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Conserved domains on  [gi|721346924|gb|AIX09779|]
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recombinase A, partial [Mesorhizobium sp. RITF721]

Protein Classification

recombinase RecA family protein( domain architecture ID 1000164)

recombinase RecA catalyzes an ATP-dependent DNA strand-exchange reaction, which is a critical step in the repair of DNA double-strand breaks by homologous recombination

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
recA super family cl35814
recombinase A; Provisional
1-145 3.13e-122

recombinase A; Provisional


The actual alignment was detected with superfamily member PRK09354:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 346.78  E-value: 3.13e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:PRK09354  51 ALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:PRK09354 131 DTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQ 195
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-145 3.13e-122

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 346.78  E-value: 3.13e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:PRK09354  51 ALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:PRK09354 131 DTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQ 195
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-145 1.63e-118

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 337.53  E-value: 1.63e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:COG0468   54 ALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:COG0468  134 ETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQ 198
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-145 7.25e-110

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: 312.41  E-value: 7.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:pfam00154  43 ALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924   81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:pfam00154 123 DMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQ 187
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
1-145 1.24e-108

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: 308.33  E-value: 1.24e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:cd00983   15 ALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd00983   95 DTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQ 159
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-145 1.11e-107

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: 308.92  E-value: 1.11e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:TIGR02012  46 ALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIA 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924   81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:TIGR02012 126 ETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQ 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
9-145 2.43e-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: 49.68  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924     9 RGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISqpDTGEQALEICDTLVRSGA 88
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 721346924    89 IDVLVVDSVAALTPRAEiegemgdalpgLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:smart00382  79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTTN 124
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-145 3.13e-122

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 346.78  E-value: 3.13e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:PRK09354  51 ALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:PRK09354 131 DTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQ 195
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-145 1.63e-118

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 337.53  E-value: 1.63e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:COG0468   54 ALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:COG0468  134 ETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQ 198
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
1-145 7.25e-110

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: 312.41  E-value: 7.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:pfam00154  43 ALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924   81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:pfam00154 123 DMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQ 187
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
1-145 1.24e-108

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: 308.33  E-value: 1.24e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:cd00983   15 ALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd00983   95 DTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQ 159
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
1-145 1.11e-107

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: 308.92  E-value: 1.11e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:TIGR02012  46 ALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIA 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924   81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:TIGR02012 126 ETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQ 190
recA PRK09519
intein-containing recombinase RecA;
1-145 1.07e-73

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 234.22  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEIC 80
Cdd:PRK09519  51 ALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIA 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  81 DTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:PRK09519 131 DMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQ 195
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
10-145 2.31e-41

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: 135.94  E-value: 2.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  10 GRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYAR-----------KLGVDLENLLISQPDTGEQALE 78
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 721346924  79 ICDTLVRSGA----IDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd01393   81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQ 151
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
5-145 1.78e-15

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


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 70.04  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEhALDP-----VYARKLGVDLENLLISQP-DTGEQALE 78
Cdd:cd01394   14 GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNIIVFEPySFDEQGVA 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  79 ICDT--LVRSGAIDVLVVDSVAALTpRAEiegEMGDAlpGLQARLMSQaLRKLtASISRS-NTMVIFINQ 145
Cdd:cd01394   93 IQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKL-LSIARKyDIPVVITNQ 154
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
5-145 5.73e-14

DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).


Pssm-ID: 274047 [Multi-domain]  Cd Length: 209  Bit Score: 65.90  E-value: 5.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEhALDPVYARKLGVD-----LENLLISQP-DTGEQALE 78
Cdd:TIGR02237   7 GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfDFDEQGVA 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721346924   79 ICDT--LVRSGAIDVLVVDSVAALTpRAEIEGEMGDALPGLQARLmsQALRKLTAsisRSNTMVIFINQ 145
Cdd:TIGR02237  86 IQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLAR---KKNLAVVITNQ 148
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
5-145 2.93e-11

