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Conserved domains on  [gi|918566729|gb|ALA10495|]
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RecA, partial [Burkholderia sp. JPY690]

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
 1-111 1.47e-83

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 247.01  E-value: 1.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:PRK09354  55 GGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLV 134

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:PRK09354 135 RSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-111 1.47e-83

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 247.01  E-value: 1.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:PRK09354  55 GGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLV 134

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:PRK09354 135 RSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-109 7.86e-81

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 240.46  E-value: 7.86e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:COG0468   58 GGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLV 137

                         90       100
                 ....*....|....*....|....*....
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDS 109
Cdd:COG0468  138 RSGAVDLIVVDSVAALVPKAEIEGEMGDS 166
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-111 3.33e-75

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: 222.05  E-value: 3.33e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:cd00983   19 GGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLI 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:cd00983   99 RSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 129
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-111 3.42e-73

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: 218.04  E-value: 3.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:pfam00154  47 GGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLV 126

                          90       100       110
                  ....*....|....*....|....*....|.
gi 918566729   81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:pfam00154 127 RSGAIDLIVVDSVAALVPKAEIEGEMGDSHV 157
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-111 3.35e-72

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: 217.24  E-value: 3.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:TIGR02012  50 GGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLV 129

                          90       100       110
                  ....*....|....*....|....*....|.
gi 918566729   81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:TIGR02012 130 RSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 5-106 1.50e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.99  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729     5 RGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSqpDTGEQALEIADALVRSGS 84
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 918566729    85 IDMIVIDSVAALVPKAEIEGEM 106
Cdd:smart00382  79 PDVLILDEITSLLDAEQEALLL 100
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-111 1.47e-83

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 247.01  E-value: 1.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:PRK09354  55 GGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLV 134

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:PRK09354 135 RSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-109 7.86e-81

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 240.46  E-value: 7.86e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:COG0468   58 GGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLV 137

                         90       100
                 ....*....|....*....|....*....
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDS 109
Cdd:COG0468  138 RSGAVDLIVVDSVAALVPKAEIEGEMGDS 166
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-111 3.33e-75

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: 222.05  E-value: 3.33e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:cd00983   19 GGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLI 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:cd00983   99 RSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 129
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-111 3.42e-73

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: 218.04  E-value: 3.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:pfam00154  47 GGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLV 126

                          90       100       110
                  ....*....|....*....|....*....|.
gi 918566729   81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:pfam00154 127 RSGAIDLIVVDSVAALVPKAEIEGEMGDSHV 157
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-111 3.35e-72

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: 217.24  E-value: 3.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:TIGR02012  50 GGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLV 129

                          90       100       110
                  ....*....|....*....|....*....|.
gi 918566729   81 RSGSIDMIVIDSVAALVPKAEIEGEMGDSLP 111
Cdd:TIGR02012 130 RSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
recA PRK09519
intein-containing recombinase RecA;
1-109 1.38e-52

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 175.67  E-value: 1.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSQPDTGEQALEIADALV 80
Cdd:PRK09519  55 GGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLI 134

                         90       100
                 ....*....|....*....|....*....
gi 918566729  81 RSGSIDMIVIDSVAALVPKAEIEGEMGDS 109
Cdd:PRK09519 135 RSGALDIVVIDSVAALVPRAELEGEMGDS 163
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 6-110 3.35e-29

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: 103.59  E-value: 3.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   6 GRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYA-----------GKLGVNVADLLVSQPDTGEQALE 74
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 918566729  75 IADALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSL 110
Cdd:cd01393   81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSS 120
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 1-96 2.80e-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: 68.11  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEhALDI----QYAGKLGVNVAD-LLVSQP-DTGEQALE 74
Cdd:cd01394   14 GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqQIAGERFESIASnIIVFEPySFDEQGVA 92

