|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-310 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 658.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 1 FGKGSIMRMGDGEvAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHAL 80
Cdd:PRK09354 22 FGKGSIMRLGDDA-AMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 81 DVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLT 160
Cdd:PRK09354 101 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 161 GTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAI 240
Cdd:PRK09354 181 GNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAE 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 241 FDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESLGV 310
Cdd:PRK09354 261 FDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKKIREKLGL 330
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-310 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 639.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 1 FGKGSIMRMGDGEVaENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHAL 80
Cdd:COG0468 25 FGKGSIMRLGDKAR-QDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 81 DVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLT 160
Cdd:COG0468 104 DPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 161 GTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAI 240
Cdd:COG0468 184 GAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAE 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 241 FDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESLGV 310
Cdd:COG0468 264 FDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKIREKLGL 333
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-306 |
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: 576.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 1 FGKGSIMRMGDgEVAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHAL 80
Cdd:TIGR02012 17 FGKGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 81 DVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLT 160
Cdd:TIGR02012 96 DPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 161 GTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAI 240
Cdd:TIGR02012 176 GALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170664172 241 FDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRE 306
Cdd:TIGR02012 256 FDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVRE 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-250 |
8.10e-178 |
|
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: 491.53 E-value: 8.10e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 1 FGKGSIMRMGDGEVaENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHAL 80
Cdd:pfam00154 14 FGKGSIMKLGDEKK-LDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 81 DVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLT 160
Cdd:pfam00154 93 DPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 161 GTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAI 240
Cdd:pfam00154 173 GSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAE 252
|
250
....*....|
gi 170664172 241 FDILYGEGIS 250
Cdd:pfam00154 253 FDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
17-251 |
5.12e-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: 465.49 E-value: 5.12e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 17 NIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL 96
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 176
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170664172 177 RMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISR 251
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-231 |
1.28e-109 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 335.91 E-value: 1.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 1 FGKGSIMRMGDgEVAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHAL 80
Cdd:PRK09519 22 YGKGSVMRLGD-EARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 81 DVQYAAKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLT 160
Cdd:PRK09519 101 DPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170664172 161 GTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNK 231
Cdd:PRK09519 181 GALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
40-208 |
6.48e-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: 171.38 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 40 GRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPE-----------LLISQPDTGEQALE 108
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQILEASPSselelaealsrLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 109 ITDALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 184
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 170664172 185 G-NPETTTGGNALKFYSSVRLDIRR 208
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
199-310 |
1.04e-28 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 115.96 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 199 YSSVR--LDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNG 276
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110
....*....|....*....|....*....|....
gi 170664172 277 EKIGQGKDNAREFLRENPEIAREIENRIRESLGV 310
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGI 770
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
21-261 |
2.97e-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: 84.29 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELL---- 96
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERFESIAsnii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 ISQP-DTGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIFI 173
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 174 NQIRMKIGVMFGNPettTGGNALKFYSSVRLDIRRIGSikkndevignETRVKVVKNKVSPPfreaifdilygEGISRQG 253
Cdd:cd01394 153 NQVYSDIDDDRLKP---VGGTLLEHWSKAIIRLEKSPP----------GLRRATLEKHRSRP-----------EGQSAGF 208
|
....*...
gi 170664172 254 EIIDLGVQ 261
Cdd:cd01394 209 RITDRGIR 216
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
21-249 |
3.55e-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: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAELQK-LGGT---AAFIDAEHALD----VQYAAKLGV 90
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRperlVAIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 NVPELLISQP-------DTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 161
Cdd:pfam08423 98 DPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 162 TIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRV-KVVKnkvSP-- 234
Cdd:pfam08423 172 LADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLR-----KGRG-----EQRIcKIYD---SPcl 238
|
250
....*....|....*
gi 170664172 235 PFREAIFDIlYGEGI 249
Cdd:pfam08423 239 PESEAVFAI-GSGGI 252
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
21-188 |
7.24e-14 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 69.56 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPELL-- 96
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 -----------ISQPDTGEQALEITDAlVRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKR 165
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREA-VEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 170664172 166 TNCLVIFINQIRMKIGVMFGNPE 188
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
17-210 |
1.57e-13 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 68.35 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 17 NIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEhALDVQYAAKL-GVNVPEL 95
Cdd:PRK09361 1 MDERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 96 L----ISQP-DTGEQALEITDA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRTNC 168
Cdd:PRK09361 79 LsniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 170664172 169 LVIFINQIRMKIGvmfGNPETTTGGNALKFYSS--VRLDIRRIG 210
Cdd:PRK09361 154 AVVITNQVYSDID---SDGLRPLGGHTLEHWSKtiLRLEKFRNG 194
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
16-249 |
1.57e-13 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 69.91 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 16 ENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQK------LGGTAAFIDAEHALD----VQYA 85
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRperiEQMA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 86 AKLGVNVPELL-----ISQPDTGEQALEITDA--LVRSG-SIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLMSQ--A 155
Cdd:PRK04301 158 EALGLDPDEVLdnihvARAYNSDHQMLLAEKAeeLIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQQKLNKHlhD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 156 LRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP- 234
Cdd:PRK04301 235 LLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK----SKGNKRI-----ARLVD---SPh 299
|
250
....*....|....*.
