142 5.84e-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: 53.46  E-value: 5.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    27 KEDIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQK-LGGT---AAFIDAEHALD----VQY 96
Cdd:pfam08423  14 SELIQI-TTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRperlVAI 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25991843    97 AAKLGVNVPELLISQP-------DTGEQALEITDALVRSGSIDMIVIDSVAAL 142
Cdd:pfam08423  92 AERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATAL 144
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 33-142 1.02e-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: 52.27  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPEL--- 107
Cdd:cd01124   1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 25991843 108 ----LISQPDTGEQALEITD------ALVRSGSIDMIVIDSVAAL 142
Cdd:cd01124  80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL 124
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 51-152 1.20e-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: 51.22  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843     51 RGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELLISqpDTGEQALEITDALVRSGS 130
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 25991843    131 IDMIVIDSVAALVPKAEIEGEM 152
Cdd:smart00382  79 PDVLILDEITSLLDAEQEALLL 100
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 28-139 1.77e-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: 49.07  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  28 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDvQY---AAKLGVNV 104
Cdd:cd01121  59 EEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGS 136

                        90       100       110
                ....*....|....*....|....*....|....*
gi 25991843 105 PELLIsqpdTGEQALEITDALVRSGSIDMIVIDSV 139
Cdd:cd01121 137 DNLYL----LAETNLEAILAEIEELKPSLVVIDSI 167
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 33-143 2.20e-07

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: 48.78  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-LQKLGGTAAFIDA-EHALDV-QYAAKLGVNVPELL- 108
Cdd:pfam06745   1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25991843   109 --------ISQPDTGEQALEITDAL----------VRSGSIDMIVIDSVAALV 143
Cdd:pfam06745  80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTLF 132
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
 40-143 4.39e-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: 48.06  E-value: 4.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  40 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIA------ELQKLGGTAAFIDAEHALDVQ----------------YA 97
Cdd:cd19491   1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALtvqlprELGGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25991843  98 AKLGVNVPELLISQPDTGEQALEITD-ALVRSGSIDMIVIDSVAALV 143
Cdd:cd19491  80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF 126
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 33-142 3.24e-06

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


Pssm-ID: 410923 [Multi-domain]  Cd Length: 233  Bit Score: 45.43  E-value: 3.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd19515   1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 25991843 103 NVPELL-----ISQPDTGEQAL---EITDALVRSGSIDMIVIDSVAAL 142
Cdd:cd19515  80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSH 127
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 52-94 5.19e-06

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


Pssm-ID: 410898 [Multi-domain]  Cd Length: 226  Bit Score: 44.65  E-value: 5.19e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25991843  52 GRVVEIYGPESSGKTTLTLQVIA-----------ELQKLGGTAAFIDAEHALDV 94
Cdd:cd19490   1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDI 54
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 33-86 5.96e-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: 44.65  E-value: 5.96e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFI 86
Cdd:cd19488   1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
radA PRK04301
DNA repair and recombination protein RadA; Validated
 27-89 6.66e-06

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 44.87  E-value: 6.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25991843   27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAE 89
Cdd:PRK04301  78 RKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTE 145
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
 26-142 1.70e-05

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 43.57  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   26 VKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL--QKLGGT--AAFIDAEHALD----VQ 95
Cdd:PLN03186  98 QRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQ 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 25991843   96 YAAKLGVNVPELL----ISQPDTGEQALEItdaLVRSGSI------DMIVIDSVAAL 142
Cdd:PLN03186 177 IAERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATAL 230
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 51-139 3.12e-05

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


Pssm-ID: 433243  Cd Length: 199  Bit Score: 42.31  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    51 RGRVVEIYGPESSGKTTLTLQViaelqklgGTAAFIDAEHALDVQYAAKLgvNVPELLISQPDTGEQALEITDALVRsgS 130
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68


                  ....*....
gi 25991843   131 IDMIVIDSV 139
Cdd:pfam13479  69 YKTIVIDTV 77
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
 57-143 3.64e-05

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: 42.31  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    57 IYGPESSGKTTLTLQVIAELQKLGGTAAFIDA-----EHALDVQYAAK-----LGVNVPELLISQPDTGEQALE-ITDAL 125
Cdd:pfam01637  25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRrlaeaLGIAVPKAELEESKLAFLAIElLLEAL 104

                          90
                  ....*....|....*...
gi 25991843   126 VRSGSIDMIVIDSVAALV 143
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
49-153 1.07e-04

