|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-242 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 522.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 1 ALKKIEKNFGKGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAY 80
Cdd:PRK09354 14 ALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 81 IDAENALDPVYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMS 160
Cdd:PRK09354 94 IDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 161 QALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNKVA 240
Cdd:PRK09354 174 QALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVA 253
|
..
gi 430769177 241 PP 242
Cdd:PRK09354 254 PP 255
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-242 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 513.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 1 ALKKIEKNFGKGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAY 80
Cdd:COG0468 17 ALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 81 IDAENALDPVYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMS 160
Cdd:COG0468 97 IDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 161 QALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNKVA 240
Cdd:COG0468 177 QALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVA 256
|
..
gi 430769177 241 PP 242
Cdd:COG0468 257 PP 258
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-242 |
4.15e-167 |
|
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: 463.77 E-value: 4.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 1 ALKKIEKNFGKGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAY 80
Cdd:TIGR02012 9 ALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 81 IDAENALDPVYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMS 160
Cdd:TIGR02012 89 IDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 161 QALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNKVA 240
Cdd:TIGR02012 169 QALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVA 248
|
..
gi 430769177 241 PP 242
Cdd:TIGR02012 249 PP 250
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-242 |
2.96e-166 |
|
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: 459.17 E-value: 2.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 1 ALKKIEKNFGKGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAY 80
Cdd:pfam00154 6 ALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 81 IDAENALDPVYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMS 160
Cdd:pfam00154 86 IDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 161 QALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNKVA 240
Cdd:pfam00154 166 QALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVA 245
|
..
gi 430769177 241 PP 242
Cdd:pfam00154 246 PP 247
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
25-242 |
8.35e-159 |
|
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: 439.30 E-value: 8.35e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 25 ISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPVYAEHLGVNIDDLLL 104
Cdd:cd00983 2 VEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 105 SQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMSQALRKLSGTLNKTKTIALFINQIR 184
Cdd:cd00983 82 SQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 430769177 185 EKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNKVAPP 242
Cdd:cd00983 162 EKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPP 219
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-238 |
4.68e-123 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 367.88 E-value: 4.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 1 ALKKIEKNFGKGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAY 80
Cdd:PRK09519 14 AVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 81 IDAENALDPVYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMS 160
Cdd:PRK09519 94 IDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 430769177 161 QALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQIKEGTNIIGNRVRIKVVKNK 238
Cdd:PRK09519 174 QALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
47-215 |
7.02e-48 |
|
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: 156.36 E-value: 7.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 47 GRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPVYA-----------EHLGVNIDDLLLSQPDTGEQGLE 115
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 116 IADALV----SSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLMSQALRKLSGTLNKTKTIALFINQIREKVGVMF 191
Cdd:cd01393 81 ALDSLPeslfPPPNTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 430769177 192 G-NPETTPGGRALKFYATIRLEVRR 215
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
28-220 |
6.92e-21 |
|
