NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|410369280|gb|AFV66638|]
View 

recombinase A, partial [Aeromonas sp. REm-amp_154]

Protein Classification

recombinase RecA( domain architecture ID 11484000)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-209 1.94e-168

recombinase A; Provisional


:

Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 466.58  E-value: 1.94e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   1 QKQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ 80
Cdd:PRK09354   6 EKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  81 KKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHV 160
Cdd:PRK09354  86 KAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 161 GLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:PRK09354 166 GLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGN 214
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-209 1.94e-168

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 466.58  E-value: 1.94e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   1 QKQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ 80
Cdd:PRK09354   6 EKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  81 KKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHV 160
Cdd:PRK09354  86 KAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 161 GLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:PRK09354 166 GLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGN 214
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-209 5.00e-165

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 458.10  E-value: 5.00e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   1 QKQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ 80
Cdd:COG0468    9 EKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  81 KKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHV 160
Cdd:COG0468   89 KAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 161 GLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:COG0468  169 GLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGN 217
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
2-209 6.44e-148

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: 413.69  E-value: 6.44e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    2 KQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK 81
Cdd:TIGR02012   2 KQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   82 KGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVG 161
Cdd:TIGR02012  82 AGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 410369280  162 LQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:TIGR02012 162 LQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGN 209
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
4-209 2.11e-147

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: 410.25  E-value: 2.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    4 KALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKG 83
Cdd:pfam00154   1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   84 KVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQ 163
Cdd:pfam00154  81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 410369280  164 ARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGR 206
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
32-209 2.05e-128

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: 361.10  E-value: 2.05e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  32 DIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLL 111
Cdd:cd00983    1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 112 ISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQI 191
Cdd:cd00983   81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
                        170
                 ....*....|....*...
gi 410369280 192 RMKI*VMFGSPETTTGGN 209
Cdd:cd00983  161 REKIGVMFGNPETTTGGN 178
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
55-195 1.30e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.99  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    55 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAV 134
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410369280   135 DVIIVDSVAALTPKaeiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKI 195
Cdd:smart00382  80 DVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDL 129
 
Name Accession Description Interval E-value
recA PRK09354
recombinase A; Provisional
1-209 1.94e-168

recombinase A; Provisional


Pssm-ID: 236476 [Multi-domain]  Cd Length: 349  Bit Score: 466.58  E-value: 1.94e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   1 QKQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ 80
Cdd:PRK09354   6 EKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  81 KKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHV 160
Cdd:PRK09354  86 KAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 161 GLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:PRK09354 166 GLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGN 214
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
1-209 5.00e-165

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


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 458.10  E-value: 5.00e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   1 QKQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ 80
Cdd:COG0468    9 EKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  81 KKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHV 160
Cdd:COG0468   89 KAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHV 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 161 GLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:COG0468  169 GLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGN 217
tigrfam_recA TIGR02012
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ...
2-209 6.44e-148

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: 413.69  E-value: 6.44e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    2 KQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK 81
Cdd:TIGR02012   2 KQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   82 KGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVG 161
Cdd:TIGR02012  82 AGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 410369280  162 LQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:TIGR02012 162 LQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGN 209
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
4-209 2.11e-147

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: 410.25  E-value: 2.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    4 KALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKG 83
Cdd:pfam00154   1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   84 KVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQ 163
Cdd:pfam00154  81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 410369280  164 ARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGR 206
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
32-209 2.05e-128

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: 361.10  E-value: 2.05e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  32 DIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLL 111
Cdd:cd00983    1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 112 ISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQI 191
Cdd:cd00983   81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
                        170
                 ....*....|....*...
gi 410369280 192 RMKI*VMFGSPETTTGGN 209
Cdd:cd00983  161 REKIGVMFGNPETTTGGN 178
recA PRK09519
intein-containing recombinase RecA;
2-208 6.75e-100

intein-containing recombinase RecA;


Pssm-ID: 77219 [Multi-domain]  Cd Length: 790  Bit Score: 306.25  E-value: 6.75e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   2 KQKALAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK 81
Cdd:PRK09519   7 REKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  82 KGKVCAFIDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVG 161
Cdd:PRK09519  87 AGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVG 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 410369280 162 LQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMFGSPETTTGG 208
Cdd:PRK09519 167 LQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGG 213
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
55-209 1.66e-47

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: 154.05  E-value: 1.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  55 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYA-----------AKLGVNVDDLLISQPDTGEQALE 123
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 124 ICDMLVRSNA----VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKI*VMF 199
Cdd:cd01393   81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
                        170
                 ....*....|.
gi 410369280 200 G-SPETTTGGN 209
Cdd:cd01393  161 GaSLVPPALGN 171
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
36-195 3.10e-17