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 58.77  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPV--YARKLGVDLE------NLLISQPDTGEQA 76
Cdd:COG0467   15 GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEeyiesgLLRIIDLSPEELG 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  77 LEICDTL------VRSGAIDVLVVDSVAALTpraeiegemgDALPGLQARLmsQALRKLTASISRSNTMVIFINQ 145
Cdd:COG0467   95 LDLEELLarlreaVEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKKRGVTTLLTSE 157
radB PRK09361
DNA repair and recombination protein RadB; Provisional
5-145 5.79e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 57.95  E-value: 5.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEhALDPVYARKLGVD-----LENLLISQP-DTGEQALE 78
Cdd:PRK09361  18 GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIAGEdfeelLSNIIIFEPsSFEEQSEA 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 721346924  79 ICDT--LVRSGaIDVLVVDSVAALTpRAEIEGEMGDalpglqarlmSQALRKLTASIS-------RSNTMVIFINQ 145
Cdd:PRK09361  97 IRKAekLAKEN-VGLIVLDSATSLY-RLELEDEEDN----------SKLNRELGRQLThllklarKHDLAVVITNQ 160
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
1-104 9.85e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 57.25  E-value: 9.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGVGGLPRGRIVEIYGPE-SSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISQPDTGEQALEI 79
Cdd:COG4544   39 ALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRARRPADALWA 118
                         90       100
                 ....*....|....*....|....*
gi 721346924  80 CDTLVRSGAIDVLVVDsVAALTPRA 104
Cdd:COG4544  119 AEEALRSGACGAVVAW-LERLDLTA 142
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
1-114 1.37e-10

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


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 56.94  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   1 ALGvGGLPRGRIVEIYGPESSGKTTLALHTVAEA---QKKGG---ICAFVDAEHAL------------DPVYARK----- 57
Cdd:cd19493    3 ALA-GGLPLGAITEITGASGSGKTQFALTLASSAampARKGGldgGVLYIDTESKFsaerlaeiaearFPEAFSGfmeen 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 721346924  58 --LGVDLENLLISQPDTGEQALEICDTL---VRSGAIDVLVVDSVAALTpRAEIEGEMGDAL 114
Cdd:cd19493   82 erAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALV-RREFGGSDGEVT 142
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
5-145 2.14e-09

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: 53.81  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVY--ARKLGVDLE------NLLISQPDTGEQA 76
Cdd:cd01124   14 GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemedegKLIIVDAPPTEAG 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 721346924  77 LEICDTL-------VRSGAIDVLVVDSVAALTPRAEiegemgdalpglQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd01124   94 RFSLDELlsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRAAGVTTIFTSE 157
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
5-145 2.12e-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: 51.14  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQ------KKGGICAFVDAEHAL-------------DPVYARKLGVDLENL 65
Cdd:cd19491    7 GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpKRYHLEKAKNFLDNI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  66 LISQ-PDTgeQALEICDT-----LVRSGAIDVLVVDSVAALTpRAEIEGEMGDALpgLQARLMSQALRKLTASISRSNTM 139
Cdd:cd19491   87 FVEHvADL--ETLEHCLNyqlpaLLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLADKYNLA 161

                 ....*.
gi 721346924 140 VIFINQ 145
Cdd:cd19491  162 VVVVNQ 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
9-145 2.43e-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: 49.68  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924     9 RGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYARKLGVDLENLLISqpDTGEQALEICDTLVRSGA 88
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 721346924    89 IDVLVVDSVAALTPRAEiegemgdalpgLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:smart00382  79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTTN 124
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
5-145 5.06e-08

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


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 49.94  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    5 GGLPRGRIVEIYGPESSGKTTLALH-TVAEAQKKGGICAFVDA-EHALDPVY-ARKLGVDLENLL---------ISQPDT 72
Cdd:pfam06745  14 GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLEeegklaiidASTSGI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   73 GEQALEICDTL----------VRSGAIDVLVVDSVAALtprAEIEGEMgdalpglQARlmsQALRKLTASISRSNTMVIF 142
Cdd:pfam06745  94 GIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRRLKRVLKGLGVTAIF 160

                  ...
gi 721346924  143 INQ 145
Cdd:pfam06745 161 TSE 163
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
5-145 7.77e-07