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: 87.37 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAE----NALDPVYAEHLGVNIDDLL 103
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEglspERFQQIAGERFESIASNII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 104 LSQP-DTGEQGLEIADA--LVSSGAVDILVVDSVAALVpRAEiegEMGDAhvGLQARLMSQaLRKLSGTLNKTKTIALFI 180
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 430769177 181 NQIREKvgvmFGNPETTP-GGRALKFY--ATIRLE-----VRRAEQIK 220
Cdd:cd01394 153 NQVYSD----IDDDRLKPvGGTLLEHWskAIIRLEksppgLRRATLEK 196
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
35-235 |
1.74e-16 |
|
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: 75.15 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 35 LDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAEnALDPVYAEHLGVNIDDLLLSQ------PD 108
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 109 TGEQGLEIADA--LVSSGAVDILVVDSVAALVpRAEIEGEMGDAHVGLQARLmsqalrKLSGTLNKTKTIALFI-NQIRE 185
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL------TLLLSLARKKNLAVVItNQVYT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 430769177 186 KVgvmfGNPETTP-GGRALKFY--ATIRLE----VRRAEQIKEGTNIIGNRVRIKVV 235
Cdd:TIGR02237 152 DV----NNGTLRPlGGHLLEHWskVILRLEkfrgRRLATLEKHRSRPEGESVYFRIT 204
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
25-220 |
7.62e-16 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 73.74 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 25 ISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAEnALDPVYAEHL-GVNIDDLL 103
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 104 ----LSQP-DTGEQGLEIADA-LVSSGAVDILVVDSVAALVpRAEIEGEM--GDAHVGLQARLmsQALRKLSgtlnKTKT 175
Cdd:PRK09361 80 sniiIFEPsSFEEQSEAIRKAeKLAKENVGLIVLDSATSLY-RLELEDEEdnSKLNRELGRQL--THLLKLA----RKHD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 430769177 176 IA-LFINQIREKVgvmfGNPETTP-GGRALKFY--ATIRLE-----VRRAEQIK 220
Cdd:PRK09361 153 LAvVITNQVYSDI----DSDGLRPlGGHTLEHWskTILRLEkfrngKRRATLEK 202
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
22-218 |
1.21e-15 |
|
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: 73.88 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 22 QTTISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKT----TVALHAVAEVQKQG--GTAAYIDAENALDPV----Y 91
Cdd:pfam08423 13 RSELIQITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFRPErlvaI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 92 AEHLGVNIDDLLLSQP-------DTGEQGLEIADALVSSGAVDILVVDSVAALVpRAEIE--GEMGDAHVGLqARLMSqA 162
Cdd:pfam08423 92 AERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-T 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 430769177 163 LRKLSGTLNktktIALFI-NQIREKVG---VMF-GNPETTPGGRALKFYATIRLEVR--RAEQ 218
Cdd:pfam08423 169 LQRLADEFG----VAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRkgRGEQ 227
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
28-218 |
6.54e-14 |
|
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: 68.54 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVAlHAVAeVQKQ--------GGTAAYIDAENALDP----VYAEHL 95
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLC-VTAQlpgsmgggGGKVAYIDTEGTFRPdrirPIAERF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 96 GVN----IDDLLLSQPDTGEQGLEIADALVSSGAVD----ILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLRK 165
Cdd:cd19514 78 GVDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 166 LSGTLNktktIALFI-NQIREKVG--VMF-GNPETTPGGRALKFYATIRLEVR--RAEQ 218
Cdd:cd19514 155 ISEEYN----VAVFItNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRkgRGEE 209
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
28-215 |
4.60e-13 |
|
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: 66.23 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQ------GGTAAYIDAENALDP----VYAEHLGV 97
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPpeegglNGKAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 98 NIDDLL-----LSQPDTGEQGL---EIADALVSSGAVDILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLRKLS 167
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHD-LHRLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 430769177 168 GTLNktktIALFI-NQIREKVGVMFGNPETTPGGRALKFYATIRLEVRR 215
Cdd:cd19515 157 DLYN----IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
21-218 |
1.47e-12 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 65.79 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 21 AQTTISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVAlHAVA-------EVQKQGGTAAYIDAENALDP---- 89
Cdd:PTZ00035 93 ARKNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLC-HTLCvtcqlpiEQGGGEGKVLYIDTEGTFRPeriv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 90 VYAEHLGVNIDDLL----LSQPDTGEQGLEI---ADALVSSGAVDILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMS 160
