|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
5-318 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 664.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 5 KQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH 84
Cdd:PRK09354 20 KQFGKGSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 85 ALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRK 164
Cdd:PRK09354 99 ALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 165 LTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFRE 244
Cdd:PRK09354 179 LTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQ 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2000171745 245 AIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESLGVVA 318
Cdd:PRK09354 259 AEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKKIREKLGLSA 332
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
5-320 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 645.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 5 KQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH 84
Cdd:COG0468 23 KQFGKGSIMRLGD-KARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 85 ALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRK 164
Cdd:COG0468 102 ALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 165 LTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFRE 244
Cdd:COG0468 182 LTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2000171745 245 AIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESLGVVAMP 320
Cdd:COG0468 262 AEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKIREKLGLGAVS 337
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
5-312 |
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: 581.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 5 KQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH 84
Cdd:TIGR02012 15 KQFGKGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 85 ALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRK 164
Cdd:TIGR02012 94 ALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 165 LTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFRE 244
Cdd:TIGR02012 174 LTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFRE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2000171745 245 AIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRE 312
Cdd:TIGR02012 254 AEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVRE 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-256 |
3.62e-180 |
|
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: 498.08 E-value: 3.62e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 1 AESKKQFGKGSIMRMGDGDvKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFI 80
Cdd:pfam00154 8 KQIEKQFGKGSIMKLGDEK-KLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 81 DAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQ 160
Cdd:pfam00154 87 DAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 161 ALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSP 240
Cdd:pfam00154 167 ALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAP 246
|
250
....*....|....*.
gi 2000171745 241 PFREAIFDILYGEGIS 256
Cdd:pfam00154 247 PFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
23-257 |
4.30e-168 |
|
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: 466.26 E-value: 4.30e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 23 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL 102
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 182
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2000171745 183 RMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISR 257
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-237 |
9.66e-111 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 339.38 E-value: 9.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 1 AESKKQFGKGSIMRMGDgDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFI 80
Cdd:PRK09519 16 AQIEKSYGKGSVMRLGD-EARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 81 DAEHALDVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQ 160
Cdd:PRK09519 95 DAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2000171745 161 ALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNK 237
Cdd:PRK09519 175 ALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
46-214 |
8.13e-53 |
|
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: 171.77 E-value: 8.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 46 GRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPE-----------LLISQPDTGEQALE 114
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSselelaealsrLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 115 ITDALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 190
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 2000171745 191 G-NPETTTGGNALKFYSSVRLDIRR 214
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
205-319 |
8.19e-29 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 116.73 E-value: 8.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 205 YSSVR--LDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNG 282
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110
....*....|....*....|....*....|....*..
gi 2000171745 283 EKIGQGKDNAREFLRENPEIAREIENRIRESLGVVAM 319
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAV 773
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
27-267 |
4.40e-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: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL---- 102
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERFESIAsnii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 ISQP-DTGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIFI 179
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 180 NQIRMKIGVMFGNPettTGGNALKFYSSVRLDIRRIGSikkndevignETRVKVVKNKVSPPfreaifdilygEGISRQG 259
Cdd:cd01394 153 NQVYSDIDDDRLKP---VGGTLLEHWSKAIIRLEKSPP----------GLRRATLEKHRSRP-----------EGQSAGF 208
|
....*...
gi 2000171745 260 EIIDLGVQ 267
Cdd:cd01394 209 RITDRGIR 216
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
27-194 |
2.95e-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: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPELL-- 102
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 -----------ISQPDTGEQALEITDAlVRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKR 171
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREA-VEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 2000171745 172 TNCLVIFINQIRMKIGVMFGNPE 194
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
21-255 |
3.77e-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: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 21 KEDIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQK-LGGT---AAFIDAEHALD----VQY 90
Cdd:pfam08423 14 SELIQI-TTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRperlVAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 91 AAKLGVNVPELLISQP-------DTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQA 161
Cdd:pfam08423 92 AERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 162 LRKLTGTIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRV-KVVKn 236
Cdd:pfam08423 166 LRTLQRLADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLR-----KGRG-----EQRIcKIYD- 234
|
250 260
....*....|....*....|.