                         90       100
                 ....*....|....*....|....
gi 918566729  75 IADA--LVRSGSIDMIVIDSVAAL 96
Cdd:cd01394   93 IQEAekLLKSDKVDLVVVDSATAL 116
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 1-96 1.78e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 58.33  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEhALDI----QYAGKLGVNVAD-LLVSQP-DTGEQALE 74
Cdd:PRK09361  18 GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPerfkQIAGEDFEELLSnIIIFEPsSFEEQSEA 96

                         90       100
                 ....*....|....*....|....
gi 918566729  75 IADA--LVRSgSIDMIVIDSVAAL 96
Cdd:PRK09361  97 IRKAekLAKE-NVGLIVLDSATSL 119
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
 1-108 3.54e-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: 57.04  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEhALDI----QYAGKLGVNVAD-LLVSQP-DTGEQALE 74
Cdd:TIGR02237   7 GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkQIAEDRPERALSnFIVFEVfDFDEQGVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 918566729   75 IADA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGD 108
Cdd:TIGR02237  86 IQKTskFIDRDSASLVVVDSFTALY-RLELSDDRIS 120
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
1-96 2.88e-10

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 54.92  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALD--IQYAGKLGVNVADLLVS-------------Q 65
Cdd:COG0467   15 GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIESgllriidlspeelG 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  66 PDTGEQALEIADAlVRSGSIDMIVIDSVAAL 96
Cdd:COG0467   95 LDLEELLARLREA-VEEFGAKRVVIDSLSGL 124
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 1-108 8.20e-10

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


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 53.48  E-value: 8.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKT----TLTLQVIAEMQKLGGTAA--FIDAEHALDIQ-------------YAGKLGVN---- 57
Cdd:cd19493    6 GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFMEENerae 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 918566729  58 -VAD-LLVSQPDTGEQALEIADAL---VRSGSIDMIVIDSVAALVPKaEIEGEMGD 108
Cdd:cd19493   86 eMLKrVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-EFGGSDGE 140
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 5-106 1.50e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.99  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729     5 RGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVADLLVSqpDTGEQALEIADALVRSGS 84
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 918566729    85 IDMIVIDSVAALVPKAEIEGEM 106
Cdd:smart00382  79 PDVLILDEITSLLDAEQEALLL 100
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
 1-97 3.04e-08

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


Pssm-ID: 410899 [Multi-domain]  Cd Length: 250  Bit Score: 49.60  E-value: 3.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQ------KLGGTAAFIDAEHALDIQ----------------YAGKLGVNV 58
Cdd:cd19491    7 GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFPSKrlqqlasslpkryhleKAKNFLDNI 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 918566729  59 ADLLVSQPDTGEQAL-EIADALVRSGSIDMIVIDSVAALV 97
Cdd:cd19491   87 FVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF 126
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
1-91 4.29e-08

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 49.16  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPE-SSGKTTLTLQVIAEMQKLGGTAAFIDAEHALdiqYA---GKLGVNVADLLVSQPDTGEQALEIA 76
Cdd:COG4544   43 GGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERLLLVRARRPADALWAA 119

                         90
                 ....*....|....*
gi 918566729  77 DALVRSGSIDMIVID 91
Cdd:COG4544  120 EEALRSGACGAVVAW 134
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 1-96 8.80e-07

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: 45.33  E-value: 8.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALD--IQYAGKLGVNVADL-------LVSQPDTGEQ 71
Cdd:cd01124   14 GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMedegkliIVDAPPTEAG 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 918566729  72 ALEIAD------ALVRSGSIDMIVIDSVAAL 96
Cdd:cd01124   94 RFSLDEllsrilSIIKSFKAKRVVIDSLSGL 124
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 6-48 9.73e-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: 45.03  E-value: 9.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 918566729   6 GRVVEIYGPESSGKTTLTLQVIA-----------EMQKLGGTAAFIDAEHALDI 48
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDI 54
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
 1-96 1.54e-06

