|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-341 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 681.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 1 MNDRQAALDQALKQIEKQFGKGSIMKLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAE 80
Cdd:PRK09354 4 DEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 81 VQAQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDA 160
Cdd:PRK09354 84 AQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 161 HVGLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKT 240
Cdd:PRK09354 164 HVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 241 KIKVVKNKVAPPFRIAEVDIMYGEGISREGELVDMAAEVDVINKSGSWYSYKEERIGQGRENAKQYLKEHTDIRDEISKR 320
Cdd:PRK09354 244 KVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKK 323
|
330 340
....*....|....*....|.
gi 489863227 321 VREEYEIDGTNKEPLDENEET 341
Cdd:PRK09354 324 IREKLGLSAAAAEEEEEEDEE 344
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
2-340 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 664.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 2 NDRQAALDQALKQIEKQFGKGSIMKLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEV 81
Cdd:COG0468 8 SEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 82 QAQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDAH 161
Cdd:COG0468 88 QKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 162 VGLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKTK 241
Cdd:COG0468 168 VGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 242 IKVVKNKVAPPFRIAEVDIMYGEGISREGELVDMAAEVDVINKSGSWYSYKEERIGQGRENAKQYLKEHTDIRDEISKRV 321
Cdd:COG0468 248 VKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKI 327
|
330
....*....|....*....
gi 489863227 322 REEYEIDGTNKEPLDENEE 340
Cdd:COG0468 328 REKLGLGAVSEAAAAEEEE 346
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
3-323 |
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: 607.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 3 DRQAALDQALKQIEKQFGKGSIMKLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ 82
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 83 AQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDAHV 162
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 163 GLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKTKI 242
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 243 KVVKNKVAPPFRIAEVDIMYGEGISREGELVDMAAEVDVINKSGSWYSYKEERIGQGRENAKQYLKEHTDIRDEISKRVR 322
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVR 320
|
.
gi 489863227 323 E 323
Cdd:TIGR02012 321 E 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
7-267 |
0e+00 |
|
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA repair systems. RecA protein catalyzes an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination.
Pssm-ID: 425488 [Multi-domain] Cd Length: 262 Bit Score: 525.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 7 ALDQALKQIEKQFGKGSIMKLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGG 86
Cdd:pfam00154 2 ALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 87 TAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDAHVGLQA 166
Cdd:pfam00154 82 TAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 167 RLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKTKIKVVK 246
Cdd:pfam00154 162 RLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVK 241
|
250 260
....*....|....*....|.
gi 489863227 247 NKVAPPFRIAEVDIMYGEGIS 267
Cdd:pfam00154 242 NKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
34-268 |
2.09e-174 |
|
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: 483.21 E-value: 2.09e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 34 NISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDPAYAKNLGVNIDELL 113
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 114 LSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDAHVGLQARLMSQALRKLSGVINKSKTIAIFINQI 193
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489863227 194 REKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKTKIKVVKNKVAPPFRIAEVDIMYGEGISR 268
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
3-248 |
1.59e-127 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 383.67 E-value: 1.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 3 DRQAALDQALKQIEKQFGKGSIMKLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ 82
Cdd:PRK09519 6 DREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 83 AQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVIDSVAALVPRAEIEGEMGDAHV 162
Cdd:PRK09519 86 AAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 163 GLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRAEQLKQGTDVMGNKTKI 242
Cdd:PRK09519 166 GLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRV 245
|
....*.