gi 2000171745 237 kvSP--PFREAIFDIlYGEGI 255
Cdd:pfam08423 235 --SPclPESEAVFAI-GSGGI 252
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
21-255 |
3.71e-13 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 68.75 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 21 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAEHALD----VQY 90
Cdd:PRK04301 78 RKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRperiEQM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 91 AAKLGVNVPELL-----ISQPDTGEQALEITDA--LVRSG-SIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLMSQ-- 160
Cdd:PRK04301 157 AEALGLDPDEVLdnihvARAYNSDHQMLLAEKAeeLIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQQKLNKHlh 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 161 ALRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP 240
Cdd:PRK04301 234 DLLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK----SKGNKRI-----ARLVD---SP 298
|
250
....*....|....*..
gi 2000171745 241 --PFREAIFDILyGEGI 255
Cdd:PRK04301 299 hlPEGEAVFRIT-EEGI 314
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
24-216 |
4.33e-13 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 67.58 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 24 IQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKL-GVNVPELL 102
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 ----ISQP-DTGEQALEITDA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRTNCL 175
Cdd:PRK09361 80 sniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2000171745 176 VIFINQIRMKIGvmfGNPETTTGGNALKFYSS--VRLDIRRIG 216
Cdd:PRK09361 155 VVITNQVYSDID---SDGLRPLGGHTLEHWSKtiLRLEKFRNG 194
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
27-249 |
7.23e-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: 67.00 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------LGGTAAFIDAEHALD----VQYAAKLGV 96
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 97 NVPELL-----ISQPDTGEQAL---EITDALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 168
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 169 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP--PFREAI 246
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK----GKGGKRI-----ARLVD---SPhlPEGEAV 223
|
...
gi 2000171745 247 FDI 249
Cdd:cd19515 224 FRI 226
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
34-214 |
1.02e-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: 65.90 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 34 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEhALDVQYAAKLGVNVPELLISQ------PD 107
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 108 TGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMK 185
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180
....*....|....*....|....*....
gi 2000171745 186 IGVMFGNPettTGGNALKFYSSVRLDIRR 214
Cdd:TIGR02237 153 VNNGTLRP---LGGHLLEHWSKVILRLEK 178
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
35-217 |
5.45e-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: 64.26 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 35 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVIAELQKLGGTAA--FIDAEHALDVQ-------------YAAKLG 95
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 96 VNVPELLISQ------PDTGEQALEITDAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 166
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2000171745 167 GTIKRT----NCLVIFINQIRMKIGVMFGNPETTTG--GNALKFYSSVRLDIRRIGS 217
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
16-131 |
1.01e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 63.41 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 16 GDGDVKEDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVIAELQKLGGTAAFIDAEHALdvqYA--- 91
Cdd:COG4544 18 GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApgl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2000171745 92 AKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVID 131
Cdd:COG4544 95 AAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-215 |
3.59e-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: 60.46 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 45 RGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELLISqpDTGEQALEITDALVRSGS 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 125 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINqirmkigvmfgNPETTTGGNALKF 204
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 2000171745 205 YSSVRLDIRRI 215
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
27-217 |
1.99e-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: 59.95 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-LQKLGGTAAFIDA-EHALDV-QYAAKLGVNVPELL- 102
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 --------ISQPDTGEQALEITDAL----------VRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALRK 164
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2000171745 165 LTGTIKRTNCLVIFINQIRMKigvmfgnpETTTGGNALKFYSS---VRLDIRRIGS 217
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
34-182 |
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 2000171745 34 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIA------ELQKLGGTAAFIDAEHALDVQ----------------YA 91
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALtvqlprELGGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 92 AKLGVNVPELLISQPDTGEQALEITD-ALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 170
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 2000171745 171 RTNCLVIFINQI 182
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
27-255 |
8.46e-10 |
|
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: 57.93 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQ----KLGGTAAFIDAEHALD----VQYAAKLGV 96
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQLPidrgGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 97 NVPELL----ISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 167
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 168 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFRE 244
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK-GR---------GETRICKIYDSPCLPEAE 223
|
250
....*....|.
gi 2000171745 245 AIFDIlYGEGI 255
Cdd:cd01123 224 AVFAI-TADGV 233
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
27-249 |
9.04e-10 |
|
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: 58.14 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKL----GGTAAFIDAEHALD----VQYAAKLGV 96
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 97 N----VPELLISQPDTGEQALEITDAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 166
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 167 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFR 243
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK-GR---------GEERIAKIYDSPDLPEN 223
|
....*.