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: 76.58  E-value: 3.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDP-----IYAAKLGVNVDDL 110
Cdd:cd01394    1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 111 LISQP-DTGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEiegEMGDShvGLQARLMSQaLRKLTANIKNANCLCIF 187
Cdd:cd01394   79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151

                 ....*...
gi 410369280 188 INQIRMKI 195
Cdd:cd01394  152 TNQVYSDI 159
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
36-193 6.49e-15

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 70.33  E-value: 6.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPI--YAAKLGVNVDDLL-- 111
Cdd:COG0467    2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 112 ----ISQPDTGEQALEICDML------VRSNAVDVIIVDSVAALtpkaeiEGEMGDShvglqaRLMSQALRKLTANIKNA 181
Cdd:COG0467   81 gllrIIDLSPEELGLDLEELLarlreaVEEFGAKRVVIDSLSGL------LLALPDP------ERLREFLHRLLRYLKKR 148
                        170
                 ....*....|..
gi 410369280 182 NCLCIFINQIRM 193
Cdd:COG0467  149 GVTTLLTSETGG 160
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
43-192 1.23e-12

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: 63.97  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   43 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDP-----IYAAKLGVNVDDLLISQP-D 116
Cdd:TIGR02237   1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkqIAEDRPERALSNFIVFEVfD 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410369280  117 TGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEIEGEMGDSHVGLQARLmsQALRKLTANIKNAnclCIFINQIR 192
Cdd:TIGR02237  79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLARKKNLA---VVITNQVY 150
radA PRK04301
DNA repair and recombination protein RadA; Validated
31-209 4.02e-12

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 63.74  E-value: 4.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  31 MDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK------KGKVCAFIDAE------------ 92
Cdd:PRK04301  79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEgtfrperieqma 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  93 --------HALDPIYAAKlGVNVDD--LLIsqpdtgEQALEICDmlvRSNAVDVIIVDSVAALTpKAEiegemgdsHVGL 162
Cdd:PRK04301 158 ealgldpdEVLDNIHVAR-AYNSDHqmLLA------EKAEELIK---EGENIKLVIVDSLTAHF-RAE--------YVGR 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 410369280 163 ------QARLMSQ--ALRKLtANIKnaNCLCIFINQIRMKI*VMFGSPETTTGGN 209
Cdd:PRK04301 219 gnlaerQQKLNKHlhDLLRL-ADLY--NAAVVVTNQVMARPDAFFGDPTQPIGGH 270
COG4544 COG4544
Uncharacterized conserved protein [Function unknown];
35-149 5.05e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443609 [Multi-domain]  Cd Length: 230  Bit Score: 62.64  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  35 AISTGSLSLDVALGIGGLPCGRIVEIYGPE-SSGKTTLTLQVIAEAQKKGKVCAFIDAEHALdpiYA---AKLGVNVDDL 110
Cdd:COG4544   28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410369280 111 LISQPDTGEQALEICDMLVRSNAVDVIIVDsVAALTPKA 149
Cdd:COG4544  105 LLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
radB PRK09361
DNA repair and recombination protein RadB; Provisional
33-145 4.40e-11

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 59.88  E-value: 4.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  33 IEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEhALDPIYAAKL-GVNVDDLL 111
Cdd:PRK09361   2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 410369280 112 ----ISQP-DTGEQALEICDM--LVRSNaVDVIIVDSVAAL 145
Cdd:PRK09361  80 sniiIFEPsSFEEQSEAIRKAekLAKEN-VGLIVLDSATSL 119
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
36-209 2.76e-10

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: 57.76  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK-------KGKVcAFIDAEHALDP----IYAAKLG 104
Cdd:cd19515    1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeegglNGKA-VYIDTENTFRPerimQMAKALG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 105 VNVDDLL-----ISQPDTGEQAL---EICDMLVRSNAVDVIIVDSVAALTpKAEI--EGEMGDSHVGLqARLMSQALRkl 174
Cdd:cd19515   79 LDPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR-- 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 410369280 175 TANIKNAnclCIFI-NQIRMKI*VMFGSPETTTGGN 209
Cdd:cd19515  155 LADLYNI---AVLVtNQVMAKPDAFFGDPTQAIGGH 187
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
44-168 9.55e-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: 56.17  E-value: 9.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  44 DVALGiGGLPCGRIVEIYGPESSGKT----TLTLQVIAEAQKKGK--VCAFIDAEHALDP-----IYAAKLGVN------ 106
Cdd:cd19493    1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLdgGVLYIDTESKFSAerlaeIAEARFPEAfsgfme 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410369280 107 --------VDDLLISQPDTGEQALEICDML---VRSNAVDVIIVDSVAALTPKA--EIEGEMGDSHVGLqARLMS 168
Cdd:cd19493   80 eneraeemLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS 153
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
36-145 2.67e-09

