|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-333 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 682.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 1 MSDRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAE 80
Cdd:PRK09354 4 DEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 81 VQQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDS 160
Cdd:PRK09354 84 AQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 161 HVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKT 240
Cdd:PRK09354 164 HVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 241 KIKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQ 320
Cdd:PRK09354 244 KVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKK 323
|
330
....*....|...
gi 2326810373 321 IREHYGLDNNGVV 333
Cdd:PRK09354 324 IREKLGLSAAAAE 336
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
2-327 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 668.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 2 SDRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEV 81
Cdd:COG0468 8 SEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 82 QQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSH 161
Cdd:COG0468 88 QKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 162 VGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTK 241
Cdd:COG0468 168 VGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 242 IKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQI 321
Cdd:COG0468 248 VKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKI 327
|
....*.
gi 2326810373 322 REHYGL 327
Cdd:COG0468 328 REKLGL 333
|
|
| 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: 630.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 3 DRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ 82
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 83 QQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHV 162
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 163 GLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKI 242
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 243 KVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQIR 322
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVR 320
|
.
gi 2326810373 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: 531.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 7 ALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGG 86
Cdd:pfam00154 2 ALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 87 QAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQA 166
Cdd:pfam00154 82 TAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 167 RLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVK 246
Cdd:pfam00154 162 RLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVK 241
|
250 260
....*....|....*....|.
gi 2326810373 247 NKVAPPFRTAEVDIMYGEGIS 267
Cdd:pfam00154 242 NKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
34-268 |
1.38e-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: 483.98 E-value: 1.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 34 RISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEELL 113
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 114 LSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQI 193
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2326810373 194 REKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGISK 268
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
3-248 |
1.62e-127 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 383.67 E-value: 1.62e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 3 DRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ 82
Cdd:PRK09519 6 DREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 83 QQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHV 162
Cdd:PRK09519 86 AAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 163 GLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKI 242
Cdd:PRK09519 166 GLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRV 245
|
....*.
gi 2326810373 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 |
2.02e-50 |
|
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: 166.37 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 57 GRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQ-----------KLGVNIEELLLSQPDTGEQALE 125
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 126 IAEALVRSGA----VDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMF 201
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 2326810373 202 G-NPETTPGGRALKFYSSVRLEVRR 225
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
216-327 |
8.86e-25 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 105.56 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 216 YSSVR--LEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEE 293
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110
....*....|....*....|....*....|....
gi 2326810373 294 ERLGQGRENAKQFLKENKDIMLMIQEQIREHYGL 327
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGI 770
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
38-230 |
1.91e-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: 85.44 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPV-YAQKLGVNIEELL--- 113
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPErFQQIAGERFESIAsni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 114 -LSQP-DTGEQALEI--AEALVRSGAVDIVVVDSVAALVpKAEiegDMGDShvGLQARLMSQaLRKLSGaINKSKTIAIF 189
Cdd:cd01394 79 iVFEPySFDEQGVAIqeAEKLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLS-IARKYDIPVV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2326810373 190 I-NQIREKvgvmFGNPETTP-GGRALKFYSSVRLEVRRAEQLK 230
Cdd:cd01394 151 ItNQVYSD----IDDDRLKPvGGTLLEHWSKAIIRLEKSPPGL 189
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
1-142 |
4.73e-17 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 79.20 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 1 MSDRQAALDmALKqiekqfgkGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPE-SSGKTTVALHAIA 79
Cdd:COG4544 1 MSAARTALA-ALR--------RRIWRGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2326810373 80 EVQQQGGQAAFIDAEHALdpvYA---QKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVD 142
Cdd:COG4544 72 RLAQAGGPVLWIAPPYDL---YApglAAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
45-245 |
2.10e-15 |
|
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: 73.99 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 45 LDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPVYAQKLGVNIEELLLSQP------- 117
