|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-254 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 555.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 1 AVEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQ 80
Cdd:PRK09354 34 AAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 81 DLLISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFI 160
Cdd:PRK09354 114 NLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 161 NQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQG 240
Cdd:PRK09354 194 NQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDIMYGEGISREG 273
|
250
....*....|....
gi 347800072 241 EIIDLGVQAKLVDK 254
Cdd:PRK09354 274 ELIDLGVELGIIEK 287
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-254 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 540.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 1 AVEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQ 80
Cdd:COG0468 37 ARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 81 DLLISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFI 160
Cdd:COG0468 117 NLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 161 NQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQG 240
Cdd:COG0468 197 NQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEG 276
|
250
....*....|....
gi 347800072 241 EIIDLGVQAKLVDK 254
Cdd:COG0468 277 ELLDLAVELGIIEK 290
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-254 |
1.62e-177 |
|
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: 490.73 E-value: 1.62e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 1 AVEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQ 80
Cdd:TIGR02012 29 TVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDID 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 81 DLLISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFI 160
Cdd:TIGR02012 109 NLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 161 NQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQG 240
Cdd:TIGR02012 189 NQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFDILYGEGISKLG 268
|
250
....*....|....
gi 347800072 241 EIIDLGVQAKLVDK 254
Cdd:TIGR02012 269 EIIDLAVELDIIKK 282
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-237 |
3.81e-171 |
|
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: 472.27 E-value: 3.81e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 1 AVEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQ 80
Cdd:pfam00154 26 KKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDID 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 81 DLLISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFI 160
Cdd:pfam00154 106 NLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347800072 161 NQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGIS 237
Cdd:pfam00154 186 NQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
4-238 |
4.58e-169 |
|
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: 465.88 E-value: 4.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 4 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQDLL 83
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 84 ISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 163
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347800072 164 RMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISR 238
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-218 |
3.47e-105 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 322.04 E-value: 3.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 1 AVEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQ 80
Cdd:PRK09519 34 ARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 81 DLLISQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFI 160
Cdd:PRK09519 114 SLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFI 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 347800072 161 NQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNK 218
Cdd:PRK09519 194 NQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
27-195 |
1.72e-52 |
|
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: 168.69 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 27 GRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQD-----------LLISQPDTGEQALE 95
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSselelaealsrLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 96 IADALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 171
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 347800072 172 G-NPETTTGGNALKFYSSVRLDIRR 195
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
8-248 |
8.11e-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: 8.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVN----AQDLL 83
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERfesiASNII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 84 ISQP-DTGEQALEIADA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIFI 160
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 161 NQIRMKIGVMFGNPettTGGNALKFYSSVRLDIRRIGSikkndevignETRVKVVKNKVSPPfreaifdilygEGISRQG 240
Cdd:cd01394 153 NQVYSDIDDDRLKP---VGGTLLEHWSKAIIRLEKSPP----------GLRRATLEKHRSRP-----------EGQSAGF 208
|
....*...
