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Conserved domains on  [gi|259479087|dbj|BAI40091|]
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recombinase A, partial [Aeromonas sp. GV20]

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
 1-157 4.35e-133

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 374.90  E-value: 4.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:PRK09354  75 TLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:PRK09354 155 EIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 231
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-157 4.35e-133

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 374.90  E-value: 4.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:PRK09354  75 TLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:PRK09354 155 EIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 231
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-157 9.08e-129

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 364.11  E-value: 9.08e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:COG0468   78 TLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKA 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:COG0468  158 EIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 234
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-157 5.13e-118

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: 333.60  E-value: 5.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087    1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:pfam00154  67 TLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKA 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087   81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:pfam00154 147 EIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQ 223
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-157 1.29e-116

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: 332.03  E-value: 1.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087    1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:TIGR02012  70 TLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKA 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087   81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:TIGR02012 150 EIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 226
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-157 1.79e-114

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: 323.35  E-value: 1.79e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:cd00983   39 TLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKA 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:cd00983  119 EIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIEL 195
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1-155 4.81e-03

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: 35.43  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087     1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKa 80
Cdd:smart00382  17 TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKPDVLILDEITSLLDA- 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259479087    81 eiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQirmkigvmfgsPETTTGGNALKFYASVRLDIRRI 155
Cdd:smart00382  94 ----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRRRFDRRIVLLLI 147
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
 1-157 4.35e-133

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 374.90  E-value: 4.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:PRK09354  75 TLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:PRK09354 155 EIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 231
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-157 9.08e-129

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 364.11  E-value: 9.08e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:COG0468   78 TLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKA 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:COG0468  158 EIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 234
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
 1-157 5.13e-118

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: 333.60  E-value: 5.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087    1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:pfam00154  67 TLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKA 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087   81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:pfam00154 147 EIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQ 223
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
 1-157 1.29e-116

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: 332.03  E-value: 1.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087    1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:TIGR02012  70 TLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKA 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087   81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:TIGR02012 150 EIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGT 226
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-157 1.79e-114

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: 323.35  E-value: 1.79e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:cd00983   39 TLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKA 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGA 157
Cdd:cd00983  119 EIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIEL 195
recA PRK09519
intein-containing recombinase RecA;
1-155 9.87e-76

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 240.38  E-value: 9.87e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKA 80
Cdd:PRK09519  75 TVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259479087  81 EIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRI 155
Cdd:PRK09519 155 ELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRV 229
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 1-154 5.51e-43

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: 140.57  E-value: 5.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYA-----------AKLGVNVDDLLISQPDTGEQALEICDMLVRSNA----V 65
Cdd:cd01393   16 QLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLLALDSLPESLFpppnT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087  66 DVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMFG-SPETTTGGNALKF 144
Cdd:cd01393   96 SLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGSGaSLVPPALGNTWEH 175

                        170
                 ....*....|
gi 259479087 145 YASVRLDIRR 154
Cdd:cd01393  176 SVSTRLLLYR 185
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 1-151 6.28e-06

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: 44.23  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087   1 TLTLQVIAEAQKKGKTCAFVDAEhALDP-----IYAAKLGVNVDDLLISQP-DTGEQALEICDM--LVRSNAVDVIIVDS 72
Cdd:cd01394   34 NICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNIIVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087  73 VAALTpKAEiegEMGDShvGLQARLMSQaLRKLTANIKNANCLCIFINQIRMKIGVMFGSPettTGGNALKfYAS---VR 149
Cdd:cd01394  113 ATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVITNQVYSDIDDDRLKP---VGGTLLE-HWSkaiIR 181


                 ..
gi 259479087 150 LD 151
Cdd:cd01394  182 LE 183
radA PRK04301
DNA repair and recombination protein RadA; Validated
 21-154 9.71e-05

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 41.02  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087  21 DAEHALDPIYAAKlGVNVDD--LLIsqpdtgEQALEICDmlvRSNAVDVIIVDSVAALTpKAEiegemgdsHVGL----- 93
Cdd:PRK04301 163 DPDEVLDNIHVAR-AYNSDHqmLLA------EKAEELIK---EGENIKLVIVDSLTAHF-RAE--------YVGRgnlae 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259479087  94 -QARLMSQ--ALRKLtANIKNanCLCIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRR 154
Cdd:PRK04301 224 rQQKLNKHlhDLLRL-ADLYN--AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
 21-154 1.62e-04

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: 40.42  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087  21 DAEHALDPIYAAKlGVNVD-DLLISQpdtgeqalEICDMLVRSNAVDVIIVDSVAALTpKAEI--EGEMGDSHVGLqARL 97
Cdd:cd19515   80 DPDEVLDNIYVAR-AYNSNhQMLLVE--------KAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKH 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 259479087  98 MSQALRklTANIKNAnclCIFI-NQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRR 154
Cdd:cd19515  149 LHDLHR--LADLYNI---AVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1-155 4.81e-03

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: 35.43  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259479087     1 TLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKa 80
Cdd:smart00382  17 TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKPDVLILDEITSLLDA- 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259479087    81 eiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQirmkigvmfgsPETTTGGNALKFYASVRLDIRRI 155
Cdd:smart00382  94 ----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRRRFDRRIVLLLI 147
 
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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