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: 44.60  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTL--TLQVIA----EMQKLGGTAAFIDAEHALD----IQYAGKLGVNVADLLVSQP---- 66
Cdd:pfam08423  32 GGIETGSITEIFGEFRTGKTQLchTLCVTCqlplEMGGGEGKALYIDTEGTFRperlVAIAERYGLDPEDVLDNVAyara 111

                          90       100       110
                  ....*....|....*....|....*....|...
gi 918566729   67 ---DTGEQALEIADALVRSGSIDMIVIDSVAAL 96
Cdd:pfam08423 112 ynsEHQMQLLQQAAAMMSESRFALLIVDSATAL 144
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
3-107 3.44e-06

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 44.12  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   3 LPRGRVVEIYGPESSGKTTLTLQVIAEMQK----LG-----GTAAFIDAE-HALDIQ-----YAGKLGVNVADL------ 61
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrl 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 918566729  62 --LVSQPDTGEQALEIADALVRSGsIDMIVIDSVAALVPKAEIE-GEMG 107
Cdd:COG3598   90 lsLAGDLDDTDDLEALERAIEEEG-PDLVVIDPLARVFGGDENDaEEMR 137
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 1-97 9.02e-06

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: 42.24  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEM-QKLGGTAAFID------AEHALDI-QYAGKLGVNVADLL-------VSQ 65
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQIlKSRAQDAEEIDKALqrirvvrVFD 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 918566729  66 PDTGEQALEIADALVR------SGSIDMIVIDSVAALV 97
Cdd:cd19489   82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
 1-104 2.15e-05

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 41.64  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTL--TLQVIAEM--QKLGGT--AAFIDAEHALD----IQYAGKLGVNVADLL----VSQP 66
Cdd:PLN03186 118 GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQIAERFGLNGADVLenvaYARA 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 918566729  67 DTGEQALEIadaLVRSGSI------DMIVIDSVAALVpKAEIEG 104
Cdd:PLN03186 198 YNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSG 237
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 1-93 2.73e-05

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: 41.36  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDiQY---AGKLGVNVADLLVsqpdTGEQALEIAD 77
Cdd:cd01121   77 GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGSDNLYL----LAETNLEAIL 151

                         90
                 ....*....|....*.
gi 918566729  78 ALVRSGSIDMIVIDSV 93
Cdd:cd01121  152 AEIEELKPSLVVIDSI 167
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
 6-94 4.70e-05

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: 40.29  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   6 GRVVEIYGPESSGKTTLTLQVIAEMQ------KLGGTAAFIDAEHALDIQYagklgvnvadllVSQPDTGEQALEIA--D 77
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEGSFNIHY------------FRVHDYVELLALINslP 68

                         90
                 ....*....|....*...
gi 918566729  78 ALVRSGS-IDMIVIDSVA 94
Cdd:cd19492   69 KFLEDHPkVKLIVVDSIA 86
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 1-97 9.41e-05

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: 39.54  E-value: 9.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    1 GGLPRGRVVEIYGPESSGKTTLTLQVIAE-MQKLGGTAAFIDA-EHALDI-QYAGKLGVNVADL----------LVSQP- 66
Cdd:pfam06745  14 GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLeeegklaiidASTSGi 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 918566729   67 ---------DTGEQALEIADAlVRSGSIDMIVIDSVAALV 97
Cdd:pfam06745  94 giaevedrfDLEELIERLREA-IREIGAKRVVIDSITTLF 132
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 5-93 2.23e-04

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


Pssm-ID: 433243  Cd Length: 199  Bit Score: 38.46  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    5 RGRVVEIYGPESSGKTTLTLQViaemqklgGTAAFIDAEHALDIQYAGKLgvNVADLLVSQPDTGEQALEIADALVRsgS 84
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68


                  ....*....
gi 918566729   85 IDMIVIDSV 93
Cdd:pfam13479  69 YKTIVIDTV 77
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
 11-97 3.99e-04