gi 489863227 243 KVVKNK 248
Cdd:PRK09519 246 KVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
57-225 |
8.40e-49 |
|
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: 162.14 E-value: 8.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 57 GRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDPAYA-----------KNLGVNIDELLLSQPDTGEQALE 125
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 126 IAEALVRSGA----VDMLVIDSVAALVPRAEIEGEMGDAHVGLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMF 201
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 489863227 202 G-NPEITPGGRALKFYSTVRLEVRR 225
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
216-336 |
2.76e-25 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 107.10 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 216 YSTVR--LEVRRAEQLKQGTDVMGNKTKIKVVKNKVAPPFRIAEVDIMYGEGISREGELVDMAAEVDVINKSGSWYSYKE 293
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489863227 294 ERIGQGRENAKQYLKEHTDIRDEISKRVREEYEI----------DGTNKEPLD 336
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGIgavvtddpsnDGVLPAPVD 789
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
38-230 |
2.60e-18 |
|
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: 82.36 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEhALDPAYAK-----NLGVNIDEL 112
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPERFQqiageRFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 113 LLSQP-DTGEQALEI--AEALVRSGAVDMLVIDSVAALVpRAEiegEMGDAhvGLQARLMSQaLRKLSGVINKSKTIAIF 189
Cdd:cd01394 79 IVFEPySFDEQGVAIqeAEKLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489863227 190 INQIREKvgvmFGNPEITP-GGRALKFYSTVRLEVRRAEQLK 230
Cdd:cd01394 152 TNQVYSD----IDDDRLKPvGGTLLEHWSKAIIRLEKSPPGL 189
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
45-229 |
1.86e-16 |
|
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).
Pssm-ID: 274047 [Multi-domain] Cd Length: 209 Bit Score: 77.07 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 45 LDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEhALDPAYAKNLGVNIDELLLSQP------- 117
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNFivfevfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 118 -DTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEIEGEMGDAHVGLQARlmsqaLRKLSGVINKSKTIAIFINQIREK 196
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 489863227 197 VgvmfGNPEITP-GGRALKFYS--TVRLEVRRAEQL 229
Cdd:TIGR02237 153 V----NNGTLRPlGGHLLEHWSkvILRLEKFRGRRL 184
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
1-142 |
1.11e-14 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 72.27 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 1 MNDRQAALDQALKQIEKqfgkgsimkLGEHSDQNISTISSGSLALDIALGVGGYPRGRIIEVYGPE-SSGKTTVALHAIA 79
Cdd:COG4544 1 MSAARTALAALRRRIWR---------GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489863227 80 EVQAQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAVDMLVID 142
Cdd:COG4544 72 RLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
34-226 |
2.26e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 71.43 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 34 NISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEhALDPAYAKNL-GVNIDEL 112
Cdd:PRK09361 1 MDERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 113 L----LSQP-DTGEQ--ALEIAEALVRSGaVDMLVIDSVAALVpRAEIEGEMGDAhvGLQARLMSQaLRKLSGVINKSKT 185
Cdd:PRK09361 79 LsniiIFEPsSFEEQseAIRKAEKLAKEN-VGLIVLDSATSLY-RLELEDEEDNS--KLNRELGRQ-LTHLLKLARKHDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489863227 186 IAIFINQIREKVgvmfGNPEITP-GGRALKFYS--TVRLE-----VRRA 226
Cdd:PRK09361 154 AVVITNQVYSDI----DSDGLRPlGGHTLEHWSktILRLEkfrngKRRA 198
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
30-228 |
5.14e-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: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 30 HSDQNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP-- 99
Cdd:pfam08423 11 QRRSELIQITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLC-HTLC-VTCQlplemgggEGKALYIDTEGTFRPer 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 100 --AYAKNLGVNIDELLLSQP-------DTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEIE--GEMGDAHVGLqARL 168
Cdd:pfam08423 88 lvAIAERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489863227 169 MSqALRKLSGVINksktIAIFI-NQIREKVG---VMF-GNPEITPGGRALKFYSTVRLEVR--RAEQ 228
Cdd:pfam08423 166 LR-TLQRLADEFG----VAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRkgRGEQ 227
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
38-228 |
6.67e-13 |
|
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: 67.38 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----AYAKNL 105
