|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-333 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 682.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09354 10 ALEAALKQIEKQFGKGSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09354 89 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 161 ARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVV 240
Cdd:PRK09354 169 ARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 241 KNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESL 320
Cdd:PRK09354 249 KNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKKIREKL 328
|
330
....*....|...
gi 25991705 321 GVVAMPDGVVDEA 333
Cdd:PRK09354 329 GLSAAAAEEEEEE 341
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-333 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 662.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:COG0468 13 ALEAALSQIEKQFGKGSIMRLGD-KARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:COG0468 92 GIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 161 ARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVV 240
Cdd:COG0468 172 ARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 241 KNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESL 320
Cdd:COG0468 252 KNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKIREKL 331
|
330
....*....|...
gi 25991705 321 GVVAMPDGVVDEA 333
Cdd:COG0468 332 GLGAVSEAAAAEE 344
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-318 |
0e+00 |
|
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: 595.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:TIGR02012 5 ALEAALAQIEKQFGKGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:TIGR02012 84 GTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 161 ARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVV 240
Cdd:TIGR02012 164 ARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVV 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25991705 241 KNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRE 318
Cdd:TIGR02012 244 KNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVRE 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-262 |
0e+00 |
|
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: 512.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 1 ALAAALAQIEKQFGKGSIMRMGDGDvKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:pfam00154 2 ALEAALKQIEKQFGKGSIMKLGDEK-KLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:pfam00154 81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 161 ARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVV 240
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVV 240
|
250 260
....*....|....*....|..
gi 25991705 241 KNKVSPPFREAIFDILYGEGIS 262
Cdd:pfam00154 241 KNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
29-263 |
1.41e-167 |
|
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: 465.49 E-value: 1.41e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 29 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL 108
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 188
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25991705 189 RMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISR 263
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-243 |
1.94e-114 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 349.39 E-value: 1.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 1 ALAAALAQIEKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLG 80
Cdd:PRK09519 10 ALELAVAQIEKSYGKGSVMRLGD-EARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 81 GTAAFIDAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQ 160
Cdd:PRK09519 89 GVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 161 ARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVV 240
Cdd:PRK09519 169 ARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVV 248
|
...
gi 25991705 241 KNK 243
Cdd:PRK09519 249 KNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
52-220 |
2.75e-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: 170.61 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 52 GRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPE-----------LLISQPDTGEQALE 120
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSselelaealsrLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 121 ITDALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 196
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 25991705 197 G-NPETTTGGNALKFYSSVRLDIRR 220
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
211-325 |
1.07e-28 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 116.73 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 211 YSSVR--LDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNG 288
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110
....*....|....*....|....*....|....*..
gi 25991705 289 EKIGQGKDNAREFLRENPEIAREIENRIRESLGVVAM 325
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAV 773
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
33-273 |
5.12e-19 |
|
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: 83.90 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL---- 108
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERFESIAsnii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 ISQP-DTGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIFI 185
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 186 NQIRMKIGVMFGNPettTGGNALKFYSSVRLDIRRIGSikkndevignETRVKVVKNKVSPPfreaifdilygEGISRQG 265
Cdd:cd01394 153 NQVYSDIDDDRLKP---VGGTLLEHWSKAIIRLEKSPP----------GLRRATLEKHRSRP-----------EGQSAGF 208
|
....*...
gi 25991705 266 EIIDLGVQ 273
Cdd:cd01394 209 RITDRGIR 216
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
33-200 |
2.98e-14 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 70.71 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPELL-- 108
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 -----------ISQPDTGEQALEITDAlVRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKR 177
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREA-VEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 25991705 178 TNCLVIFINQIRMKIGVMFGNPE 200
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
27-261 |
4.77e-14 |
|
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: 70.79 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 27 KEDIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQK-LGGT---AAFIDAEHALD----VQY 96
Cdd:pfam08423 14 SELIQI-TTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRperlVAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 97 AAKLGVNVPELLISQP-------DTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQA 167
Cdd:pfam08423 92 AERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 168 LRKLTGTIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRV-KVVKn 242
Cdd:pfam08423 166 LRTLQRLADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLR-----KGRG-----EQRIcKIYD- 234
|
250 260
....*....|....*....|.