gi 170664172 235 -PFREAIFDILyGEGI 249
Cdd:PRK04301 300 lPEGEAVFRIT-EEGI 314
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
21-243 |
6.03e-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: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQK------LGGTAAFIDAEHALD----VQYAAKLGV 90
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 NVPELL-----ISQPDTGEQAL---EITDALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 162
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 163 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP--PFREAI 240
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK----GKGGKRI-----ARLVD---SPhlPEGEAV 223
|
...
gi 170664172 241 FDI 243
Cdd:cd19515 224 FRI 226
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
28-208 |
7.60e-13 |
|
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: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 28 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEhALDVQYAAKLGVNVPELLISQ------PD 101
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 102 TGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMK 179
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180
....*....|....*....|....*....
gi 170664172 180 IGVMFGNPettTGGNALKFYSSVRLDIRR 208
Cdd:TIGR02237 153 VNNGTLRP---LGGHLLEHWSKVILRLEK 178
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
10-125 |
4.47e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 64.57 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 10 GDGEVAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVVAELQKLGGTAAFIDAEHALdvqYA--- 85
Cdd:COG4544 18 GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApgl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 170664172 86 AKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVID 125
Cdd:COG4544 95 AAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
29-211 |
7.23e-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: 63.88 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 29 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVVAELQKLGGTAA--FIDAEHALDVQ-------------YAAKLG 89
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 90 VNVPELLISQ------PDTGEQALEITDAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 160
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 170664172 161 GTIKRT----NCLVIFINQIRMKIGVMFGNPETTTG--GNALKFYSSVRLDIRRIGS 211
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-209 |
1.21e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.92 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 39 RGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALDVQYAAKLGVNVPELLISqpDTGEQALEITDALVRSGS 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 119 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINqirmkigvmfgNPETTTGGNALKF 198
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 170664172 199 YSSVRLDIRRI 209
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
28-176 |
2.71e-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: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 28 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVA------ELQKLGGTAAFIDAEHALDVQ----------------YA 85
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALtvqlprELGGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 86 AKLGVNVPELLISQPDTGEQALEITD-ALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 164
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 170664172 165 RTNCLVIFINQI 176
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
21-211 |
4.19e-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: 58.80 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQ-VVAELQKLGGTAAFIDA-EHALDV-QYAAKLGVNVPELL- 96
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 --------ISQPDTGEQALEITDAL----------VRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALRK 158
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 170664172 159 LTGTIKRTNCLVIFINQIRMKigvmfgnpETTTGGNALKFYSS---VRLDIRRIGS 211
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
21-249 |
6.47e-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: 58.31 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAELQ----KLGGTAAFIDAEHALD----VQYAAKLGV 90
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQLPidrgGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 NVPELL----ISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 161
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 162 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFRE 238
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK-GR---------GETRICKIYDSPCLPEAE 223
|
250
....*....|.
gi 170664172 239 AIFDIlYGEGI 249
Cdd:cd01123 224 AVFAI-TADGV 233
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
21-243 |
1.12e-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: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAELQKL----GGTAAFIDAEHALD----VQYAAKLGV 90
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 N----VPELLISQPDTGEQALEITDAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 160
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 161 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFR 237
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK-GR---------GEERIAKIYDSPDLPEN 223
|
....*.
gi 170664172 238 EAIFDI 243
Cdd:cd19514 224 EATFAI 229
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
21-177 |
2.82e-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: 56.12 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALD--VQYAAKLGVNVPEL--- 95
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 96 ----LISQPDTGEQALEITD------ALVRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 165
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 170664172 166 TNCLVIFINQIR 177
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
16-243 |
1.02e-08 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 55.51 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 16 ENIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEL--QKLGGT--AAFIDAEHALD----VQYA 85
Cdd:PLN03186 101 EIIQI-TTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 86 AKLGVNVPELL----ISQPDTGEQALEItdaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--LMS 153
Cdd:PLN03186 179 ERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmHLG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 154 QALRKLTGTIKRTNCLVIFINQIRMKI--GVMFGNPETT-TGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKN 230
Cdd:PLN03186 250 KFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGENRI-----CKVISS 320
|
250
....*....|...