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLC-VTAQlpgsmgggGGKVAYIDTEGTFRPdrirPIAERF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 106 GVN----IDELLLSQPDTGEQALEI----AEALVRSGAVDMLVIDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLRK 175
Cdd:cd19514 78 GVDhdavLDNILYARAYTSEHQMELldyvAAKFHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489863227 176 LSGVINksktIAIFI-NQIREKVG--VMF-GNPEITPGGRALKFYSTVRLEVR--RAEQ 228
Cdd:cd19514 155 ISEEYN----VAVFItNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRkgRGEE 209
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
38-225 |
1.54e-12 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 66.40 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----AYAKNL 105
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLA-VTCQlpidrgggEGKAIYIDTEGTFRPerlrAIAQRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 106 GVNIDELLLS-------QPDTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEI--EGEMGDAHVGLqARLMSqALRKL 176
Cdd:cd01123 78 GLDPDDVLDNvayarafNSDHQTQLLDQAAAMMVESRFKLLIVDSATALY-RTDYsgRGELSARQMHL-AKFLR-MLQRL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489863227 177 SGVINksktIAIFI-NQIREKVG---VMFGNPEITPGGRALKFYSTVRLEVRR 225
Cdd:cd01123 155 ADEFG----VAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
38-225 |
1.41e-11 |
|
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: 63.54 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----AYAKNL 105
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLC-HQLA-VNVQlppeegglNGKAVYIDTENTFRPerimQMAKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 106 GVNIDELL-----LSQPDTGEQAL--EIAEALVRSG-AVDMLVIDSVAALVpRAEI--EGEMGDAHVGLqARLMSQaLRK 175
Cdd:cd19515 78 GLDPDEVLdniyvARAYNSNHQMLlvEKAEDLIKEGnNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHD-LHR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489863227 176 LSGVINksktIAIFI-NQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRR 225
Cdd:cd19515 155 LADLYN----IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
33-226 |
2.90e-11 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 63.74 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 33 QNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----A 100
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQIC-HQLA-VNVQlpeekgglEGKAVYIDTEGTFRPerieQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 101 YAKNLGVNIDELL-----LSQPDTGEQAL--EIAEALVRSG-AVDMLVIDSVAALVpRAEiegemgdaHVGL------QA 166
Cdd:PRK04301 156 MAEALGLDPDEVLdnihvARAYNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQ 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489863227 167 RLMSQ--ALRKLSGVINkskTIAIFINQIREKVGVMFGNPEITPGGRALKFYSTVRLEVRRA 226
Cdd:PRK04301 227 KLNKHlhDLLRLADLYN---AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRKS 285
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
33-228 |
6.41e-11 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 62.71 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 33 QNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----A 100
Cdd:PTZ00035 95 KNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLC-HTLC-VTCQlpieqgggEGKVLYIDTEGTFRPerivQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 101 YAKNLGVNIDELL----LSQPDTGEQALEI---AEALVRSGAVDMLVIDSVAALVpRAEI--EGEMGDAHVGLqARLMSq 171
Cdd:PTZ00035 172 IAERFGLDPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYsgRGELAERQQHL-GKFLR- 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489863227 172 ALRKLSGVINksktIAIFI-NQIREKVG---VMFGNPEITPGGRALKFYSTVRLEVR--RAEQ 228
Cdd:PTZ00035 249 ALQKLADEFN----VAVVItNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRkgRGEQ 307
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
38-205 |
9.93e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 60.70 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDP--AYAKNLGVNIDELL-- 113
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 114 -----------LSQPDTGEQALEIAEALVRSGAvDMLVIDSVAALVPRAEIEGEmgdahvglqARLMsqaLRKLSGVINK 182
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 489863227 183 SKTIAIFINQIREKVGVMFGNPE 205
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-227 |
3.66e-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: 57.77 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 56 RGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDPAYAKNLGVNIDELLLSqpDTGEQALEIAEALVRSGA 135
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 136 VDMLVIDSVAALVPRaeiegemgdahVGLQARLMSQALRKLSGVINKSKTIAIFINqirekvgvmfgNPEITPGGRALKF 215
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|..