gi 25991705 243 kvSP--PFREAIFDIlYGEGI 261
Cdd:pfam08423 235 --SPclPESEAVFAI-GSGGI 252
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
30-222 |
3.77e-13 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 67.58 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 30 IQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKL-GVNVPELL 108
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 ----ISQP-DTGEQALEITDA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRTNCL 181
Cdd:PRK09361 80 sniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25991705 182 VIFINQIRMKIGvmfGNPETTTGGNALKFYSS--VRLDIRRIG 222
Cdd:PRK09361 155 VVITNQVYSDID---SDGLRPLGGHTLEHWSKtiLRLEKFRNG 194
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
27-261 |
6.42e-13 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 68.37 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAEHALD----VQY 96
Cdd:PRK04301 78 RKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRperiEQM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 97 AAKLGVNVPELL-----ISQPDTGEQALEITDA--LVRSG-SIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLMSQ-- 166
Cdd:PRK04301 157 AEALGLDPDEVLdnihvARAYNSDHQMLLAEKAeeLIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQQKLNKHlh 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 167 ALRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP 246
Cdd:PRK04301 234 DLLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK----SKGNKRI-----ARLVD---SP 298
|
250
....*....|....*..
gi 25991705 247 --PFREAIFDILyGEGI 261
Cdd:PRK04301 299 hlPEGEAVFRIT-EEGI 314
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
33-255 |
1.04e-12 |
|
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: 66.62 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 103 NVPELL-----ISQPDTGEQAL---EITDALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 174
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 175 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP--PFREAI 252
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK----GKGGKRI-----ARLVD---SPhlPEGEAV 223
|
...
gi 25991705 253 FDI 255
Cdd:cd19515 224 FRI 226
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
40-220 |
1.06e-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: 66.29 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 40 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKLGVNVPELLISQ------PD 113
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 114 TGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMK 191
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180
....*....|....*....|....*....
gi 25991705 192 IGVMFGNPettTGGNALKFYSSVRLDIRR 220
Cdd:TIGR02237 153 VNNGTLRP---LGGHLLEHWSKVILRLEK 178
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
41-223 |
9.68e-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: 63.49 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 41 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVIAELQKLGGTAA--FIDAEHALDVQ-------------YAAKLG 101
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 102 VNVPELLISQ------PDTGEQALEITDAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 172
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25991705 173 GTIKRT----NCLVIFINQIRMKIGVMFGNPETTTG--GNALKFYSSVRLDIRRIGS 223
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
22-137 |
2.75e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 62.25 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 22 GDGDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVIAELQKLGGTAAFIDAEHALdvqYA--- 97
Cdd:COG4544 18 GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApgl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 25991705 98 AKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVID 137
Cdd:COG4544 95 AAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
51-221 |
4.94e-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: 60.08 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 51 RGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELLISqpDTGEQALEITDALVRSGS 130
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 131 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINqirmkigvmfgNPETTTGGNALKF 210
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 25991705 211 YSSVRLDIRRI 221
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
33-223 |
1.49e-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: 60.34 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-LQKLGGTAAFIDA-EHALDV-QYAAKLGVNVPELL- 108
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 --------ISQPDTGEQALEITDAL----------VRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALRK 170
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25991705 171 LTGTIKRTNCLVIFINQIRMKigvmfgnpETTTGGNALKFYSS---VRLDIRRIGS 223
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
40-188 |
3.18e-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: 59.61 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 40 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIA------ELQKLGGTAAFIDAEHALDVQ----------------YA 97
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALtvqlprELGGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 98 AKLGVNVPELLISQPDTGEQALEITD-ALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 176
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 25991705 177 RTNCLVIFINQI 188
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
33-255 |
1.09e-09 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 57.75 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKL----GGTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 103 N----VPELLISQPDTGEQALEITDAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 172
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 173 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFR 249
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK-GR---------GEERIAKIYDSPDLPEN 223
|
....*.
gi 25991705 250 EAIFDI 255
Cdd:cd19514 224 EATFAI 229
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
33-261 |
1.23e-09 |
|
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: 57.54 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQ----KLGGTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQLPidrgGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 103 NVPELL----ISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 173
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 174 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFRE 250
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK-GR---------GETRICKIYDSPCLPEAE 223
|
250
....*....|.