Cdd:PTZ00035 171 QIAERFGLDPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYsgRGELAERQQHL-GKFLR 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 430769177 161 qALRKLSGTLNktktIALFI-NQIREKVG---VMFGNPETTPGGRALKFYATIRLEVR--RAEQ 218
Cdd:PTZ00035 249 -ALQKLADEFN----VAVVItNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRkgRGEQ 307
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
28-218 |
1.69e-12 |
|
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: 64.65 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKT----TVALHAVAEVQKQG--GTAAYIDAENALDPV----YAEHLGV 97
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFRPErllaIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 98 NIDDLLLS-------QPDTGEQGLEIADALVSSGAVDILVVDSVAALVpRAEIEGEmGDahvgLQARLMS-----QALRK 165
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMHlakflRMLQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 166 LSGTLNktktIALFI-NQIREKV--GVMFGNPETTP-GGRALKFYATIRLEVR--RAEQ 218
Cdd:cd19513 154 LADEFG----VAVVItNQVVAQVdgAAMFAGDPKKPiGGNIMAHASTTRLYLRkgRGET 208
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
28-215 |
1.82e-12 |
|
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: 64.86 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVAlHAVA-------EVQKQGGTAAYIDAENALDPV----YAEHLG 96
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLAvtcqlpiDRGGGEGKAIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 97 VNIDDLLLS-------QPDTGEQGLEIADALVSSGAVDILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMSqALRKLS 167
Cdd:cd01123 79 LDPDDVLDNvayarafNSDHQTQLLDQAAAMMVESRFKLLIVDSATALY-RTDYsgRGELSARQMHL-AKFLR-MLQRLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 430769177 168 GTLNktktIALFI-NQIREKVG---VMFGNPETTPGGRALKFYATIRLEVRR 215
Cdd:cd01123 156 DEFG----VAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
28-218 |
2.01e-12 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 65.57 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVAlHAVA-----EVQKQGGTA--AYIDAENALDP----VYAEHLG 96
Cdd:PLN03187 108 ITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlPTEMGGGNGkvAYIDTEGTFRPdrivPIAERFG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 97 VN----IDDLLLSQPDTGEQgleIADALVSSGA------VDILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLR 164
Cdd:PLN03187 186 MDadavLDNIIYARAYTYEH---QYNLLLGLAAkmaeepFRLLIVDSVIALF-RVDFtgRGELAERQQKL-AQMLSR-LT 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 165 KLSGTLNktktIALFI-NQIREKVG--VMFGNPETTPGGRALKFYATIRLEVR--RAEQ 218
Cdd:PLN03187 260 KIAEEFN----VAVYMtNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRkgKGEQ 314
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
16-215 |
2.58e-12 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 65.14 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 16 RMGDAAQTTISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKT----TVALHAVAEVQKQGGT--AAYIDAENALDP 89
Cdd:PLN03186 93 SQLHAQRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGGEgkAMYIDTEGTFRP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 90 ----VYAEHLGVNIDDLL----LSQPDTGEQGLEI---ADALVSSGAVDILVVDSVAALVpRAEIEGEmGDahvgLQAR- 157
Cdd:PLN03186 172 qrliQIAERFGLNGADVLenvaYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSGR-GE----LSARq 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 430769177 158 -LMSQALRKLSgTLNKTKTIALFI-NQIREKV--GVMFGNPETTP-GGRALKFYATIRLEVRR 215
Cdd:PLN03186 246 mHLGKFLRSLQ-RLADEFGVAVVItNQVVAQVdgSAFFAGPQLKPiGGNIMAHASTTRLALRK 307
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
24-216 |
2.85e-12 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 64.90 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 24 TISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQ---KQGG---TAAYIDAENALDP----VYAE 93
Cdd:PRK04301 80 NVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeEKGGlegKAVYIDTEGTFRPerieQMAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 94 HLGVNIDDLL-----LSQPDTGEQGL--EIADALVSSG-AVDILVVDSVAALVpRAEiegemgdaHVGL------QARLM 159
Cdd:PRK04301 159 ALGLDPDEVLdnihvARAYNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLN 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 160 SQ--ALRKLSGTLNktkTIALFINQIREKVGVMFGNPETTPGGRALKFYATIRLEVRRA 216
Cdd:PRK04301 230 KHlhDLLRLADLYN---AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRKS 285
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
28-195 |
5.31e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 63.01 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPV--YAEHLGVNIDDLL-- 103
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 104 -----------LSQPDTGEQGLEIADALVSSGAvDILVVDSVAALvpRAEIEGEMgdahvglQARLMsqaLRKLSGTLNK 172