gi 489863227 216 YSTVRLEVRRAE 227
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
46-225 |
8.80e-10 |
|
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: 58.10 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 46 DIALGvGGYPRGRIIEVYGPESSGKTTVALH----AIAEVQAQGGTAA--FIDAEHALDP-------------AYAKNLG 106
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTlassAAMPARKGGLDGGvlYIDTESKFSAerlaeiaearfpeAFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 107 VNIDELLLSQ------PDTGEQALEIAEAL---VRSGAVDMLVIDSVAALVpRAEIEGEMGDA---HVGLqARLMSqALR 174
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALV-RREFGGSDGEVterHNAL-AREAS-SLK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489863227 175 KLSgviNKSKTIAIFINQIREKVG-VMFGNPEITPG-GRALKFYSTVRLEVRR 225
Cdd:cd19493 157 RLA---EEFRIAVLVTNQATTHFGdAGDGSSGVTAAlGDAWAHAVNTRLRLER 206
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
38-228 |
9.70e-10 |
|
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: 58.10 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----AYAKNL 105
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLC-HTLA-VTCQlpidqgggEGKALYIDTEGTFRPerllAIAERY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 106 GVNIDELLLS-------QPDTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEIEGEmGDahvgLQARLM--SQALRKL 176
Cdd:cd19513 78 GLNGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRML 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489863227 177 SGVINKSKtIAIFI-NQIREKV--GVMFGNPEITP-GGRALKFYSTVRLEVR--RAEQ 228
Cdd:cd19513 152 QRLADEFG-VAVVItNQVVAQVdgAAMFAGDPKKPiGGNIMAHASTTRLYLRkgRGET 208
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
33-225 |
1.23e-09 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 58.98 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 33 QNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQAQGGT--AAFIDAEHALDP----AYA 102
Cdd:PLN03186 100 QEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGGEgkAMYIDTEGTFRPqrliQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 103 KNLGVNIDELL----LSQPDTGEQALEI---AEALVRSGAVDMLVIDSVAALVpRAEIEGEmGDahvgLQAR--LMSQAL 173
Cdd:PLN03186 179 ERFGLNGADVLenvaYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKFL 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489863227 174 RKLSGVINKSkTIAIFI-NQIREKV--GVMFGNPEITP-GGRALKFYSTVRLEVRR 225
Cdd:PLN03186 253 RSLQRLADEF-GVAVVItNQVVAQVdgSAFFAGPQLKPiGGNIMAHASTTRLALRK 307
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
38-228 |
6.03e-09 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 56.71 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIA-----EVQAQGGTA--AFIDAEHALDP----AYAKNLG 106
Cdd:PLN03187 108 ITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlPTEMGGGNGkvAYIDTEGTFRPdrivPIAERFG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 107 VN----IDELLLSQPDTGEQ---ALEIAEALVRSGAVDMLVIDSVAALVpRAEI--EGEMGDAhvglQARLmSQALRKLS 177
Cdd:PLN03187 186 MDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALF-RVDFtgRGELAER----QQKL-AQMLSRLT 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489863227 178 GVINKSKTIAIFINQIREKVG--VMFGNPEITPGGRALKFYSTVRLEVR--RAEQ 228
Cdd:PLN03187 260 KIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRkgKGEQ 314
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
33-228 |
8.84e-09 |
|
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: 55.94 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 33 QNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVAlHAIAeVQAQ--------GGTAAFIDAEHALDP----A 100
Cdd:TIGR02238 73 KKVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLS-HTLC-VTAQlpremgggNGKVAYIDTEGTFRPdrirA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 101 YAKNLGVN----IDELLLSQPDTGEQALEIAE---ALVRSGAVDMLVIDSVAALVpRAEI--EGEMGDAHVGLqARLMSQ 171
Cdd:TIGR02238 150 IAERFGVDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFsgRGELSERQQKL-AQMLSR 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489863227 172 aLRKLSGVINksktIAIFI-NQIREKVG--VMF-GNPEITPGGRALKFYSTVRLEVR--RAEQ 228
Cdd:TIGR02238 228 -LNKISEEFN----VAVFVtNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRkgRGEE 285
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
45-198 |
1.35e-08 |
|
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: 54.99 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 45 LDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ------AQGGTAAFIDAEHAL----------------DPAYA 102
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 103 KNLGVNIDELLLSQPDTGEQAL-EIAEALVRSGAVDMLVIDSVAALVpRAEIEGEMGDahVGLQARLMSQALRKLSGVIN 181
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSD--LVERAKYLRRLADHLKRLAD 156
|
170
....*....|....*..