gi 25991705 251 AIFDIlYGEGI 261
Cdd:cd01123 224 AVFAI-TADGV 233
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
33-189 |
1.28e-09 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 57.27 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPEL--- 107
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 108 ----LISQPDTGEQALEITD------ALVRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 177
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 25991705 178 TNCLVIFINQIR 189
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
26-255 |
5.00e-09 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 56.66 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 26 VKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL--QKLGGT--AAFIDAEHALD----VQ 95
Cdd:PLN03186 98 QRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 96 YAAKLGVNVPELL----ISQPDTGEQALEItdaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--L 163
Cdd:PLN03186 177 IAERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmH 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 164 MSQALRKLTGTIKRTNCLVIFINQIRMKI--GVMFGNPETT-TGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVV 240
Cdd:PLN03186 248 LGKFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGENRI-----CKVI 318
|
250
....*....|....*
gi 25991705 241 KNKVSPPfREAIFDI 255
Cdd:PLN03186 319 SSPCLPE-AEARFSI 332
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
10-220 |
1.94e-08 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 55.17 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 10 EKQFGKGSIMRMGDGDVKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL-QKLGG---TA 83
Cdd:PLN03187 85 EKLLNQGFITGSDALLKRKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQLpTEMGGgngKV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 84 AFIDAEHALD----VQYAAKLGVN----VPELLISQPDTGEQ---ALEITDALVRSGSIDMIVIDSVAALVPKAEI-EGE 151
Cdd:PLN03187 164 AYIDTEGTFRpdriVPIAERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGE 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25991705 152 MGDSlpglQARLmSQALRKLTGTIKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNALKFYSSVRLDIRR 220
Cdd:PLN03187 244 LAER----QQKL-AQMLSRLTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
27-262 |
2.18e-08 |
|
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: 54.73 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQY 96
Cdd:TIGR02239 72 RQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 97 AAKLGVNVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA-- 167
Cdd:TIGR02239 151 AERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArf 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 168 LRKLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNK 243
Cdd:TIGR02239 225 LRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK-GR---------GEQRICKIYDS 294
|
250
....*....|....*....
gi 25991705 244 VSPPFREAIFDIlYGEGIS 262
Cdd:TIGR02239 295 PCLPESEAMFAI-YEDGIG 312
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
33-261 |
2.22e-08 |
|
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: 53.86 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQYAAKLGV 102
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 103 NVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 173
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 174 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGNALKFYSSVRLDIRRigsikkndeviGN-ETRVKVVKNKVSPPFR 249
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK-----------GRgETRICKIYDSPCLPEA 222
|
250
....*....|..
gi 25991705 250 EAIFDIlYGEGI 261
Cdd:cd19513 223 EAVFAI-TEDGI 233
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
52-193 |
4.36e-08 |
|
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: 53.12 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 52 GRVVEIYGPESSGKTTLTLQVIA-----------ELQKLGGTAAFIDAEHALDV------------QYAAKLGVNVPE-- 106
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDIlrlrsilearirAAIQAANSSDDEed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 107 -----------LLISQPDTGEQ------ALEIT-DALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 165
Cdd:cd19490 81 veeiareclqrLHIFRCHSSLQllatllSLENYlLSLSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 25991705 166 QALRKLTgtiKRTNCLVIFINQIRMKIG 193
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
28-185 |
2.38e-07 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 51.38 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 28 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDvQY---AAKLGVNV 104
Cdd:cd01121 59 EEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 105 PELLIsqpdTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCLV 182
Cdd:cd01121 137 DNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIPV 203
|
...
gi 25991705 183 IFI 185
Cdd:cd01121 204 FLV 206
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
25-255 |
2.97e-07 |
|
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: 51.32 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 25 DVKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKLGGTA----AFIDAEHALD----V 94
Cdd:TIGR02238 70 QKRKKVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGGGngkvAYIDTEGTFRpdriR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 95 QYAAKLGVN----VPELLISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQA 167
Cdd:TIGR02238 149 AIAERFGVDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQM 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 168 LRKLTGTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKV 244
Cdd:TIGR02238 225 LSRLNKISEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK-GR---------GEERVAKLYDSP 294
|
250
....*....|.
gi 25991705 245 SPPFREAIFDI 255
Cdd:TIGR02238 295 DMPEAEASFQI 305
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
52-193 |
3.28e-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: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 52 GRVVEIYGPESSGKTTLTLQVIAELQ------KLGGTAAFIDAE-----HALDV-QYAAKLGV--NVPELLISQPDtgeq 117
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25991705 118 aleitdalvrsgsIDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 193
Cdd:cd19492 77 -------------VKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
49-185 |
3.78e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 51.05 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 49 LPRGRVVEIYGPESSGKTTLTLQVIAELQK----LG-----GTAAFIDAE-HALDVQ-----YAAKLGVNVPEL-----L 108
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 IS-----QPDTGEQALEitdALVRSGSIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVI 183
Cdd:COG3598 90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVL 155
|
..