gi 2000171745 244 EAIFDI 249
Cdd:cd19514 224 EATFAI 229
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
27-183 |
1.21e-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: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPEL--- 101
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 102 ----LISQPDTGEQALEITD------ALVRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 171
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 2000171745 172 TNCLVIFINQIR 183
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
20-249 |
3.14e-09 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 57.43 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 20 VKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL--QKLGGT--AAFIDAEHALD----VQ 89
Cdd:PLN03186 98 QRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 90 YAAKLGVNVPELL----ISQPDTGEQALEItdaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--L 157
Cdd:PLN03186 177 IAERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmH 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 158 MSQALRKLTGTIKRTNCLVIFINQIRMKI--GVMFGNPETT-TGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVV 234
Cdd:PLN03186 248 LGKFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGENRI-----CKVI 318
|
250
....*....|....*
gi 2000171745 235 KNKVSPPfREAIFDI 249
Cdd:PLN03186 319 SSPCLPE-AEARFSI 332
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
27-255 |
1.52e-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: 54.25 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQYAAKLGV 96
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 97 NVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 167
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 168 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGNALKFYSSVRLDIRRigsikkndeviGN-ETRVKVVKNKVSPPFR 243
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK-----------GRgETRICKIYDSPCLPEA 222
|
250
....*....|..
gi 2000171745 244 EAIFDIlYGEGI 255
Cdd:cd19513 223 EAVFAI-TEDGI 233
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
21-256 |
1.53e-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: 55.12 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 21 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQY 90
Cdd:TIGR02239 72 RQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 91 AAKLGVNVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA-- 161
Cdd:TIGR02239 151 AERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArf 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 162 LRKLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNK 237
Cdd:TIGR02239 225 LRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK-GR---------GEQRICKIYDS 294
|
250
....*....|....*....
gi 2000171745 238 VSPPFREAIFDIlYGEGIS 256
Cdd:TIGR02239 295 PCLPESEAMFAI-YEDGIG 312
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
21-214 |
1.81e-08 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 55.17 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 21 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL-QKLGG---TAAFIDAEHALD----VQY 90
Cdd:PLN03187 102 RKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQLpTEMGGgngKVAYIDTEGTFRpdriVPI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 91 AAKLGVN----VPELLISQPDTGEQ---ALEITDALVRSGSIDMIVIDSVAALVPKAEI-EGEMGDSlpglQARLmSQAL 162
Cdd:PLN03187 181 AERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQML 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2000171745 163 RKLTGTIKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNALKFYSSVRLDIRR 214
Cdd:PLN03187 256 SRLTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
46-187 |
4.07e-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: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 46 GRVVEIYGPESSGKTTLTLQVIA-----------ELQKLGGTAAFIDAEHALDV------------QYAAKLGVNVPE-- 100
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDIlrlrsilearirAAIQAANSSDDEed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 101 -----------LLISQPDTGEQ------ALEIT-DALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 159
Cdd:cd19490 81 veeiareclqrLHIFRCHSSLQllatllSLENYlLSLSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 2000171745 160 QALRKLTgtiKRTNCLVIFINQIRMKIG 187
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
43-179 |
1.62e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 51.83 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 43 LPRGRVVEIYGPESSGKTTLTLQVIAELQK----LG-----GTAAFIDAE-HALDVQ-----YAAKLGVNVPEL-----L 102
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 IS-----QPDTGEQALEitdALVRSGSIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVI 177
Cdd:COG3598 90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVL 155
|
..
gi 2000171745 178 FI 179
Cdd:COG3598 156 LV 157
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
22-179 |
2.15e-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: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 22 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEHALDvQY---AAKLGVNV 98
Cdd:cd01121 59 EEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 99 PELLIsqpdTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCLV 176
Cdd:cd01121 137 DNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIPV 203
|
...
gi 2000171745 177 IFI 179
Cdd:cd01121 204 FLV 206
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
19-249 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 19 DVKEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKLGGTA----AFIDAEHALD----V 88
Cdd:TIGR02238 70 QKRKKVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGGGngkvAYIDTEGTFRpdriR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 89 QYAAKLGVN----VPELLISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQA 161
Cdd:TIGR02238 149 AIAERFGVDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQM 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 162 LRKLTGTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKV 238
Cdd:TIGR02238 225 LSRLNKISEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK-GR---------GEERVAKLYDSP 294
|
250
....*....|.