gi 489863227 182 KSKTIAIFINQIREKVG 198
Cdd:cd19491 157 KYNLAVVVVNQVTDRFD 173
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
33-225 |
1.13e-07 |
|
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: 52.80 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 33 QNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQAQG--GTAAFIDAEHALDP----AYA 102
Cdd:TIGR02239 73 QEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFRPerllAIA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 103 KNLGVNIDELLLS-------QPDTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEIEGEmGDahvgLQARLMSQA--L 173
Cdd:TIGR02239 152 ERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArfL 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489863227 174 RKLSGVINKSKTIAIFINQIREKV---GVMFGNPEITP-GGRALKFYSTVRLEVRR 225
Cdd:TIGR02239 226 RSLQRLADEFGVAVVITNQVVAQVdgaGSMFAGDPKKPiGGNIMAHASTTRLSLRK 281
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
57-225 |
1.31e-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: 51.58 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 57 GRIIEVYGPESSGKTTVALHAIA-----------EVQAQGGTAAFIDAEHALD-----------------PAYAKNLGVN 108
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDilrlrsileariraaiqAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 109 IDELLLS--------QPDTGEQALEIAEAL-------VRSGAVDMLVIDSVAALVPRAEIEGEMGDAHVGLQARLMSQAL 173
Cdd:cd19490 81 VEEIAREclqrlhifRCHSSLQLLATLLSLenyllslSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489863227 174 RKLSGVINKSKTIAIF----INQIREKVGVMFGNPEITPGGRALKF----------YSTVRLEVRR 225
Cdd:cd19490 161 RELRRLRRRFQLVVIAtkqaLFPGKSASTDNPAANNAVSKASAPSHreylprpwqrLVTHRLVLSR 226
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
38-210 |
5.78e-07 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFI----DAEHALDPAYAK--NLGVNIDE 111
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFtfeeSPERLLRNAKSFgwDFDEMEDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 112 LLLSQPD---------TGEQALEIAEALVRSGAVDMLVIDSVAALvpRAEIEGEMgdahvglQARlmsQALRKLSGVINK 182
Cdd:cd01124 80 GKLIIVDappteagrfSLDELLSRILSIIKSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRA 147
|
170 180
....*....|....*....|....*...
gi 489863227 183 SKTIAIFINQIREkvgvmFGNPEITPGG 210
Cdd:cd01124 148 AGVTTIFTSEMRS-----FLSSESAGGG 170
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
55-176 |
8.99e-06 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 46.82 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 55 PRGRIIEVYGPESSGKTTVALHAIAEV---------QAQGGTAAFIDAE---HALDP---AYAKNLGVNIDEL-----LL 114
Cdd:COG3598 11 PEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEddrGELRRrlkALGADLGLPFADLdgrlrLL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489863227 115 SQPDTGE--QALEIAEALVRSGAVDMLVIDSVAALVPraeiegemGDAHVGLQARLMSQALRKL 176
Cdd:COG3598 91 SLAGDLDdtDDLEALERAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL 146
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
52-195 |
1.42e-05 |
|
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: 45.70 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 52 GGYPRGRIIEVYGPESSGKTTVALH-AIAEVQAQGGTAAFIDA-EHALD-PAYAKNLGVNIDELL---------LSQPDT 119
Cdd:pfam06745 14 GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLEKLEeegklaiidASTSGI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 120 GEQALEIAEAL----------VRSGAVDMLVIDSVAALvprAEIEGEMgdahvglQARlmsQALRKLSGVINKSKTIAIF 189
Cdd:pfam06745 94 GIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRRLKRVLKGLGVTAIF 160
|
....*.