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNFivfevfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 118 -DTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGDMGDSHVGLQARlmsqaLRKLSGAINKSKTIAIFINQIREK 196
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2326810373 197 VgvmfGNPETTP-GGRALKFYSS--VRLE----VRRAEQLKQGNDVMGNKTKIKVV 245
Cdd:TIGR02237 153 V----NNGTLRPlGGHLLEHWSKviLRLEkfrgRRLATLEKHRSRPEGESVYFRIT 204
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
35-226 |
9.05e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 69.51 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 35 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPV-YAQKLGVNIEELL 113
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPErFKQIAGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 114 ----LSQP-DTGEQ--ALEIAEALVRSGaVDIVVVDSVAALVpKAEIEGDMGDShvGLQARLMSQaLRKLSGaINKSKTI 186
Cdd:PRK09361 80 sniiIFEPsSFEEQseAIRKAEKLAKEN-VGLIVLDSATSLY-RLELEDEEDNS--KLNRELGRQ-LTHLLK-LARKHDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2326810373 187 AIFI-NQIREKVgvmfGNPETTP-GGRALKFYSS--VRLE-----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 ... |
34-228 |
4.87e-13 |
|
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: 68.10 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 34 RISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQG--GQAAFIDAEHALDPV----YAQ 103
Cdd:pfam08423 18 QITT---GSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFRPErlvaIAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 104 KLGVNIEELLLSQP-------DTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIE--GDMGDSHVGLqARLMSqALR 174
Cdd:pfam08423 94 RYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-TLQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2326810373 175 KLSGAINksktIAIFI-NQIREKVG---VMF-GNPETTPGGRALKFYSSVRLEVR--RAEQ 228
Cdd:pfam08423 171 RLADEFG----VAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRkgRGEQ 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-227 |
3.39e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.46 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 56 RGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSqpDTGEQALEIAEALVRSGA 135
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 136 VDIVVVDSVAALVPKaeiegdmgdshVGLQARLMSQALRKLSGAINKSKTIAIFINqirekvgvmfgNPETTPGGRALKF 215
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|..
gi 2326810373 216 YSSVRLEVRRAE 227
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
38-205 |
4.64e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 61.86 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPV--YAQKLGVNIEELL-- 113
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 114 -----------LSQPDTGEQALEIAEALVRSGAvDIVVVDSVAALVPKAEIEGDmgdshvglqARLMsqaLRKLSGAINK 182
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 2326810373 183 SKTIAIFINQIREKVGVMFGNPE 205
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
38-228 |
1.86e-10 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 60.06 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ-------QGGQAAFIDAEHALDP----VYAQKLG 106
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLCVTAQlpgsmggGGGKVAYIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 107 VN----IEELLLSQPDTGEQALEI----AEALVRSGAVDIVVVDSVAALVpKAEI--EGDMGDSHVGLqARLMSQaLRKL 176
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELldyvAAKFHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2326810373 177 SGAINksktIAIFI-NQIREKVG--VMF-GNPETTPGGRALKFYSSVRLEVR--RAEQ 228
Cdd:cd19514 156 SEEYN----VAVFItNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRkgRGEE 209
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
38-225 |
6.48e-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: 58.70 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ-------QGGQAAFIDAEHALDPV----YAQKLG 106
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLAVTCQlpidrggGEGKAIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 107 VNIEELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEI-EGDMGDSHVGLqARLMSqALRKLSG 178
Cdd:cd01123 79 LDPDDVLDNvayarafNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLR-MLQRLAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2326810373 179 AINksktIAIFI-NQIREKVG---VMFGNPETTPGGRALKFYSSVRLEVRR 225
Cdd:cd01123 157 EFG----VAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
40-228 |
3.85e-09 |
|
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: 56.17 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 40 SGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQGGQ--AAFIDAEHALDPV----YAQKLGVNI 109
Cdd:cd19513 3 TGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVTCQLPIDQGGGEgkALYIDTEGTFRPErllaIAERYGLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 110 EELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQARLMS-----QALRKLS 177
Cdd:cd19513 82 EDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSG-RGE----LSARQMHlakflRMLQRLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2326810373 178 GAINksktIAIFI-NQIREKV--GVMFGNPETTP-GGRALKFYSSVRLEVR--RAEQ 228
Cdd:cd19513 156 DEFG----VAVVItNQVVAQVdgAAMFAGDPKKPiGGNIMAHASTTRLYLRkgRGET 208
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
34-226 |
7.43e-09 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 56.42 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 34 RISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ---QQGG---QAAFIDAEHALDP----VYAQ 103
Cdd:PRK04301 83 KITT---GSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeEKGGlegKAVYIDTEGTFRPerieQMAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 104 KLGVNIEELL-----LSQPDTGEQAL--EIAEALVRSG-AVDIVVVDSVAALVpKAEiegdmgdsHVGL------QARLM 169
Cdd:PRK04301 159 ALGLDPDEVLdnihvARAYNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLN 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2326810373 170 SQ--ALRKLSGAINkskTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRA 226
Cdd:PRK04301 230 KHlhDLLRLADLYN---AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRKS 285
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
46-198 |
1.39e-08 |
|
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: 54.63 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 46 DTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEV---QQQGGQAA---FIDAEHALDP-------------VYAQKLG 106
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampARKGGLDGgvlYIDTESKFSAerlaeiaearfpeAFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 107 VNIEELLLSQ------PDTGEQALEIAEAL---VRSGAVDIVVVDSVAALVPKA--EIEGDMGDSHVGLqARLMSqALRK 175
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS-SLKR 157
|
170 180
....*....|....*....|...