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: 46.53  E-value: 7.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDPV----YARKLGVD----LENLLISQ 69
Cdd:pfam08423  32 GGIETGSITEIFGEFRTGKTQLC-HTLCvtcqlplEMGGGEGKALYIDTEGTFRPErlvaIAERYGLDpedvLDNVAYAR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   70 PDTGEQALEIcdtLVRSGA------IDVLVVDSVAALTpRAEIEGEmGDalpgLQARLM--SQALRKLTASISRSNTMVI 141
Cdd:pfam08423 111 AYNSEHQMQL---LQQAAAmmsesrFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQRLADEFGVAVV 181

                  ....
gi 721346924  142 FINQ 145
Cdd:pfam08423 182 ITNQ 185
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
2-145 1.01e-06

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: 46.20  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   2 LGvGGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDP----VYARKLGVD----LENLL 66
Cdd:cd19514   12 LG-GGIESMSITEVFGEFRTGKTQLS-HTLCvtaqlpgSMGGGGGKVAYIDTEGTFRPdrirPIAERFGVDhdavLDNIL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  67 ISQPDTGEQALEICDTL----VRSGAIDVLVVDSVAAL-----TPRaeieGEMGDAlpglQARLmSQALRKLTASISRSN 137
Cdd:cd19514   90 YARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALfrvdfSGR----GELAER----QQKL-AQMLSRLQKISEEYN 160

                 ....*...
gi 721346924 138 TMVIFINQ 145
Cdd:cd19514  161 VAVFITNQ 168
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
10-145 4.07e-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: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  10 GRIVEIYGPESSGKTTLALHTVAEA---QKKGGICA--------FVDAEHALDPVYARKL-------------------G 59
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCilpSSWGGVPLggleaavvFIDTDGRFDILRLRSIleariraaiqaanssddeeD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  60 VD------LENLLISQPDTGEQ---ALEICDTL----VRSGAIDVLVVDSVAALTPRAEIEGEMGDALPGLQARLMSQAL 126
Cdd:cd19490   81 VEeiarecLQRLHIFRCHSSLQllaTLLSLENYllslSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAIL 160
                        170
                 ....*....|....*....
gi 721346924 127 RKLTASISRSNTMVIFINQ 145
Cdd:cd19490  161 RELRRLRRRFQLVVIATKQ 179
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
5-145 1.29e-05

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: 43.29  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDPV----YARKLGVD----LENLLISQ 69
Cdd:cd01123   14 GGIETGSITEMFGEFRTGKTQLC-HTLAvtcqlpiDRGGGEGKAIYIDTEGTFRPErlraIAQRFGLDpddvLDNVAYAR 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721346924  70 PDTGEQALEICD---TLVRSGAIDVLVVDSVAALTpRAEIEGEmgDALPGLQARLmSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd01123   93 AFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR--GELSARQMHL-AKFLRMLQRLADEFGVAVVVTNQ 167
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
5-145 1.79e-05

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 42.84  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLAlHTVAEA----QKKGGIC---AFVDAEHALDP----VYARKLGVD----LENLLISQ 69
Cdd:PLN03187 121 GGIETRCITEAFGEFRSGKTQLA-HTLCVTtqlpTEMGGGNgkvAYIDTEGTFRPdrivPIAERFGMDadavLDNIIYAR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  70 PDTGEQ---ALEICDTLVRSGAIDVLVVDSVAAL-----TPRAEiegemgdaLPGLQARLmSQALRKLTASISRSNTMVI 141
Cdd:PLN03187 200 AYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALfrvdfTGRGE--------LAERQQKL-AQMLSRLTKIAEEFNVAVY 270

                 ....
gi 721346924 142 FINQ 145
Cdd:PLN03187 271 MTNQ 274
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
5-145 4.60e-05

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


Pssm-ID: 131292 [Multi-domain]  Cd Length: 313  Bit Score: 41.69  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDP----VYARKLGVD----LENLLISQ 69
Cdd:TIGR02238  91 GGIESMSITEVFGEFRCGKTQLS-HTLCvtaqlprEMGGGNGKVAYIDTEGTFRPdrirAIAERFGVDpdavLDNILYAR 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721346924   70 PDTGEQALE---ICDTLVRSGAIDVLVVDSVAALTpRAEIEGEmgDALPGLQARLmSQALRKLTASISRSNTMVIFINQ 145
Cdd:TIGR02238 170 AYTSEHQMElldYLAAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLNKISEEFNVAVFVTNQ 244
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
9-143 5.05e-05