gi 489863227 190 INQIRE 195
Cdd:pfam06745 161 TSEKPS 166
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
60-214 |
7.01e-05 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 41.72 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 60 IEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAehaldpayaknlgvnidelllsqPDTgeqALEIAEALVRSGAVDML 139
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF-----------------------LDT---ILEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489863227 140 VIDSVAALVPRAEiegemgdahvGLQARLMSQALRKLSGVINKSKTIAIFINQIREKVGVMFGNPEITPGGRALK 214
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
38-91 |
2.14e-04 |
|
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: 41.95 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489863227 38 ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFI 91
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
38-147 |
4.40e-04 |
|
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410892 [Multi-domain] Cd Length: 218 Bit Score: 41.16 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 38 ISSGSLALDIALGVGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDPAY--AKNLGVNIDELLLS 115
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489863227 116 Q---------PDTG-EQALEIAEALVRSGAVDMLVIDSVAAL 147
Cdd:cd19484 81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSAL 122
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
52-227 |
4.47e-04 |
|
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410897 [Multi-domain] Cd Length: 209 Bit Score: 41.08 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 52 GGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGG-TAAFIDAEHALDP-------AYAKNLGVNIDEL----------- 112
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGqNVLYIDTKSSFSArrlaqilKSRAQDAEEIDKAlqrirvvrvfd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 113 ---LLSQPDTGEQALEIAEALVRSGaVDMLVIDSVAALVprAEIEGemGDAHVGLQARLMSQA--LRKLSgvinKSKTIA 187
Cdd:cd19489 82 pyeLLDLLEELRNTLSQQQENLYSR-LKLVIIDSLSALI--SPLLG--GSKHSEGHALLASLArlLKKLA----AEYQIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489863227 188 IFINQIREKVGVMFGNPEITPG-GRALKFYSTVRLEVRRAE 227
Cdd:cd19489 153 VLVTNLTVRGGDGGQQGSTKPAlGEYWESVPSTRLLLSRDE 193
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
25-190 |
5.60e-04 |
|
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: 40.98 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 25 MKLGEHSDQNISTISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDP--AYA 102
Cdd:cd01121 51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQikLRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 103 KNLGVNIDELLLsqpdTGEQALEIAEALVRSGAVDMLVIDSVAALVpRAEIEGEMGDAhvgLQARLMSQALRKLSgvinK 182
Cdd:cd01121 130 ERLGLGSDNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVY-SPELTSSPGSV---SQVRECAAELLRLA----K 197
|
....*...
gi 489863227 183 SKTIAIFI 190
Cdd:cd01121 198 ETGIPVFL 205
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
25-94 |
7.45e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.40 E-value: 7.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489863227 25 MKLgehsDQNIST--ISSGSLALDIALGvGGYPRGRIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAE 94
Cdd:PRK09302 244 MRL----TQRSSNerISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFE 310
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
62-99 |
1.34e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 39.11 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489863227 62 VYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDP 99
Cdd:cd17929 20 LHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTP 57
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
58-142 |
2.86e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.32 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 58 RIIEVYGPESSGKTTVALHAIAEVQAQGGTAAFIDAEHALDPA-YAKNLGVNIDELLLSQPDTGEQALEIAEALVRSGAV 136
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKdLLRALLRALGLPLSGRLSKEELLAALQQLLLALAVA 85
|
....*.
gi 489863227 137 DMLVID 142
Cdd:pfam13401 86 VVLIID 91
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
51-152 |
4.01e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 37.75 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 51 VGGY-PRGRIIEVYGPESSGKTTVALH---AIA--------EVQAQGGTAAFIDAE--------------HALDPAYAKN 104
Cdd:pfam13481 26 IKGLlPAGGLGLLAGAPGTGKTTLALDlaaAVAtgkpwlggPRVPEQGKVLYVSAEgpadelrrrlraagADLDLPARLL 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489863227 105 LGVNIDELLLSQPDTGEQAL-----EIAEALVRSGAVDMLVIDSVAALVPRAE 152
Cdd:pfam13481 106 FLSLVESLPLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALGGDE 158
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
56-144 |
5.97e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 37.31 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863227 56 RGRIIEVYGPESSGKTTVALHAiaevqaqgGTAAFIDAEHALDPAYAKNlGVNIDElLLSQPDTGEQALEIAEALVRSga 135
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDR-FPDIVI-RDSWQDFLDAIDELTAAELAD-- 68
|
....*....
gi 489863227 136 VDMLVIDSV 144
Cdd:pfam13479 69 YKTIVIDTV 77
|
|
| |