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 41.42  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  49 LPRGRVVEIYGPESSGKTTLTLQVIAELQK----LG-----GTAAFIDAE-HALDVQ-----YAAKLGVNVPEL-----L 108
Cdd:COG3598  10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrL 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 25991843 109 IS-----QPDTGEQALEitdALVRSGSIDMIVIDSVAALVPKAEIE-GEMG 153
Cdd:COG3598  90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFGGDENDaEEMR 137
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
 33-142 1.59e-04

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: 40.59  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQ----KLGGTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd01123   1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQLPidrgGGEGKAIYIDTEGTFRperlRAIAQRFGL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25991843 103 NVPELL----ISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAAL 142
Cdd:cd01123  80 DPDDVLdnvaYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATAL 126
PRK06067 PRK06067
flagellar accessory protein FlaH; Validated
 27-149 1.75e-04

flagellar accessory protein FlaH; Validated


Pssm-ID: 180381  Cd Length: 234  Bit Score: 40.34  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH------------ALDV 94
Cdd:PRK06067   1 EGKKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENtsksylkqmesvKIDI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   95 -QYAAKLGVNVPELLISQ----PDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIE 149
Cdd:PRK06067  80 sDFFLWGYLRIFPLNTEGfewnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
recomb_RAD51 TIGR02239
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ...
 27-142 4.21e-04

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: 39.71  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843    27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQY 96
Cdd:TIGR02239  72 RQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAI 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25991843    97 AAKLGVNVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAAL 142
Cdd:TIGR02239 151 AERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATAL 203
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 52-140 4.79e-04

RAD51C recombinase; RAD51C 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. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.


Pssm-ID: 410900 [Multi-domain]  Cd Length: 172  Bit Score: 38.74  E-value: 4.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  52 GRVVEIYGPESSGKTTLTLQVIAELQ------KLGGTAAFIDAE-----HALDV-QYAAKLGV--NVPELLISQPDtgeq 117
Cdd:cd19492   1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76

                        90       100
                ....*....|....*....|...
gi 25991843 118 aleitdalvrsgsIDMIVIDSVA 140
Cdd:cd19492  77 -------------VKLIVVDSIA 86
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 47-143 9.62e-04

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: 38.00  E-value: 9.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  47 GGLPRGRVVEIYGPESSGKTTLTLQVIAEL-QKLGGTAAFID------AEHALD-VQYAAKLGVNVPELL-------ISQ 111
Cdd:cd19489   2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQiLKSRAQDAEEIDKALqrirvvrVFD 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 25991843 112 PDTGEQALEITDALVR------SGSIDMIVIDSVAALV 143
Cdd:cd19489  82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
 33-89 1.17e-03

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: 38.07  E-value: 1.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAE 89
Cdd:cd19513   1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTE 62
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
 10-142 1.19e-03

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 38.22  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   10 EKQFGKGSIMRMGDGDVKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL-QKLGG---TA 83
Cdd:PLN03187  85 EKLLNQGFITGSDALLKRKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQLpTEMGGgngKV 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843   84 AFIDAEHALD----VQYAAKLGVN----VPELLISQPDTGEQ---ALEITDALVRSGSIDMIVIDSVAAL 142
Cdd:PLN03187 164 AYIDTEGTFRpdriVPIAERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIAL 233
PTZ00035 PTZ00035
Rad51 protein; Provisional
 33-89 1.49e-03

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 38.06  E-value: 1.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25991843   33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAE 89
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQLpieQGGGeGKVLYIDTE 161
KaiC-N cd19485
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ...
 35-142 2.76e-03

N-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: 410893 [Multi-domain]  Cd Length: 226  Bit Score: 36.96  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991843  35 TGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-LQKLGGTAAFIDAEHALD--VQYAAKLGVNVPELLIS- 110
Cdd:cd19485   3 TGIEGFDDITH-GGLPKGRPTLICGTAGTGKTLFAAQFLVNgIKEFGEPGVFVTFEESPEdiIKNMASFGWDLPKLVAEg 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 25991843 111 -------------QPDTGEQALE-----ITDAlVRSGSIDMIVIDSVAAL 142
Cdd:cd19485  82 kllildaspepseEEVTGEYDLEallirIEYA-IRKIGAKRVSLDSLEAV 130
FlaH COG2874
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
33-71 3.31e-03

Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];


Pssm-ID: 442121  Cd Length: 230  Bit Score: 36.73  E-value: 3.31e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25991843  33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQ 71
Cdd:COG2874   3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQ 40
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 53-71 6.32e-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: 35.57  E-value: 6.32e-03
                        10
                ....*....|....*....
gi 25991843  53 RVVeIYGPESSGKTTLTLQ 71
Cdd:COG3172  10 KIV-LLGAESTGKTTLARA 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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