gi 347800072 241 EIIDLGVQ 248
Cdd:cd01394 209 RITDRGIR 216
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
8-236 |
2.31e-16 |
|
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: 76.19 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIA----EMQKLGGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCqlplEMGGGEGKALYIDTEGTFRperlVAIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQDLLISQP-------DTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 148
Cdd:pfam08423 98 DPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 149 TIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRV-KVVKnkvSP-- 221
Cdd:pfam08423 172 LADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLR-----KGRG-----EQRIcKIYD---SPcl 238
|
250
....*....|....*
gi 347800072 222 PFREAIFDIlYGEGI 236
Cdd:pfam08423 239 PESEAVFAI-GSGGI 252
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
3-236 |
2.10e-14 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 71.45 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 3 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQK------LGGTAAFIDAE------------ 64
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEgtfrperieqma 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 65 --------HALD-VQYAQKLGVNAQDLLIsqpdtgEQALEIADalvRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQ 135
Cdd:PRK04301 158 ealgldpdEVLDnIHVARAYNSDHQMLLA------EKAEELIK---EGENIKLVIVDSLTAHF-RAEYVGR--GNLAERQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 136 ARLMSQ--ALRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVK 213
Cdd:PRK04301 226 QKLNKHlhDLLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK----SKGNKRI-----AR 293
|
250 260
....*....|....*....|....*
gi 347800072 214 VVKnkvSP--PFREAIFDILyGEGI 236
Cdd:PRK04301 294 LVD---SPhlPEGEAVFRIT-EEGI 314
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
8-175 |
2.46e-14 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 69.94 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALD--VQYAQKLGVNAQDLL-- 83
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 84 -------ISQPDTGEQALEIADAL---VRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKRT 153
Cdd:COG0467 81 gllriidLSPEELGLDLEELLARLreaVEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 347800072 154 NCLVIFINQIRMKIGVMFGNPE 175
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
5-197 |
3.59e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 69.51 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 5 IQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEhALDVQ-YAQKLGVN----A 79
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPErFKQIAGEDfeelL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 80 QDLLISQP-DTGEQALEIADA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRTNCL 156
Cdd:PRK09361 80 SNIIIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 347800072 157 VIFINQIRMKIGvmfGNPETTTGGNALKFYSS--VRLDIRRIG 197
Cdd:PRK09361 155 VVITNQVYSDID---SDGLRPLGGHTLEHWSKtiLRLEKFRNG 194
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
8-230 |
1.57e-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: 67.77 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQK------LGGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQDLL-----ISQPDTGEQAL---EIADALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 149
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 150 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP--PFREAI 227
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK----GKGGKRI-----ARLVD---SPhlPEGEAV 223
|
...
gi 347800072 228 FDI 230
Cdd:cd19515 224 FRI 226
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
16-198 |
1.16e-12 |
|
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: 65.03 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 16 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVIAEMQKLGGTAA--FIDAEHALDVQ-------------YAQKLG 76
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 77 VN------AQDLLISQPDTGEQALEIADAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 147
Cdd:cd19493 80 ENeraeemLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 347800072 148 GTIKRT----NCLVIFINQIRMKIGVMFGNPETTTG--GNALKFYSSVRLDIRRIGS 198
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
7-112 |
2.52e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 64.57 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 7 VVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVIAEMQKLGGTAAFIDAEHALdvqYA---QKLGVNAQDL 82
Cdd:COG4544 28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
|
90 100 110
....*....|....*....|....*....|
gi 347800072 83 LISQPDTGEQALEIADALVRSGSIDMIVID 112
Cdd:COG4544 105 LLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
15-195 |
2.68e-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: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 15 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQDLL----ISQP--- 87
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTEGLSPERFKQIAEDRPERALsnfiVFEVfdf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 88 DTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMKI 167
Cdd:TIGR02237 80 DEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTDV 153
|
170 180
....*....|....*....|....*...
gi 347800072 168 GVMFGNPettTGGNALKFYSSVRLDIRR 195
Cdd:TIGR02237 154 NNGTLRP---LGGHLLEHWSKVILRLEK 178
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
8-236 |
1.03e-11 |
|
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: 62.72 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVIAEMQKLGGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchtlavTCQLPIDQGGGEGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQDLLIS-------QPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 148
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 149 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGNALKFYSSVRLDIRRigsikkndeviGN-ETRVKVVKNKVSPPFR 224
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK-----------GRgETRICKIYDSPCLPEA 222
|
250
....*....|..
gi 347800072 225 EAIFDIlYGEGI 236
Cdd:cd19513 223 EAVFAI-TEDGI 233
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
8-236 |
2.01e-11 |
|
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: 61.78 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVIAEMQKLGGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchtlavTCQLPIDRGGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQDLLIS-------QPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 148
Cdd:cd01123 80 DPDDVLDNvayarafNSDHQTQLLDQAAAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 149 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFRE 225
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK-GR---------GETRICKIYDSPCLPEAE 223
|
250
....*....|.
gi 347800072 226 AIFDIlYGEGI 236
Cdd:cd01123 224 AVFAI-TADGV 233
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
4-237 |
4.08e-11 |
|
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: 62.05 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 4 DIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVIAEMQKLGGTAAFIDAEHALD----VQYAQ 73
Cdd:TIGR02239 74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchtlavTCQLPIDQGGGEGKALYIDTEGTFRperlLAIAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 74 KLGVNAQDLLIS-------QPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA--LR 144
Cdd:TIGR02239 153 RYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArfLR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 145 KLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVS 220
Cdd:TIGR02239 227 SLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK-GR---------GEQRICKIYDSPC 296
|
250
....*....|....*..