gi 2326810373 176 LSgaiNKSKTIAIFINQIREKVG 198
Cdd:cd19493 158 LA---EEFRIAVLVTNQATTHFG 177
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
35-225 |
8.64e-08 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 53.20 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 35 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQG--GQAAFIDAEHALDP----VYAQK 104
Cdd:PLN03186 102 IIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGgeGKAMYIDTEGTFRPqrliQIAER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 105 LGVN----IEELLLSQPDTGEQALEI---AEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQAR--LMSQALRK 175
Cdd:PLN03186 181 FGLNgadvLENVAYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSG-RGE----LSARqmHLGKFLRS 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2326810373 176 LSgAINKSKTIAIFI-NQIREKV--GVMFGNPETTP-GGRALKFYSSVRLEVRR 225
Cdd:PLN03186 255 LQ-RLADEFGVAVVItNQVVAQVdgSAFFAGPQLKPiGGNIMAHASTTRLALRK 307
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
35-225 |
8.98e-08 |
|
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: 52.37 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 35 ISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQQ-------GGQAAFIDAEHALDP----VYAQ 103
Cdd:cd19515 1 IST---GSKELDKLLG-GGIETQAITEVFGEFGSGKTQLC-HQLAVNVQLppeegglNGKAVYIDTENTFRPerimQMAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 104 KLGVNIEELL-----LSQPDTGEQAL--EIAEALVRSG-AVDIVVVDSVAALVpKAEI--EGDMGDSHVGLqARLMSQaL 173
Cdd:cd19515 76 ALGLDPDEVLdniyvARAYNSNHQMLlvEKAEDLIKEGnNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHD-L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2326810373 174 RKLSGAINksktIAIFI-NQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRR 225
Cdd:cd19515 153 HRLADLYN----IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
35-225 |
1.64e-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: 52.03 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 35 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQGGQ--AAFIDAEHALDPV----YAQK 104
Cdd:TIGR02239 75 VIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGGEgkALYIDTEGTFRPErllaIAER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 105 LGVNIEELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQARLMSQA--LRK 175
Cdd:TIGR02239 154 YGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSG-RGE----LSARQMHLArfLRS 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2326810373 176 LSGAINKSKTIAIFINQIREKV---GVMFGNPETTP-GGRALKFYSSVRLEVRR 225
Cdd:TIGR02239 228 LQRLADEFGVAVVITNQVVAQVdgaGSMFAGDPKKPiGGNIMAHASTTRLSLRK 281
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
8-228 |
1.70e-07 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 52.09 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 8 LDMALKQIEKQFGKGSIMKLGEKTDTRISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIA-----EVQ 82
Cdd:PLN03187 81 CEAAEKLLNQGFITGSDALLKRKSVVRITT---GSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlPTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 83 QQGG--QAAFIDAEHALDP----VYAQKLGVN----IEELLLSQPDTGEQ---ALEIAEALVRSGAVDIVVVDSVAALVP 149
Cdd:PLN03187 156 MGGGngKVAYIDTEGTFRPdrivPIAERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 150 KAEI-EGDMGDSHVGLqARLMSQaLRKLSGAINksktIAIFI-NQIREKVG--VMFGNPETTPGGRALKFYSSVRLEVR- 224
Cdd:PLN03187 236 VDFTgRGELAERQQKL-AQMLSR-LTKIAEEFN----VAVYMtNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRk 309
|
....*
gi 2326810373 225 -RAEQ 228
Cdd:PLN03187 310 gKGEQ 314
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
45-198 |
2.17e-07 |
|
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: 51.14 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 45 LDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ---QQGGQ---AAFIDAEHAL----------------DPVYA 102
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprELGGLgggAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 103 QKLGVNIEELLLSQPDTGEQAL-EIAEALVRSGAVDIVVVDSVAALVpkaEIEGDMGDSHVGLQARLMSQALRKLSGAIN 181
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF---RSEFDTSRSDLVERAKYLRRLADHLKRLAD 156
|
170
....*....|....*..