gi 170664172 231 KVSPPfREAIFDI 243
Cdd:PLN03186 321 PCLPE-AEARFSI 332
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
21-249 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEL---QKLG-GTAAFIDAEHALD----VQYAAKLGV 90
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 NVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 161
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 162 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGNALKFYSSVRLDIRRigsikkndeviGN-ETRVKVVKNKVSPPFR 237
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK-----------GRgETRICKIYDSPCLPEA 222
|
250
....*....|..
gi 170664172 238 EAIFDIlYGEGI 249
Cdd:cd19513 223 EAVFAI-TEDGI 233
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
15-250 |
1.66e-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: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 15 AENIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEL---QKLG-GTAAFIDAEHALD----VQY 84
Cdd:TIGR02239 73 QEVIQL-TTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 85 AAKLGVNVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA-- 155
Cdd:TIGR02239 151 AERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArf 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 156 LRKLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNK 231
Cdd:TIGR02239 225 LRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK-GR---------GEQRICKIYDS 294
|
250
....*....|....*....
gi 170664172 232 VSPPFREAIFDIlYGEGIS 250
Cdd:TIGR02239 295 PCLPESEAMFAI-YEDGIG 312
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
21-208 |
2.09e-08 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 54.78 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEL-QKLGG---TAAFIDAEHALD----VQYAAKLGV 90
Cdd:PLN03187 108 ITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQLpTEMGGgngKVAYIDTEGTFRpdriVPIAERFGM 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 91 N----VPELLISQPDTGEQ---ALEITDALVRSGSIDMIVIDSVAALVPKAEI-EGEMGDSlpglQARLmSQALRKLTGT 162
Cdd:PLN03187 187 DadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSRLTKI 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 170664172 163 IKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNALKFYSSVRLDIRR 208
Cdd:PLN03187 262 AEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
15-173 |
9.59e-08 |
|
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: 52.15 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 15 AENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEHALDvQY---AAKLGVN 91
Cdd:cd01121 58 AEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 92 VPELLIsqpdTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCL 169
Cdd:cd01121 136 SDNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIP 202
|
....
gi 170664172 170 VIFI 173
Cdd:cd01121 203 VFLV 206
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
37-173 |
1.12e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 52.21 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 37 LPRGRVVEIYGPESSGKTTLTLQVVAELQK----LG-----GTAAFIDAE-HALDVQ-----YAAKLGVNVPEL-----L 96
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 IS-----QPDTGEQALEitdALVRSGSIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVI 171
Cdd:COG3598 90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVL 155
|
..
gi 170664172 172 FI 173
Cdd:COG3598 156 LV 157
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
40-181 |
1.36e-07 |
|
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: 51.19 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 40 GRVVEIYGPESSGKTTLTLQVVA-----------ELQKLGGTAAFIDAEHALDV------------QYAAKLGVNVPE-- 94
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDIlrlrsilearirAAIQAANSSDDEed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 95 -----------LLISQPDTGEQ------ALEIT-DALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 153
Cdd:cd19490 81 veeiareclqrLHIFRCHSSLQllatllSLENYlLSLSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 170664172 154 QALRKLTgtiKRTNCLVIFINQIRMKIG 181
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
20-243 |
1.52e-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: 52.09 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 20 VVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAELQKLGGTA----AFIDAEHALD----VQYAAKLG 89
Cdd:TIGR02238 77 KITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGGGngkvAYIDTEGTFRpdriRAIAERFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 90 VN----VPELLISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 162
Cdd:TIGR02238 156 VDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLNKI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 163 IKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFREA 239
Cdd:TIGR02238 232 SEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK-GR---------GEERVAKLYDSPDMPEAEA 301
|
....