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREAVEEFGA-KRVVIDSLSGL--LLALPDPE-------RLREF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 430769177 173 TKTIALFINQIREKVGVMFGNPE 195
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
28-218 |
1.20e-11 |
|
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: 63.26 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVA--LHAVAEVQKQGGTA----AYIDAENALDP----VYAEHLGV 97
Cdd:TIGR02238 78 ITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLShtLCVTAQLPREMGGGngkvAYIDTEGTFRPdrirAIAERFGV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 98 N----IDDLLLSQPDTGEQGLEIAD---ALVSSGAVDILVVDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLRKLSG 168
Cdd:TIGR02238 157 DpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFsgRGELSERQQKL-AQMLSR-LNKISE 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 430769177 169 TLNktktIALFI-NQIREKVG--VMF-GNPETTPGGRALKFYATIRLEVR--RAEQ 218
Cdd:TIGR02238 234 EFN----VAVFVtNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRkgRGEE 285
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
36-215 |
7.91e-11 |
|
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: 60.03 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 36 DDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEV----QKQGGTAA--YIDAENAL------------DPVY------ 91
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampaRKGGLDGGvlYIDTESKFsaerlaeiaearFPEAfsgfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 92 -AEHLGVNIDDLLLSQPDTGEQGLEIADAL---VSSGAVDILVVDSVAALVpRAEIEGEMGDA---HVGLqARLMSqALR 164
Cdd:cd19493 80 eNERAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALV-RREFGGSDGEVterHNAL-AREAS-SLK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 430769177 165 KLSGTLNKTktiALFINQIREKVG-VMFGNPETTPG-GRALKFYATIRLEVRR 215
Cdd:cd19493 157 RLAEEFRIA---VLVTNQATTHFGdAGDGSSGVTAAlGDAWAHAVNTRLRLER 206
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
25-215 |
1.13e-10 |
|
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: 60.51 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 25 ISTISSGSLALDDALGvGGYPRGRIVEIYGPESSGKT----TVALHAVAEVQKQG--GTAAYIDAENALDPV----YAEH 94
Cdd:TIGR02239 75 VIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFRPErllaIAER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 95 LGVNIDDLLLS-------QPDTGEQGLEIADALVSSGAVDILVVDSVAALVpRAEIEGEmGDahvgLQARLMSQA--LRK 165
Cdd:TIGR02239 154 YGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArfLRS 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 430769177 166 LSgTLNKTKTIALFI-NQIREKV---GVMFGNPETTP-GGRALKFYATIRLEVRR 215
Cdd:TIGR02239 228 LQ-RLADEFGVAVVItNQVVAQVdgaGSMFAGDPKKPiGGNIMAHASTTRLSLRK 281
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
11-132 |
2.33e-10 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 58.79 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 11 KGAIMRMGDAAQTTISTISSGSLALDDALGVGGYPRGRIVEIYGPE-SSGKTTVALHAVAEVQKQGGTAAYIDAENALDP 89
Cdd:COG4544 12 RRRIWRGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 430769177 90 VYAEHLGVNIDDLLLSQPDTGEQGLEIADALVSSGAVDILVVD 132
Cdd:COG4544 92 PGLAAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-217 |
6.28e-10 |
|
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: 56.23 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 46 RGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPVYAEHLGVNIDDLLLSqpDTGEQGLEIADALVSSGA 125
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 126 VDILVVDSVAALVPRaeiegemgdahVGLQARLMSQALRKLSGTLNKTKTIALFINqirekvgvmfgNPETTPGGRALKF 205
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|..
gi 430769177 206 YATIRLEVRRAE 217
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
35-188 |
2.03e-07 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 50.37 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 35 LDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQ------KQGGTAAYIDAENAL----------------DPVYA 92
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 93 EHLGVNIDDLLLSQPDTGEQGL-EIADALVSSGAVDILVVDSVAALVpRAEIEGEMGDahVGLQARLMSQ---ALRKLSG 168
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSD--LVERAKYLRRladHLKRLAD 156
|
170 180
....*....|....*....|.
gi 430769177 169 TLNktktIA-LFINQIREKVG 188
Cdd:cd19491 157 KYN----LAvVVVNQVTDRFD 173
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
28-186 |
5.13e-07 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAE--------NALDPVYAEHLGVNI 99
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEesperllrNAKSFGWDFDEMEDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 100 DDLLLSQPDTGEQGLEIADALVS-------SGAVDILVVDSVAALvpRAEIEGEMgdahvglQARlmsQALRKLSGTLNK 172
Cdd:cd01124 80 GKLIIVDAPPTEAGRFSLDELLSrilsiikSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRA 147
|
170
....*....|....