gi 347800072 221 PPFREAIFDIlYGEGIS 237
Cdd:TIGR02239 297 LPESEAMFAI-YEDGIG 312
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
8-230 |
4.50e-11 |
|
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: 60.83 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEMQKL----GGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQ----DLLISQPDTGEQALEIADAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 147
Cdd:cd19514 80 DHDavldNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 148 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFR 224
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK-GR---------GEERIAKIYDSPDLPEN 223
|
....*.
gi 347800072 225 EAIFDI 230
Cdd:cd19514 224 EATFAI 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-196 |
7.65e-11 |
|
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: 58.92 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 26 RGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDVQYAQKLGVNAQDLLISqpDTGEQALEIADALVRSGS 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 106 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINqirmkigvmfgNPETTTGGNALKF 185
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 347800072 186 YSSVRLDIRRI 196
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
3-230 |
1.34e-10 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 60.52 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 3 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEM--QKLGGT--AAFIDAEHALD----VQYA 72
Cdd:PLN03186 100 QEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 73 QKLGVNAQDLL----ISQPDTGEQALEIadaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--LMS 140
Cdd:PLN03186 179 ERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmHLG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 141 QALRKLTGTIKRTNCLVIFINQIRMKI--GVMFGNPETT-TGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKN 217
Cdd:PLN03186 250 KFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGENRI-----CKVISS 320
|
250
....*....|...
gi 347800072 218 KVSPPfREAIFDI 230
Cdd:PLN03186 321 PCLPE-AEARFSI 332
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
8-198 |
1.78e-10 |
|
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: 59.18 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-MQKLGGTAAFIDA-EHALDV-QYAQKLGVNAQDLL- 83
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 84 --------ISQPDTGEQALEIADAL----------VRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALRK 145
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 347800072 146 LTGTIKRTNCLVIFINQIRMKigvmfgnpETTTGGNALKFYSS---VRLDIRRIGS 198
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
15-163 |
2.74e-10 |
|
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: 58.84 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 15 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQ------KLGGTAAFIDAEHALD----VQYAQKLGVNAQDLLI 84
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFPskrlQQLASSLPKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 85 SQP------------DTGEQAL-EIADALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 151
Cdd:cd19491 80 KNFldnifvehvadlETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 347800072 152 RTNCLVIFINQI 163
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
4-195 |
6.24e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 58.64 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 4 DIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVIAEMQKLGGTAAFIDAEHALD----VQYAQ 73
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahtlcvTTQLPTEMGGGNGKVAYIDTEGTFRpdriVPIAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 74 KLGVNAQ----DLLISQPDTGEQ---ALEIADALVRSGSIDMIVIDSVAALVPKAEI-EGEMGDSlpglQARLmSQALRK 145
Cdd:PLN03187 183 RFGMDADavldNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSR 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 347800072 146 LTGTIKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNALKFYSSVRLDIRR 195
Cdd:PLN03187 258 LTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
8-244 |
2.57e-09 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 56.54 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVIAEMQKLGGTAAFIDAEHALD----VQYAQKLGV 77
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchtlcvTCQLPIEQGGGEGKVLYIDTEGTFRperiVQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 78 NAQDLL----ISQPDTGEQALEI---ADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 148
Cdd:PTZ00035 179 DPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlGKFLRALQK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 149 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRVKVVKNKVSPPFRE 225
Cdd:PTZ00035 253 LADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGRG-----EQRICKIYDSPNLPESE 322
|
250
....*....|....*....
gi 347800072 226 AIFdilygeGISRQGeIID 244
Cdd:PTZ00035 323 AVF------AISEGG-IID 334
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
3-160 |
4.38e-09 |
|
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: 55.62 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 3 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDvQY---AQKLGVNA 79
Cdd:cd01121 59 EEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 80 QDLLIsqpdTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCLV 157
Cdd:cd01121 137 DNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIPV 203
|
...