gi 25991705 184 FI 185
Cdd:COG3598 156 LV 157
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
33-269 |
1.15e-06 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 49.61 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQYAAKLGV 102
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQLpieQGGGeGKVLYIDTEGTFRperiVQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 103 NVPELL----ISQPDTGEQALEI---TDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 173
Cdd:PTZ00035 179 DPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlGKFLRALQK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 174 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRVKVVKNKVSPPFRE 250
Cdd:PTZ00035 253 LADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGRG-----EQRICKIYDSPNLPESE 322
|
250
....*....|....*....
gi 25991705 251 AIFdilygeGISRQGeIID 269
Cdd:PTZ00035 323 AVF------AISEGG-IID 334
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
55-209 |
6.63e-06 |
|
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: 44.80 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 55 VEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAehALDVQYAAKlgvnvpellisqpdtgeqaleitdALVRSGSIDMI 134
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF--LDTILEAIE------------------------DLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25991705 135 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 209
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
33-86 |
7.40e-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: 46.19 E-value: 7.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 25991705 33 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFI 86
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
51-185 |
3.34e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 41.16 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 51 RGRVVEIYGPESSGKTTLTLQViaelqklgGTAAFIDAEHALDVQYAAKLgvNVPELLISQPDTGEQALEITDALVRsgS 130
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25991705 131 IDMIVIDSVAALV-----------PKAEIEGEMGDSLP-GLQARLMSQALRKLTGTIKRtnclVIFI 185
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGKN----VIFT 131
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
57-143 |
8.70e-04 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 40.00 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 57 IYGPESSGKTTLTLQVIAELQKLGGTAAFIDA-----EHALDVQYAAK-----LGVNVPELLISQPDTGEQALE-ITDAL 125
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRrlaeaLGIAVPKAELEESKLAFLAIElLLEAL 104
|
90
....*....|....*...
gi 25991705 126 VRSGSIDMIVIDSVAALV 143
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
47-143 |
9.60e-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: 39.93 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 47 GGLPRGRVVEIYGPESSGKTTLTLQVIAEL-QKLGGTAAFID------AEHALD-VQYAAKLGVNVPELL-------ISQ 111
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQiLKSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 25991705 112 PDTGEQALEITDALVR------SGSIDMIVIDSVAALV 143
Cdd:cd19489 82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
27-149 |
1.17e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 39.96 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 27 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH------------ALDV 94
Cdd:PRK06067 1 EGKKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENtsksylkqmesvKIDI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 95 -QYAAKLGVNVPELLISQ----PDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIE 149
Cdd:PRK06067 80 sDFFLWGYLRIFPLNTEGfewnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
49-185 |
6.21e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 37.36 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 49 LPRGRVVEIYGPESSGKTTLTLQVIA-----------ELQKLGGTAAFIDAEHALDVQ----YAAKLGVNVPELL----- 108
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpwlggPRVPEQGKVLYVSAEGPADELrrrlRAAGADLDLPARLlflsl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 109 -----ISQPDTGEQAL-----EITDALVRSGSIDMIVIDSVAALVPkaeiegemGDSLPGLQARLMSQALRKLtgtIKRT 178
Cdd:pfam13481 110 veslpLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRL---ARRT 178
|
....*..
gi 25991705 179 NCLVIFI 185
Cdd:pfam13481 179 GATVLLV 185
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
43-183 |
7.96e-03 |
|
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410938 [Multi-domain] Cd Length: 161 Bit Score: 36.70 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25991705 43 ALGVGgLPRGrvVEIYGPESSGKTTLTLQVIAELQklggtAAFIDaehaldvqyaaklgVNVPELLISQPDTGEQALEIT 122
Cdd:cd19530 24 ALGID-LPTG--VLLYGPPGCGKTLLAKAVANESG-----ANFIS--------------VKGPELLNKYVGESERAVRQV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25991705 123 DALVRSGSIDMIVIDSVAALVPKaeiegeMGDSLPGLQARLMSQALRKLTGTIKRTNCLVI 183
Cdd:cd19530 82 FQRARASAPCVIFFDEVDALVPK------RGDGGSWASERVVNQLLTEMDGLEERSNVFVI 136
|
|
| |