gi 2000171745 239 SPPFREAIFDI 249
Cdd:TIGR02238 295 DMPEAEASFQI 305
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
46-187 |
3.10e-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: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 46 GRVVEIYGPESSGKTTLTLQVIAELQ------KLGGTAAFIDAE-----HALDV-QYAAKLGV--NVPELLISQPDtgeq 111
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2000171745 112 aleitdalvrsgsIDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 187
Cdd:cd19492 77 -------------VKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
27-263 |
9.30e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 49.61 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKLG-GTAAFIDAEHALD----VQYAAKLGV 96
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQLpieQGGGeGKVLYIDTEGTFRperiVQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 97 NVPELL----ISQPDTGEQALEI---TDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 167
Cdd:PTZ00035 179 DPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlGKFLRALQK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 168 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRVKVVKNKVSPPFRE 244
Cdd:PTZ00035 253 LADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGRG-----EQRICKIYDSPNLPESE 322
|
250
....*....|....*....
gi 2000171745 245 AIFdilygeGISRQGeIID 263
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 ... |
49-203 |
4.87e-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: 45.19 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 49 VEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAehALDVQYAAKlgvnvpellisqpdtgeqaleitdALVRSGSIDMI 128
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF--LDTILEAIE------------------------DLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2000171745 129 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 203
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
27-80 |
6.77e-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: 6.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2000171745 27 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFI 80
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
45-179 |
3.25e-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: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 45 RGRVVEIYGPESSGKTTLTLQViaelqklgGTAAFIDAEHALDVQYAAKLgvNVPELLISQPDTGEQALEITDALVRsgS 124
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2000171745 125 IDMIVIDSVAALV-----------PKAEIEGEMGDSLP-GLQARLMSQALRKLTGTIKRtnclVIFI 179
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGKN----VIFT 131
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
41-137 |
8.52e-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: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 41 GGLPRGRVVEIYGPESSGKTTLTLQVIAEL-QKLGGTAAFID------AEHALD-VQYAAKLGVNVPELL-------ISQ 105
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQiLKSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 2000171745 106 PDTGEQALEITDALVR------SGSIDMIVIDSVAALV 137
Cdd:cd19489 82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
51-137 |
9.10e-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: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 51 IYGPESSGKTTLTLQVIAELQKLGGTAAFIDA-----EHALDVQYAAK-----LGVNVPELLISQPDTGEQALE-ITDAL 119
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRrlaeaLGIAVPKAELEESKLAFLAIElLLEAL 104
|
90
....*....|....*...
gi 2000171745 120 VRSGSIDMIVIDSVAALV 137
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
21-143 |
1.31e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 39.57 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 21 KEDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKLGGTAAFIDAEH------------ALDV 88
Cdd:PRK06067 1 EGKKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENtsksylkqmesvKIDI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 89 -QYAAKLGVNVPELLISQ----PDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIE 143
Cdd:PRK06067 80 sDFFLWGYLRIFPLNTEGfewnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
43-179 |
2.86e-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: 38.13 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 43 LPRGRVVEIYGPESSGKTTLTLQVIA-----------ELQKLGGTAAFIDAEHALDVQ----YAAKLGVNVPELL----- 102
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpwlggPRVPEQGKVLYVSAEGPADELrrrlRAAGADLDLPARLlflsl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 103 -----ISQPDTGEQAL-----EITDALVRSGSIDMIVIDSVAALVPkaeiegemGDSLPGLQARLMSQALRKLtgtIKRT 172
Cdd:pfam13481 110 veslpLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRL---ARRT 178
|
....*..
gi 2000171745 173 NCLVIFI 179
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 ... |
37-177 |
6.65e-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: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000171745 37 ALGVGgLPRGrvVEIYGPESSGKTTLTLQVIAELQklggtAAFIDaehaldvqyaaklgVNVPELLISQPDTGEQALEIT 116
Cdd:cd19530 24 ALGID-LPTG--VLLYGPPGCGKTLLAKAVANESG-----ANFIS--------------VKGPELLNKYVGESERAVRQV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2000171745 117 DALVRSGSIDMIVIDSVAALVPKaeiegeMGDSLPGLQARLMSQALRKLTGTIKRTNCLVI 177
Cdd:cd19530 82 FQRARASAPCVIFFDEVDALVPK------RGDGGSWASERVVNQLLTEMDGLEERSNVFVI 136
|
|
| |