gi 2326810373 182 KSKTIAIFINQIREKVG 198
Cdd:cd19491 157 KYNLAVVVVNQVTDRFD 173
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
38-195 |
1.17e-06 |
|
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: 48.78 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALH-AIAEVQQQGGQAAFIDA-EHALDPVY-AQKLGVNIEELL- 113
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 114 --------LSQPDTGEQALEIAEAL----------VRSGAVDIVVVDSVAALvpkAEIEGDMgdshvglQARlmsQALRK 175
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180
....*....|....*....|
gi 2326810373 176 LSGAINKSKTIAIFINQIRE 195
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPS 166
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
8-225 |
1.34e-06 |
|
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: 49.39 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 8 LDMALKQIEKQFGKGSIMKLGEKTDTRISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ---- 83
Cdd:TIGR02238 51 KEAASKIINPGFITAFEISQKRKKVLKITT---GSQALDGILG-GGIESMSITEVFGEFRCGKTQLS-HTLCVTAQlpre 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 84 ---QGGQAAFIDAEHALDP----VYAQKLGVN----IEELLLSQPDTGEQALEIAE---ALVRSGAVDIVVVDSVAALVp 149
Cdd:TIGR02238 126 mggGNGKVAYIDTEGTFRPdrirAIAERFGVDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 150 KAEI--EGDMGDSHVGLqARLMSQaLRKLSGAINksktIAIFI-NQIREKVG--VMF-GNPETTPGGRALKFYSSVRLEV 223
Cdd:TIGR02238 205 RVDFsgRGELSERQQKL-AQMLSR-LNKISEEFN----VAVFVtNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILL 278
|
..
gi 2326810373 224 RR 225
Cdd:TIGR02238 279 RK 280
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
52-227 |
4.58e-06 |
|
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: 46.86 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 52 GGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAA-FID-----------------AEHALDPV-YAQKLGV----N 108
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVlYIDtkssfsarrlaqilksrAQDAEEIDkALQRIRVvrvfD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 109 IEELL--LSQPDTGeqaLEIAEALVRSGaVDIVVVDSVAALVpkAEIEGdmGDSHVGLQARLMSQA--LRKLSgainKSK 184
Cdd:cd19489 82 PYELLdlLEELRNT---LSQQQENLYSR-LKLVIIDSLSALI--SPLLG--GSKHSEGHALLASLArlLKKLA----AEY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2326810373 185 TIAIFINQIREKVGVMFGNPETTPG-GRALKFYSSVRLEVRRAE 227
Cdd:cd19489 150 QIAVLVTNLTVRGGDGGQQGSTKPAlGEYWESVPSTRLLLSRDE 193
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
38-147 |
6.16e-06 |
|
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: 46.49 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQ------KLGVNIEE 111
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNaksfgwDFDEMEDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2326810373 112 LLLSQPD---------TGEQALEIAEALVRSGAVDIVVVDSVAAL 147
Cdd:cd01124 80 GKLIIVDappteagrfSLDELLSRILSIIKSFKAKRVVIDSLSGL 124
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
57-192 |
1.75e-05 |
|
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: 45.42 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 57 GRIIEVYGPESSGKTTVALHAIA---------EVQQQGGQAA--FIDAEHALDP-----VYAQKLGVNIEELLLSQPDTG 120
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 121 EQALeIAEALVR----------------------------SGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQA 172
Cdd:cd19490 81 VEEI-ARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAI 159
|
170 180
....*....|....*....|
gi 2326810373 173 LRKLSGAINKSKTIAIFINQ 192
Cdd:cd19490 160 LRELRRLRRRFQLVVIATKQ 179
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
38-147 |
6.92e-05 |
|
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: 43.47 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVY--AQKLGVNIEELLLS 115
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2326810373 116 Q---------PDTG-EQALEIAEALVRSGAVDIVVVDSVAAL 147
Cdd:cd19484 81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSAL 122
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
33-190 |
7.26e-05 |
|
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: 43.67 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 33 TRISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPV--YAQKLGVNIE 110