gi 430769177 173 TKTIALFINQIREK 186
Cdd:cd01124 148 AGVTTIFTSEMRSF 161
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
35-226 |
7.26e-07 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 48.40 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 35 LDDALGvGGYPRGRIVEIYGPESSGKTTVALH-AVAEVQKQGGTAAYIDAENalDPV----YAEHLGVNIDDLL------ 103
Cdd:pfam06745 8 LDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLEE--PPEdlreNARSFGWDLEKLEeegkla 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 104 ---LSQPDTGEQGLEIADAL----------VSSGAVDILVVDSVAALvprAEIEGEMgdahvglQARlmsQALRKLSGTL 170
Cdd:pfam06745 85 iidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRRLKRVL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 171 NKTKTIALFINQIREKvgvmfgnpETTPGGRALKFYA---TIRLEVRRAEQIKEGTNII 226
Cdd:pfam06745 152 KGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIvdgVIRLDLKEIEEERVRTIEI 202
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
28-180 |
9.41e-06 |
|
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: 45.60 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPV--YAEHLGVNIDDLLLs 105
Cdd:cd01121 64 ISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSDNLYL- 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430769177 106 qpdTGEQGLEIADALVSSGAVDILVVDSVAALVpRAEIEGEMGDAhvgLQARLMSQALRKLSgtlnKTKTIALFI 180
Cdd:cd01121 142 ---LAETNLEAILAEIEELKPSLVVIDSIQTVY-SPELTSSPGSV---SQVRECAAELLRLA----KETGIPVFL 205
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
28-100 |
1.45e-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: 44.65 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYI---DAENALDPVYAEHlGVNID 100
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAVALSH-GWSLD 74
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
47-215 |
1.99e-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: 44.26 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 47 GRIVEIYGPESSGKTTVALHAVA---------EVQKQGGTAA--YIDAENALDPV----YAEHLGVNIDDLLLSQPDTGE 111
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDILrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 112 QGLEIADAL----------------------------VSSGAVDILVVDSVAALVPRAEIEGEMGDAHVGLQARLM---S 160
Cdd:cd19490 81 VEEIARECLqrlhifrchsslqllatllslenyllslSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430769177 161 QALRKLSGTLNK----TKTialFINQIREKVGVMFGNPETTPGGRALKF----------YATIRLEVRR 215
Cdd:cd19490 161 RELRRLRRRFQLvviaTKQ---ALFPGKSASTDNPAANNAVSKASAPSHreylprpwqrLVTHRLVLSR 226
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
28-135 |
6.05e-05 |
|
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: 42.67 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPVY--AEHLGVNIDDLLls 105
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFerSEALGIDLRAMV-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 430769177 106 qpDTGEQGLEIADAL--------------VSSGAVDILVVDSVA 135
Cdd:cd19487 78 --EKGLLSIEQIDPAelspgefaqrvrtsVEQEDARVVVIDSLN 119
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
50-204 |
2.41e-04 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 39.79 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 50 VEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDaenALDPVyaehlgvniddlllsqpdtgeqgLEIADALVSSGAVDIL 129
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFIS---FLDTI-----------------------LEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430769177 130 VVDSVAALVPRAEiegemgdahvGLQARLMSQALRKLSGTLNKTKTIALFINQIREKVGVMFGNPETTPGGRALK 204
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
28-100 |
4.21e-04 |
|
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: 40.39 E-value: 4.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 430769177 28 ISSGSLALDDALGVGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAENALDPVYAEHLGVNID 100
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIRNAKSIGID 73
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
45-242 |
4.45e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 40.65 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 45 PRGRIVEIYGPESSGKTTVALHAVAEV---------QKQGGTAAYIDAENALDPV------YAEHLGVNIDDLL------ 103
Cdd:COG3598 11 PEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEDDRGELrrrlkaLGADLGLPFADLDgrlrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 104 -LSQPDTGEQGLEIADALVSSGAVDILVVDSVAALVPraeiegemGDAHVGLQARLMSQALRKLSGTLNKTktiALFINQ 182
Cdd:COG3598 91 sLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLAERTGAA---VLLVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 183 IReKVGVMFGNPETTPGGRALKFYATIRLEVRRAEQikegtniiGNRVRIKVVKNKVAPP 242
Cdd:COG3598 160 TG-KGGAGKDSGDRARGSSALRGAARSVLVLSREKG--------EDLRVLTRAKSNYGPE 210
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
28-84 |
5.78e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.63 E-value: 5.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 430769177 28 ISSGSLALDDALGvGGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGGTAAYIDAE 84
Cdd:PRK09302 255 ISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFE 310
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
42-87 |
1.11e-03 |
|
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: 39.16 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 430769177 42 GGYPRGRIVEIYGPESSGKTTVALHAVAEVQKQGG-TAAYIDAENAL 87
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGqNVLYIDTKSSF 48
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
46-134 |
9.29e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 36.15 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430769177 46 RGRIVEIYGPESSGKTTVALHAvaevqkqgGTAAYIDAENALDPVYAEHLGVniDDLLLSQPDTGEQGLEIADALVSSga 125
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPD--IVIRDSWQDFLDAIDELTAAELAD-- 68
|
....*....
gi 430769177 126 VDILVVDSV 134
Cdd:pfam13479 69 YKTIVIDTV 77
|
|
|