gi 347800072 158 IFI 160
Cdd:cd01121 204 FLV 206
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
186-254 |
4.60e-09 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 56.64 E-value: 4.60e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347800072 186 YSSVR--LDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKLVDK 254
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRK 727
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
27-168 |
4.74e-09 |
|
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: 55.05 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 27 GRVVEIYGPESSGKTTLTLQVIA-----------EMQKLGGTAAFIDAEHALDV----QYAQKLGVNAQDLLISQPDTGE 91
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDIlrlrSILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 92 QALEIADALVR----------------------------SGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 140
Cdd:cd19490 81 VEEIARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 347800072 141 QALRKLTgtiKRTNCLVIFINQIRMKIG 168
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
8-164 |
1.00e-08 |
|
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: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALD--VQYAQKLGVN------A 79
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDfdemedE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 80 QDLLISQPDTGEQALEIADAL-------VRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 152
Cdd:cd01124 80 GKLIIVDAPPTEAGRFSLDELlsrilsiIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 347800072 153 TNCLVIFINQIR 164
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
24-160 |
4.52e-08 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 52.98 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 24 LPRGRVVEIYGPESSGKTTLTLQVIAEMQK----LG-----GTAAFIDAE----------HALDVQYAQKLGVNAQDLLI 84
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEddrgelrrrlKALGADLGLPFADLDGRLRL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347800072 85 SQPDTGEQALEIADAL---VRSGSIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVIFI 160
Cdd:COG3598 90 LSLAGDLDDTDDLEALeraIEEEGPDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVLLV 157
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
7-230 |
5.98e-08 |
|
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: 52.47 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 7 VVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIA----EMQKLGGTAAFIDAEHALD----VQYAQKLG 76
Cdd:TIGR02238 77 KITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAqlprEMGGGNGKVAYIDTEGTFRpdriRAIAERFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 77 VNA----QDLLISQPDTGEQALEIAD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 149
Cdd:TIGR02238 156 VDPdavlDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLNKI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 150 IKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFREA 226
Cdd:TIGR02238 232 SEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK-GR---------GEERVAKLYDSPDMPEAEA 301
|
....
gi 347800072 227 IFDI 230
Cdd:TIGR02238 302 SFQI 305
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
27-168 |
1.93e-07 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 49.53 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 27 GRVVEIYGPESSGKTTLTLQVIAEMQ------KLGGTAAFIDAE-----HALDV-QYAQKLGV--NAQDLLISQPDtgeq 92
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347800072 93 aleiadalvrsgsIDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 168
Cdd:cd19492 77 -------------VKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
8-61 |
3.99e-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: 46.57 E-value: 3.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFI 61
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
30-184 |
1.23e-05 |
|
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: 43.65 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 30 VEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDaehALDVqyaqklgvnaqdllisqpdtgeqALEIADALVRSGSIDMI 109
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFIS---FLDT-----------------------ILEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347800072 110 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 184
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
22-118 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 22 GGLPRGRVVEIYGPESSGKTTLTLQVIAEM-QKLGGTAAFID------AEHALD-VQYAQKLGVNAQDLL-------ISQ 86
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQiLKSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 347800072 87 PDTGEQALEIADALVR------SGSIDMIVIDSVAALV 118
Cdd:cd19489 82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
26-114 |
1.83e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.46 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 26 RGRVVEIYGPESSGKTTLTLQViaemqklgGTAAFIDAEHALDVQYAQKLGVnaQDLLISQPDTGEQALEIADALVRsgS 105
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPD--IVIRDSWQDFLDAIDELTAAELA--D 68
|
....*....
gi 347800072 106 IDMIVIDSV 114
Cdd:pfam13479 69 YKTIVIDTV 77
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
32-118 |
5.07e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 37.30 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 32 IYGPESSGKTTLTLQVIAEMQKLGGTAAFIDA-----EHALDVQYAQKLGVNAQDLLISQPDTGEQAL------EIADAL 100
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRRLAEALGIAVPKAELEESKLaflaieLLLEAL 104
|
90
....*....|....*...
gi 347800072 101 VRSGSIDMIVIDSVAALV 118
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
8-115 |
5.56e-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: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800072 8 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAEMQKLGGTAAFIDAEHALDV--QYAQKLGVNAQDLLis 85
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTlfERSEALGIDLRAMV-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 347800072 86 qpDTGEQALEIADAL--------------VRSGSIDMIVIDSVA 115
Cdd:cd19487 78 --EKGLLSIEQIDPAelspgefaqrvrtsVEQEDARVVVIDSLN 119
|
|
| |