gi 170664172 240 IFDI 243
Cdd:TIGR02238 302 SFQI 305
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
40-181 |
2.31e-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: 49.92 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 40 GRVVEIYGPESSGKTTLTLQVVAELQ------KLGGTAAFIDAE-----HALDV-QYAAKLGV--NVPELLISQPDtgeq 105
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170664172 106 aleitdalvrsgsIDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 181
Cdd:cd19492 77 -------------VKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
16-257 |
4.66e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 50.38 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 16 ENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEL---QKLG-GTAAFIDAEHALD----VQYA 85
Cdd:PTZ00035 95 KNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQLpieQGGGeGKVLYIDTEGTFRperiVQIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 86 AKLGVNVPELL----ISQPDTGEQALEI---TDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQAL 156
Cdd:PTZ00035 174 ERFGLDPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlGKFL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 157 RKLTGTIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRVKVVKNKVS 233
Cdd:PTZ00035 248 RALQKLADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGRG-----EQRICKIYDSPN 317
|
250 260
....*....|....*....|....
gi 170664172 234 PPFREAIFdilygeGISRQGeIID 257
Cdd:PTZ00035 318 LPESEAVF------AISEGG-IID 334
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
43-197 |
2.92e-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: 45.57 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 43 VEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAehALDVQYAAKlgvnvpellisqpdtgeqaleitdALVRSGSIDMI 122
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF--LDTILEAIE------------------------DLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170664172 123 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 197
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
21-74 |
8.42e-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: 8.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 170664172 21 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFI 74
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
39-173 |
2.42e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 41.54 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 39 RGRVVEIYGPESSGKTTLTLQVvaelqklgGTAAFIDAEHALDVQYAAKLgvNVPELLISQPDTGEQALEITDALVRsgS 118
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170664172 119 IDMIVIDSVAALV-----------PKAEIEGEMGDSLP-GLQARLMSQALRKLTGTIKRtnclVIFI 173
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGKN----VIFT 131
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
37-173 |
7.49e-04 |
|
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: 40.06 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 37 LPRGRVVEIYGPESSGKTTLTLQVVA-----------ELQKLGGTAAFIDAEHALDVQ----YAAKLGVNVPELL----- 96
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpwlggPRVPEQGKVLYVSAEGPADELrrrlRAAGADLDLPARLlflsl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 97 -----ISQPDTGEQAL-----EITDALVRSGSIDMIVIDSVAALVPkaeiegemGDSLPGLQARLMSQALRKLtgtIKRT 166
Cdd:pfam13481 110 veslpLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRL---ARRT 178
|
....*..
gi 170664172 167 NCLVIFI 173
Cdd:pfam13481 179 GATVLLV 185
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
45-131 |
1.23e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 39.61 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 45 IYGPESSGKTTLTLQVVAELQKLGGTAAFIDA-----EHALDVQYAAK-----LGVNVPELLISQPDTGEQALE-ITDAL 113
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRrlaeaLGIAVPKAELEESKLAFLAIElLLEAL 104
|
90
....*....|....*...
gi 170664172 114 VRSGSIDMIVIDSVAALV 131
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
35-131 |
1.90e-03 |
|
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410897 [Multi-domain] Cd Length: 209 Bit Score: 38.77 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 35 GGLPRGRVVEIYGPESSGKTTLTLQVVAEL-QKLGGTAAFID------AEHALD-VQYAAKLGVNVPELL-------ISQ 99
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQiLKSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 170664172 100 PDTGEQALEITDALVR------SGSIDMIVIDSVAALV 131
Cdd:cd19489 82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
31-171 |
4.19e-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: 37.08 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 31 ALGVGgLPRGrvVEIYGPESSGKTTLTLQVVAELQklggtAAFIDaehaldvqyaaklgVNVPELLISQPDTGEQALEIT 110
Cdd:cd19530 24 ALGID-LPTG--VLLYGPPGCGKTLLAKAVANESG-----ANFIS--------------VKGPELLNKYVGESERAVRQV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170664172 111 DALVRSGSIDMIVIDSVAALVPKaeiegeMGDSLPGLQARLMSQALRKLTGTIKRTNCLVI 171
Cdd:cd19530 82 FQRARASAPCVIFFDEVDALVPK------RGDGGSWASERVVNQLLTEMDGLEERSNVFVI 136
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
41-65 |
6.92e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 36.72 E-value: 6.92e-03
10 20
....*....|....*....|....*
gi 170664172 41 RVVeIYGPESSGKTTLTLQVVAELQ 65
Cdd:COG3172 10 KIV-LLGAESTGKTTLARALAAHYN 33
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
16-137 |
7.30e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 37.26 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170664172 16 ENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAELQKLGGTAAFIDAEH------------ALDV- 82
Cdd:PRK06067 2 GKKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENtsksylkqmesvKIDIs 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 170664172 83 QYAAKLGVNVPELLISQ----PDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIE 137
Cdd:PRK06067 81 DFFLWGYLRIFPLNTEGfewnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| |