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: 55.06  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKK-----GKVCaFIDAEHALDP----IYAAKLG 104
Cdd:cd19514    1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 410369280 105 VN----VDDLLISQPDTGEQALEICDMLVRSNAVD----VIIVDSVAAL 145
Cdd:cd19514   79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMAL 127
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
36-145 3.54e-09

Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.


Pssm-ID: 462471 [Multi-domain]  Cd Length: 255  Bit Score: 55.00  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQK-----KGKvCAFIDAEHALDPI----YAAKLG 104
Cdd:pfam08423  19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLemgggEGK-ALYIDTEGTFRPErlvaIAERYG 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 410369280  105 VNVDDLLISQP-------DTGEQALEICDMLVRSNAVDVIIVDSVAAL 145
Cdd:pfam08423  97 LDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATAL 144
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
36-203 5.66e-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: 54.19  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVD----- 108
Cdd:cd01124    1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemede 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 109 -DLLISQPDTGEQALEICDML-------VRSNAVDVIIVDSVAALTPKAEiegemgdshvglQARLMSQALRKLTANIKN 180
Cdd:cd01124   80 gKLIIVDAPPTEAGRFSLDELlsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
                        170       180
                 ....*....|....*....|....*.
gi 410369280 181 ANCLCIFINQ---IRMKI*VMFGSPE 203
Cdd:cd01124  148 AGVTTIFTSEmrsFLSSESAGGGDVS 173
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
36-209 1.14e-08

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: 53.30  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDPI----YAAKLG 104
Cdd:cd01123    1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVtcqlpIDRGGGEGK-AIYIDTEGTFRPErlraIAQRFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 105 VNVDDLL----ISQPDTGEQALEICD----MLVRSnAVDVIIVDSVAALTPKAEI-EGEMGDSHVGLqARLMSQALRklt 175
Cdd:cd01123   79 LDPDDVLdnvaYARAFNSDHQTQLLDqaaaMMVES-RFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLRMLQR--- 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 410369280 176 anIKNANCLCIFI-NQIRMKI---*VMFGSPETTTGGN 209
Cdd:cd01123  154 --LADEFGVAVVVtNQVVAQVdgaMMFAADPKKPIGGN 189
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
55-195 1.30e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.99  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280    55 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAV 134
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410369280   135 DVIIVDSVAALTPKaeiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKI 195
Cdd:smart00382  80 DVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDL 129
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
36-193 3.48e-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: 51.86  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   36 ISTGSLSLDvALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAE-AQKKGKVCAFIDA-EHALDPIYAAK-LGVNVDDLL- 111
Cdd:pfam06745   1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLRENARsFGWDLEKLEe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  112 --------ISQPDTGEQALEICDML----------VRSNAVDVIIVDSVAALtpkAEIEGEMgdshvglQARlmsQALRK 173
Cdd:pfam06745  80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
                         170       180
                  ....*....|....*....|
gi 410369280  174 LTANIKNANCLCIFINQIRM 193
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPS 166
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
43-191 7.27e-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: 7.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  43 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ------KKGKVCAFIDAEHAL----------------DPIYA 100
Cdd:cd19491    1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 101 AKLGVNVddLLISQPDTgeQALEICDM-----LVRSNAVDVIIVDSVAALtpkAEIEGEMGDSHVGLQARLMSQALRKLT 175
Cdd:cd19491   80 KNFLDNI--FVEHVADL--ETLEHCLNyqlpaLLERGPIRLVVIDSIAAL---FRSEFDTSRSDLVERAKYLRRLADHLK 152
                        170
                 ....*....|....*.
gi 410369280 176 ANIKNANCLCIFINQI 191
Cdd:cd19491  153 RLADKYNLAVVVVNQV 168
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
32-175 1.38e-07

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 50.89  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  32 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDP----IYA 100
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVtcqlpLDQGGGEGK-AMYIDTEGTFRPqrliQIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 101 AKLGVNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAALTpKAEIEGEmGDshvgLQAR--LMSQA 170
Cdd:PLN03186 179 ERFGLNGADVLenvayARAYNTDHQSellLEAASMMAETR-FALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKF 251

                 ....*
gi 410369280 171 LRKLT 175
Cdd:PLN03186 252 LRSLQ 256
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
23-142 5.28e-07