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


Pssm-ID: 376582 [Multi-domain]  Cd Length: 222  Bit Score: 37.69  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   11 IYGPESSGKTTLTLQVIAEMQKLGGTAAFIDA-----EHALDIQYAGKLGVNVADLLVSQPDTGEQAL------EIADAL 79
Cdd:pfam01637  25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRRLAEALGIAVPKAELEESKLaflaieLLLEAL 104

                          90
                  ....*....|....*...
gi 918566729   80 VRSGSIDMIVIDSVAALV 97
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 1-40 5.03e-04

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: 37.71  E-value: 5.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFI 40
Cdd:cd19488   14 GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 3-98 1.33e-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: 36.20  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729    3 LPRGRVVEIYGPESSGKTTLTLQVIAEM-----------QKLGGTAAFIDAE----------HALDIQYAGKLGVNVADL 61
Cdd:pfam13481  30 LPAGGLGLLAGAPGTGKTTLALDLAAAVatgkpwlggprVPEQGKVLYVSAEgpadelrrrlRAAGADLDLPARLLFLSL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 918566729   62 LVSQP----DTGEQAL-----EIADALVRSGSIDMIVIDSVAALVP 98
Cdd:pfam13481 110 VESLPlfflDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG 155
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 7-25 2.10e-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: 2.10e-03
                         10
                 ....*....|....*....
gi 918566729   7 RVVeIYGPESSGKTTLTLQ 25
Cdd:COG3172   10 KIV-LLGAESTGKTTLARA 27
FlaH COG2874
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
1-97 3.53e-03

Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];


Pssm-ID: 442121  Cd Length: 230  Bit Score: 35.19  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLG----------GTAAFIDAEHALDIQYA-----GKLGVNVADLLVSQ 65
Cdd:COG2874   16 GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGlsvtyistelTTKEFIKQMKSLSYDISdyllrGRLLFLPVHPLGFE 95

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 918566729  66 PDTGE--QALE-----IADALVRSgsiDMIVIDSVAALV 97
Cdd:COG2874   96 WNSKQrkDLLKrlmkyIASNLWEA---DVIIIDSLSALL 131
KaiC-N cd19485
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ...
 1-96 4.13e-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: 35.04  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAE-MQKLGGTAAFIDAEHALD--IQYAGKLGVNVADLLVS------------- 64
Cdd:cd19485   14 GGLPKGRPTLICGTAGTGKTLFAAQFLVNgIKEFGEPGVFVTFEESPEdiIKNMASFGWDLPKLVAEgkllildaspeps 93

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 918566729  65 -QPDTGEQALE-----IADAlVRSGSIDMIVIDSVAAL 96
Cdd:cd19485   94 eEEVTGEYDLEallirIEYA-IRKIGAKRVSLDSLEAV 130
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
 1-96 4.39e-03

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: 35.03  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTL--TLQVIAEMQKL----GGTAAFIDAEHALD----IQYAGKLGVN----VADLLVSQP 66
Cdd:cd19514   14 GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGVDhdavLDNILYARA 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 918566729  67 DTGEQALEIADAL----VRSGSIDMIVIDSVAAL 96
Cdd:cd19514   94 YTSEHQMELLDYVaakfHEEAVFRLLIIDSIMAL 127
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 4-36 4.98e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 34.75  E-value: 4.98e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 918566729   4 PRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGT 36
Cdd:cd03250   29 PKGELVAIVGPVGSGKSSLLSALLGELEKLSGS 61
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 1-96 6.42e-03

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: 34.65  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918566729   1 GGLPRGRVVEIYGPESSGKTTLTLQVIAEMQK------LGGTAAFIDAEHALD----IQYAGKLGVNVADLL----VSQP 66
Cdd:cd19515   14 GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGLDPDEVLdniyVARA 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 918566729  67 -DTGEQAL---EIADALVRSGSIDMIVIDSVAAL 96
Cdd:cd19515   94 yNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSH 127
 
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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