Cdd:cd01121 62 ERIST---GIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 111 ELLLsqpdTGEQALEIAEALVRSGAVDIVVVDSVAALVPkAEIEGDMGDShvgLQARLMSQALRKLSgainKSKTIAIFI 190
Cdd:cd01121 138 NLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYS-PELTSSPGSV---SQVRECAAELLRLA----KETGIPVFL 205
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
68-140 |
1.53e-04 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 42.52 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 68 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HALDPV-YAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIVV 140
Cdd:cd17992 77 SGKTVVAALAMLAAVENGYQVALmapteILAEqHYDSLKkLLEPLGIRVA--LLTGSTKAKEKREILEKI-ASGEIDIVI 153
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
23-147 |
2.93e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 42.56 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 23 SIMKLGE-KTDTRIST--VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDP 99
Cdd:PRK09302 237 SVLPLTAmRLTQRSSNerISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQ 315
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 100 VY--AQKLGVNIEEL----LL----SQPD-TG-EQALEIAEALVRSGAVDIVVVDSVAAL 147
Cdd:PRK09302 316 LIrnARSWGIDLEKMeekgLLkiicARPEsYGlEDHLIIIKREIEEFKPSRVAIDPLSAL 375
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
68-140 |
3.38e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 42.34 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 68 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HA--LDPvYAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIV 139
Cdd:COG1200 291 SGKTVVALLAMLAAVEAGYQAALmapteILAEqHYrsLSK-LLEPLGIRVA--LLTGSTKAKERREILAAL-ASGEADIV 366
|
.
gi 2326810373 140 V 140
Cdd:COG1200 367 V 367
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
68-140 |
4.24e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 42.06 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 68 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HA--LDPvYAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIV 139
Cdd:PRK10917 293 SGKTVVAALAALAAIEAGYQAALmapteILAEqHYenLKK-LLEPLGIRVA--LLTGSLKGKERREILEAI-ASGEADIV 368
|
.
gi 2326810373 140 V 140
Cdd:PRK10917 369 I 369
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
62-99 |
5.51e-04 |
|
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: 40.27 E-value: 5.51e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2326810373 62 VYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDP 99
Cdd:cd17929 20 LHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTP 57
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
56-207 |
9.24e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.00 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 56 RGRIIEVYGPESSGKTTVALHAiaevqqqgGQAAFIDAEHALDPVYAQKlGVNIEElLLSQPDTGEQALEIAEALVRSga 135
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDR-FPDIVI-RDSWQDFLDAIDELTAAELAD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 136 VDIVVVDSVAALV-----------PKAEIEGDMGDSHV-GLQARLMSQALRKLSGAInksKTIaIFI-NQIREKVGVMFG 202
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELG---KNV-IFTaHAKTRKDEDPDG 144
|
....*
gi 2326810373 203 NPETT 207
Cdd:pfam13479 145 EKYTR 149
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
55-176 |
1.11e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 40.27 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 55 PRGRIIEVYGPESSGKTTVALHAIAEV---------QQQGGQAAFIDAEHALDPV------YAQKLGVNIEEL-----LL 114
Cdd:COG3598 11 PEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlrLL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2326810373 115 SQPDTGE--QALEIAEALVRSGAVDIVVVDSVAALvpkaeIEGDMGDSHvglQARLMSQALRKL 176
Cdd:COG3598 91 SLAGDLDdtDDLEALERAIEEEGPDLVVIDPLARV-----FGGDENDAE---EMRAFLNPLDRL 146
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
38-145 |
1.66e-03 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 39.20 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326810373 38 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVY--AQKLGVNIEELLls 115
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFerSEALGIDLRAMV-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2326810373 116 qpDTGEQALEIAEAL----------VRSGAVD----IVVVDSVA 145
Cdd:cd19487 78 --EKGLLSIEQIDPAelspgefaqrVRTSVEQedarVVVIDSLN 119
|
|
| |