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 48.68  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  23 MRLGDSKTMDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAE-AQKKGKVcAFIDAEHALDPI--Y 99
Cdd:cd01121   51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARlAQRGGKV-LYVSGEESLSQIklR 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 410369280 100 AAKLGVNVDDLLIsqpdTGEQALE-ICDMLVRSNAvDVIIVDSV 142
Cdd:cd01121  129 AERLGLGSDNLYL----LAETNLEaILAEIEELKP-SLVVIDSI 167
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
36-145 3.50e-06

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


Pssm-ID: 131292 [Multi-domain]  Cd Length: 313  Bit Score: 46.31  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKK-----GKVCaFIDAEHALDP----IYAAKLG 104
Cdd:TIGR02238  78 ITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREmgggnGKVA-YIDTEGTFRPdrirAIAERFG 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 410369280  105 VN----VDDLLISQPDTGEQALEICDMLVRSNAVD---VIIVDSVAAL 145
Cdd:TIGR02238 156 VDpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMAL 203
KaiC-like_N cd19488
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
36-128 4.10e-06

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


Pssm-ID: 410896 [Multi-domain]  Cd Length: 225  Bit Score: 45.80  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVDDLLI- 112
Cdd:cd19488    1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRavALSHGWSLDGIHIf 79
                         90
                 ....*....|....*...
gi 410369280 113 --SQPDTGEQALEICDML 128
Cdd:cd19488   80 elSPSESALDAAQQYTIL 97
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
36-209 5.48e-06

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: 45.39  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDP----IYAAKLG 104
Cdd:cd19513    1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPerllAIAERYG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 105 VNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAALTpKAEIEGEmGDshvgLQARLM--SQALRKL 174
Cdd:cd19513   79 LNGEDVLdnvayARAYNTDHQMqllIQASAMMAESR-YALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRML 151
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 410369280 175 TaNIKNANCLCIFI-NQIRMKI--*VMF-GSPETTTGGN 209
Cdd:cd19513  152 Q-RLADEFGVAVVItNQVVAQVdgAAMFaGDPKKPIGGN 189
PTZ00035 PTZ00035
Rad51 protein; Provisional
36-145 9.40e-06

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 45.37  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAE-----AQKKGKVCaFIDAEHALDP-----IyAAKL 103
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGKVL-YIDTEGTFRPerivqI-AERF 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 410369280 104 GVN----VDDLLISQPDTGEQALE----ICDMLVRSNAVdVIIVDSVAAL 145
Cdd:PTZ00035 177 GLDpedvLDNIAYARAYNHEHQMQllsqAAAKMAEERFA-LLIVDSATAL 225
FlaH COG2874
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
36-146 1.20e-05

Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];


Pssm-ID: 442121  Cd Length: 230  Bit Score: 44.44  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHA----LDPIYAakLGVNVDDLL 111
Cdd:COG2874    3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTtkefIKQMKS--LSYDISDYL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410369280 112 IS--------QPDTGE----QALEICDMLVRSNA-----VDVIIVDSVAALT 146
Cdd:COG2874   80 LRgrllflpvHPLGFEwnskQRKDLLKRLMKYIAsnlweADVIIIDSLSALL 131
recomb_RAD51 TIGR02239
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ...
32-145 3.64e-05

DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).


Pssm-ID: 274048 [Multi-domain]  Cd Length: 316  Bit Score: 43.56  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   32 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKvCAFIDAEHALDPI----YA 100
Cdd:TIGR02239  74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIA 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 410369280  101 AKLGVNVDDLLIS-------QPDTGEQALEICDMLVRSNAVDVIIVDSVAAL 145
Cdd:TIGR02239 152 ERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATAL 203
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
55-194 8.31e-05

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: 41.95  E-value: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  55 GRIVEIYGPESSGKTTLTLQVIAEA-----------QKKGKVCAFIDAEHALDP-----IYAAKLGVNVDDLLISQPDTG 118
Cdd:cd19490    1 GDVIEITGPSGSGKTELLYHLAARCilpsswggvplGGLEAAVVFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280 119 -EQALEIC-----------------------DMLVRSNA---VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQAL 171
Cdd:cd19490   81 vEEIAREClqrlhifrchsslqllatllsleNYLLSLSAnpeLGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAIL 160
                        170       180
                 ....*....|....*....|...
gi 410369280 172 RKLTANIKNANCLCIFINQIRMK 194
Cdd:cd19490  161 RELRRLRRRFQLVVIATKQALFP 183
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
50-79 1.18e-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: 41.47  E-value: 1.18e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 410369280  50 GGLPCGRIVEIYGPESSGKTTLTLQVIAEA 79
Cdd:cd19489    2 GGLRTGEITELVGESSSGKTQLCLTAAANV 31
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
32-145 1.19e-04