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


Pssm-ID: 433243  Cd Length: 199  Bit Score: 41.16  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924    9 RGRIVEIYGPESSGKTTLAlhtvAEAQKKggicAFVDAEHALDPVYARKLGVdlenllISQPDTGEQALEICDTLVRSG- 87
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFA----KTLPKP----LFLDTEKGSKALDGDRFPD------IVIRDSWQDFLDAIDELTAAEl 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 721346924   88 -AIDVLVVDSVAAL-----------TPRAEIEGEMGDALP-GLQARLMSQALRKLTASISrsntMVIFI 143
Cdd:pfam13479  67 aDYKTIVIDTVDWLerlclayickqNGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGK----NVIFT 131
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
5-127 6.25e-05

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: 41.18  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFV---DAEHALDPVyARKLGVDLENLLI---SQPDTGEQALE 78
Cdd:cd19488   14 GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAV-ALSHGWSLDGIHIfelSPSESALDAAQ 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 721346924  79 ICDTL----VRSGAIDVLVVDSVAALTP-RAEIegemgDALpgLQARLMSQ-ALR 127
Cdd:cd19488   93 QYTILhpseLELSETTRLIFERVERLKPsRVVI-----DSL--SELRLLAQdSLR 140
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
5-145 6.50e-05

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 41.26  E-value: 6.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-EAQ---KKG---GICAFVDAEHALDP----VYARKLGVD----LENLLISQ 69
Cdd:PLN03186 118 GGIETGSITEIYGEFRTGKTQLC-HTLCvTCQlplDQGggeGKAMYIDTEGTFRPqrliQIAERFGLNgadvLENVAYAR 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  70 PDTGEQALEIcdtLVRSGAI------DVLVVDSVAALTpRAEIEGEmGDalpgLQAR--LMSQALRKLTASISRSNTMVI 141
Cdd:PLN03186 197 AYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKFLRSLQRLADEFGVAVV 267

                 ....
gi 721346924 142 FINQ 145
Cdd:PLN03186 268 ITNQ 271
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
10-145 2.84e-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: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  10 GRIVEIYGPESSGKTTLALHTVAEAQKK------GGICAFVDAEHALDPVYARKLgvDLENLLisqpdtgeQALEICDTL 83
Cdd:cd19492    1 GKITEICGVPGVGKTQLCMQLAVNVQIPkcfgglAGEAIYIDTEGSFNIHYFRVH--DYVELL--------ALINSLPKF 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 721346924  84 VRSGA-IDVLVVDSVaALTPRAEIEGemgdalPGLQARLMSQALRKLTASISRSNTMVIFINQ 145
Cdd:cd19492   71 LEDHPkVKLIVVDSI-AFPFRHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQ 126
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
5-98 2.98e-04

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


Pssm-ID: 410895 [Multi-domain]  Cd Length: 219  Bit Score: 39.20  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVYAR--KLGVDLE------NLLISQPDTGE-- 74
Cdd:cd19487   14 GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERseALGIDLRamvekgLLSIEQIDPAEls 93
                         90       100
                 ....*....|....*....|....*.
gi 721346924  75 --QALEICDTLVRSGAIDVLVVDSVA 98
Cdd:cd19487   94 pgEFAQRVRTSVEQEDARVVVIDSLN 119
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
2-97 3.43e-04

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: 39.05  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   2 LGvGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPV--YARKLGVDLENLLIsqpdTGEQALE- 78
Cdd:cd01121   75 LG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSDNLYL----LAETNLEa 149
                         90
                 ....*....|....*....
gi 721346924  79 ICDTLVRSgAIDVLVVDSV 97
Cdd:cd01121  150 ILAEIEEL-KPSLVVIDSI 167
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
5-35 6.30e-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: 6.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 721346924   5 GGLPRGRIVEIYGPESSGKT----TLALHTVAEAQ 35
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTqlclTAAANVASRSG 36
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
11-82 8.07e-04

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: 37.49  E-value: 8.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  11 RIVeIYGPESSGKTTLA------LHT--VAEA-----QKKGGICAFVDaehaLDPVYARKLgvDLENLLISQPDtgeqAL 77
Cdd:COG3172   10 KIV-LLGAESTGKTTLAralaahYNTpwVPEYgreylEEKGRALTYDD----LLAIARGQL--ALEDAAAKRAN----KL 78

                 ....*
gi 721346924  78 EICDT 82
Cdd:COG3172   79 LFCDT 83
PTZ00035 PTZ00035
Rad51 protein; Provisional
5-100 1.11e-03

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 37.67  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDP----VYARKLGVD----LENLLISQ 69
Cdd:PTZ00035 113 GGIETGSITELFGEFRTGKTQLC-HTLCvtcqlpiEQGGGEGKVLYIDTEGTFRPerivQIAERFGLDpedvLDNIAYAR 191
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 721346924  70 PDTGEQALEIcdtLVRSGAIDV------LVVDSVAAL 100
Cdd:PTZ00035 192 AYNHEHQMQL---LSQAAAKMAeerfalLIVDSATAL 225
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
7-143 1.37e-03

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 37.57  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   7 LPRGRIVEIYGPESSGKTTLALH---TVAEAQK------KGGICAFVDAE----------HALDPVYARKLGVDLENLLI 67
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAGGPwlgrrvPPGKVLYLAAEddrgelrrrlKALGADLGLPFADLDGRLRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  68 SQPDTGEQALEICDTL---VRSGAIDVLVVDSVAALTPRAEIE-GEMGDALpglqarlmsQALRKLtasISRSNTMVIFI 143
Cdd:COG3598   90 LSLAGDLDDTDDLEALeraIEEEGPDLVVIDPLARVFGGDENDaEEMRAFL---------NPLDRL---AERTGAAVLLV 157
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
12-46 1.84e-03

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: 36.91  E-value: 1.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 721346924   12 IVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDA 46
Cdd:pfam01637  22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDP 56
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
5-145 2.14e-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: 36.91  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   5 GGLPRGRIVEIYGPESSGKTTLAlHTVA-------EAQKKGGICAFVDAEHALDPV----YARKLGVD----LENLLISQ 69
Cdd:cd19513   14 GGIETGSITELFGEFRTGKTQLC-HTLAvtcqlpiDQGGGEGKALYIDTEGTFRPErllaIAERYGLNgedvLDNVAYAR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924  70 PDTGEQALEIcdtLVRSGAI------DVLVVDSVAALTpRAEIEGEmGDalpgLQARLM--SQALRKLTASISRSNTMVI 141
Cdd:cd19513   93 AYNTDHQMQL---LIQASAMmaesryALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQRLADEFGVAVV 163

                 ....
gi 721346924 142 FINQ 145
Cdd:cd19513  164 ITNQ 167
AAA_22 pfam13401
AAA domain;
11-104 5.79e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 34.62  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   11 RIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEH-----ALDPVYARKLGVDLENllisqPDTGEQALE-ICDTLV 84
Cdd:pfam13401   6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSgtspkDLLRALLRALGLPLSG-----RLSKEELLAaLQQLLL 80
                          90       100
                  ....*....|....*....|
gi 721346924   85 RSGAIDVLVVDSVAALTPRA 104
Cdd:pfam13401  81 ALAVAVVLIIDEAQHLSLEA 100
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
8-46 7.80e-03

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


Pssm-ID: 440952  Cd Length: 353  Bit Score: 35.38  E-value: 7.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 721346924   8 PRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDA 46
Cdd:COG1341   33 SGPGRIMVLGPVDSGKSTLTTLLANKLLAEGLKVAIIDA 71
KaiC_C cd19484
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ...
2-101 7.93e-03

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


Pssm-ID: 410892 [Multi-domain]  Cd Length: 218  Bit Score: 35.00  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 721346924   2 LGVGGLPRGRIVEIYGPESSGKTTLALHTVAEAQKKGGICAFVDAEHALDPVY--ARKLGVDLENLLISQ---------P 70
Cdd:cd19484   12 LGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERKGllkiicarpE 91
                         90       100       110
                 ....*....|....*....|....*....|..
gi 721346924  71 DTG-EQALEICDTLVRSGAIDVLVVDSVAALT 101
Cdd:cd19484   92 LYGlEDHLIIIKSEINEFKPSRVIVDPLSALA 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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