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 42.07  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  32 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKVcAFIDAEHALDP----IYA 100
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVttqlpTEMGGGNGKV-AYIDTEGTFRPdrivPIA 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410369280 101 AKLGVN----VDDLLISQPDTGEQ---ALEICDMLVRSNAVDVIIVDSVAAL 145
Cdd:PLN03187 182 ERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIAL 233
PRK06067 PRK06067
flagellar accessory protein FlaH; Validated
32-152 1.23e-04

flagellar accessory protein FlaH; Validated


Pssm-ID: 180381  Cd Length: 234  Bit Score: 41.50  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  32 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPiYAAK---LGVNVD 108
Cdd:PRK06067   3 KKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKS-YLKQmesVKIDIS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 410369280 109 DLLIS---------------QPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIE 152
Cdd:PRK06067  81 DFFLWgylrifplntegfewNSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
57-91 5.48e-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: 39.61  E-value: 5.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 410369280   57 IVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDA 91
Cdd:pfam01637  22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDP 56
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
52-174 7.10e-04

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 39.50  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  52 LPCGRIVEIYGPESSGKTTLTLQV---IAEAQ-------KKGKVcAFIDAEHALDPI------YAAKLGVNVDDL----- 110
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQLaaaVAAGGpwlgrrvPPGKV-LYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlr 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410369280 111 LIS-----QPDTGEQALEicdMLVRSNAVDVIIVDSVAALTPkaeiegemGDSHVGLQARLMSQALRKL 174
Cdd:COG3598   89 LLSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL 146
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
56-142 7.42e-04

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


Pssm-ID: 433243  Cd Length: 199  Bit Score: 39.23  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280   56 RIVeIYGPESSGKTTLtlqvIAEAQKKgkvcAFIDAEHALDPIYAAKLGVnvddllISQPDTGEQALEICDMLVRSNAV- 134
Cdd:pfam13479   4 KIL-IYGPSGIGKTTF----AKTLPKP----LFLDTEKGSKALDGDRFPD------IVIRDSWQDFLDAIDELTAAELAd 68

                  ....*....
gi 410369280  135 -DVIIVDSV 142
Cdd:pfam13479  69 yKTIVIDTV 77
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
49-91 1.57e-03

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


Pssm-ID: 440952  Cd Length: 353  Bit Score: 38.46  E-value: 1.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 410369280  49 IGGLPCGRIVeIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDA 91
Cdd:COG1341   30 ILSSGPGRIM-VLGPVDSGKSTLTTLLANKLLAEGLKVAIIDA 71
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
44-86 1.84e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 38.53  E-value: 1.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 410369280  44 DVALGIgglPCGRIVEIYGPESSGKTTLtLQVIA--EAQKKGKVC 86
Cdd:PRK10851  20 DISLDI---PSGQMVALLGPSGSGKTTL-LRIIAglEHQTSGHIR 60
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
36-87 4.12e-03

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: 36.89  E-value: 4.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410369280  36 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCA 87
Cdd:cd19487    1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSV 51
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
56-74 6.12e-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: 36.34  E-value: 6.12e-03
                         10
                 ....*....|....*....
gi 410369280  56 RIVeIYGPESSGKTTLTLQ 74
Cdd:COG3172   10 KIV-LLGAESTGKTTLARA 27
Tdk COG1435
Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the ...
55-140 7.14e-03

Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441044  Cd Length: 192  Bit Score: 36.23  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  55 GRIVEIYGPESSGKTTLTLQVI--AEAQKKgKVCAFIdaeHALDPIYAAK-----LGVNVDDLLISQPDtgeqalEICDM 127
Cdd:COG1435    4 GKLEFIYGPMFSGKSEELLRRAhnYEEAGQ-KVLLFK---PAIDDRYGEGkivsrIGLSREAIPVDDDT------DILEL 73
                         90
                 ....*....|...
gi 410369280 128 LVRSNAVDVIIVD 140
Cdd:COG1435   74 VREGPDVDVVLID 86
KaiC_C cd19484
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ...
36-146 9.91e-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: 35.77  E-value: 9.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369280  36 ISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKVCAFIDAEHALDPIY--AAKLGVNVDDLLIS 113
Cdd:cd19484    1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 410369280 114 Q---------PDTG-EQALEICDMLVRSNAVDVIIVDSVAALT 146
Cdd:cd19484   81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSALA 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH