|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
4-341 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 689.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 4 QAPDREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVA 83
Cdd:PRK09354 3 MDEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 84 NAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGD 163
Cdd:PRK09354 83 EAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 164 SHVGLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAVGNR 243
Cdd:PRK09354 163 SHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 244 TRVKVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEGEQLGQGKENARKFLLENTDVANEIEK 323
Cdd:PRK09354 243 TKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEK 322
|
330
....*....|....*...
gi 217035322 324 KIKEKLGIGAVVTAEADD 341
Cdd:PRK09354 323 KIREKLGLSAAAAEEEEE 340
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-348 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 682.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 1 MAQ--QAPDREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVA 78
Cdd:COG0468 1 MAKkvASSEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 79 LHAVANAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIE 158
Cdd:COG0468 81 LHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 159 GEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTD 238
Cdd:COG0468 161 GEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 239 AVGNRTRVKVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEGEQLGQGKENARKFLLENTDVA 318
Cdd:COG0468 241 VIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELA 320
|
330 340 350
....*....|....*....|....*....|
gi 217035322 319 NEIEKKIKEKLGIGAVVTAEADDVLPAPVD 348
Cdd:COG0468 321 EEIEAKIREKLGLGAVSEAAAAEEEEDEEE 350
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
7-327 |
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: 617.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 7 DREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQ 86
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 87 AAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHV 166
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 167 GLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAVGNRTRV 246
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 247 KVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEGEQLGQGKENARKFLLENTDVANEIEKKIK 326
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVR 320
|
.
gi 217035322 327 E 327
Cdd:TIGR02012 321 E 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
10-271 |
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: 515.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 10 KALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAG 89
Cdd:pfam00154 1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 90 GIAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQ 169
Cdd:pfam00154 81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 170 ARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAVGNRTRVKVV 249
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVV 240
|
250 260
....*....|....*....|..
gi 217035322 250 KNKVSPPFKQAEFDILYGQGIS 271
Cdd:pfam00154 241 KNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
39-272 |
5.11e-173 |
|
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: 479.74 E-value: 5.11e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 39 ISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLV 118
Cdd:cd00983 2 VEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 119 SQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINNLR 198
Cdd:cd00983 82 SQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 217035322 199 EKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAVGNRTRVKVVKNKVSPPFKQAEFDILYGQGISR 272
Cdd:cd00983 162 EKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
4-252 |
2.80e-165 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 480.74 E-value: 2.80e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 4 QAPDREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVA 83
Cdd:PRK09519 3 QTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 84 NAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGD 163
Cdd:PRK09519 83 NAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 164 SHVGLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAVGNR 243
Cdd:PRK09519 163 SHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNR 242
|
....*....
gi 217035322 244 TRVKVVKNK 252
Cdd:PRK09519 243 TRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
61-229 |
5.36e-56 |
|
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: 180.63 E-value: 5.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 61 GRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYA-----------KKLGVDTDSLLVSQPDTGEQALE 129
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 130 IADMLVRSGA----LDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMF 205
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 217035322 206 G-SPETTTGGKALKFYASVRLDVRR 229
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
220-349 |
2.45e-50 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 179.52 E-value: 2.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 220 YASVR--LDVRRIETLKDGTDAVGNRTRVKVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEG 297
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 217035322 298 EQLGQGKENARKFLLENTDVANEIEKKIKEKLGIGAVVTAEA--DDVLPAPVDF 349
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAVVTDDPsnDGVLPAPVDF 790
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
42-264 |
2.61e-16 |
|
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: 76.58 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEhALDPEYAKKL-----GVDTDSL 116
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPERFQQIagerfESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 117 LVSQP-DTGEQALEIADM--LVRSGALDIIVIDSVAALVpRAEiegEMGDShvGLQARLMSQaLRKMTGALNNSGTTAIF 193
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 217035322 194 INNLREKIGVMFGSPettTGGKALKFYASVRLdvrRIETLKDGtdavgnRTRVKVVKNKVSPPFKQAEFDI 264
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLEHWSKAII---RLEKSPPG------LRRATLEKHRSRPEGQSAGFRI 210
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
30-140 |
6.33e-14 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 70.34 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 30 RLGEEVRQPISVIPTGSISLDVALGIGGLPRGRVIEIYGPE-SSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAKK 108
Cdd:COG4544 17 RGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAA 96
|
90 100 110
....*....|....*....|....*....|..
gi 217035322 109 LGVDTDSLLVSQPDTGEQALEIADMLVRSGAL 140
Cdd:COG4544 97 AGLDPERLLLVRARRPADALWAAEEALRSGAC 128
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
49-233 |
1.09e-13 |
|
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).
Pssm-ID: 274047 [Multi-domain] Cd Length: 209 Bit Score: 68.98 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 49 LDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEhALDPEYAKKLGVD-----TDSLLVSQP-- 121
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 122 -DTGEQALEIADMLVRSGALDIIVIDSVAALVpRAEIEGEMGDSHVGL--QARLMSQALRKMTGAlnnsgttAIFINNLR 198
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELarQLTLLLSLARKKNLA-------VVITNQVY 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 217035322 199 EKIGVMFGSPettTGGKALKFYASV-----RLDVRRIETL 233
Cdd:TIGR02237 151 TDVNNGTLRP---LGGHLLEHWSKVilrleKFRGRRLATL 187
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
39-160 |
1.83e-13 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 68.74 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 39 ISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEhALDPEYAKKL-GVDTDSLL 117
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 217035322 118 ----VSQP-DTGEQALEIADM--LVRSGAlDIIVIDSVAALVpRAEIEGE 160
Cdd:PRK09361 80 sniiIFEPsSFEEQSEAIRKAekLAKENV-GLIVLDSATSLY-RLELEDE 127
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
42-209 |
4.01e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 64.94 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDP--EYAKKLGVDTDSLLVS 119
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 120 -------------QPDTGEQALEIADMLVRSGAlDIIVIDSVAALVPRAEIEGEmgdshvglqARLMsqaLRKMTGALNN 186
Cdd:COG0467 81 gllriidlspeelGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 217035322 187 SGTTAIFINNLREKIGVMFGSPE 209
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
64-218 |
3.72e-10 |
|
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: 56.74 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 64 IEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAehaldpeyakklgvdtdsllvsqpdtgeqaLEIADMLVRS----GA 139
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF------------------------------LDTILEAIEDlieeKK 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217035322 140 LDIIVIDSVAALVPRAEiegemgdshvGLQARLMSQALRKMTGALNNSGTTAIFINNLREKIGVMFGSPETTTGGKALK 218
Cdd:cd01120 51 LDIIIIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
42-229 |
1.34e-09 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 57.54 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ------AAGGIAAFIDAEHALDPE----YAKKLGV 111
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLCHTLAVTCQlpidrgGGEGKAIYIDTEGTFRPErlraIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 112 DTDSLL----VSQPDTGEQALEI----ADMLVRSgALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQALRkmt 181
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLldqaAAMMVES-RFKLLIVDSATALY-RTDYsgRGELSARQMHL-AKFLRMLQR--- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 217035322 182 gaLNNSGTTAIFINN---LREKIGVMF-GSPETTTGGKALKFYASVRLDVRR 229
Cdd:cd01123 154 --LADEFGVAVVVTNqvvAQVDGAMMFaADPKKPIGGNILAHASTTRLYLRK 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
60-231 |
1.71e-09 |
|
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: 55.84 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 60 RGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSqpDTGEQALEIADMLVRSGA 139
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 140 LDIIVIDSVAALVPRaeiegemgdshVGLQARLMSQALRKMTGALNNSGTTAIFINNlrekigvmfgsPETTTGGKALKF 219
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRR 136
|
170
....*....|..
gi 217035322 220 YASVRLDVRRIE 231
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
42-200 |
2.32e-09 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDP--EYAKKLGVDTDSL--- 116
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERllRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 117 ----LVSQPDTGEQALEIADML------VRSGALDIIVIDSVAALvpRAEIEGEMgdshvglQARlmsQALRKMTGALNN 186
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDELLsrilsiIKSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRA 147
|
170
....*....|....
gi 217035322 187 SGTTAIFINNLREK 200
Cdd:cd01124 148 AGVTTIFTSEMRSF 161
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
50-163 |
3.54e-09 |
|
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: 56.17 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 50 DVALGiGGLPRGRVIEIYGPESSGKTTVALHAVA----NAQAAGGIAA--FIDAEHALDPE---------YAKKLGVDTD 114
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASsaamPARKGGLDGGvlYIDTESKFSAErlaeiaearFPEAFSGFME 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217035322 115 S----------LLVSQPDTGEQALEIADML---VRSGALDIIVIDSVAALVpRAEIEGEMGD 163
Cdd:cd19493 80 EneraeemlkrVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALV-RREFGGSDGE 140
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
9-196 |
4.95e-09 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 57.05 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 9 EKALELAMAQIDKNFGKGSVMrlgEEVRQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKT----TVALHA-VA 83
Cdd:PLN03186 75 EKILEAASKLVPLGFTTASQL---HAQRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCqLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 84 NAQAAG-GIAAFIDAEHALDPE----YAKKLGVDTDSLL-----VSQPDTGEQA---LEIADMLVRSgALDIIVIDSVAA 150
Cdd:PLN03186 151 LDQGGGeGKAMYIDTEGTFRPQrliqIAERFGLNGADVLenvayARAYNTDHQSellLEAASMMAET-RFALMIVDSATA 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 217035322 151 LVpRAEIEGEmGDshvgLQAR--LMSQALRKMTGALNNSGtTAIFINN 196
Cdd:PLN03186 230 LY-RTEFSGR-GE----LSARqmHLGKFLRSLQRLADEFG-VAVVITN 270
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
42-229 |
6.75e-09 |
|
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: 55.45 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ------AAGGIAAFIDAEHALDPE----YAKKLGV 111
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQlppeegGLNGKAVYIDTENTFRPErimqMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 112 DTDSLL----VSQP-DTGEQAL---EIADMLVRSGALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQALRkmt 181
Cdd:cd19515 80 DPDEVLdniyVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR--- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 217035322 182 gaLNNSGTTAIFI-NNLREKIGVMFGSPETTTGGKALKFYASVRLDVRR 229
Cdd:cd19515 155 --LADLYNIAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
36-229 |
1.48e-08 |
|
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: 55.00 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 36 RQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVAlHAVA-NAQ------AAGGIAAFIDAEHALDPE---- 104
Cdd:pfam08423 13 RSELIQITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLC-HTLCvTCQlplemgGGEGKALYIDTEGTFRPErlva 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 105 YAKKLGVDTDSLLVSQP-------DTGEQALEIADMLVRSGALDIIVIDSVAALVpRAEIE--GEMGDSHVGLqARLMSq 175
Cdd:pfam08423 91 IAERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 217035322 176 ALRKMTGALNnsgtTAIFINNL----REKIGVMF-GSPETTTGGKALKFYASVRLDVRR 229
Cdd:pfam08423 168 TLQRLADEFG----VAVVITNQvvaqVDGAAGMFsGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
32-229 |
1.77e-08 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 55.27 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 32 GEEV---RQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ------AAGGIAAFIDAEHALD 102
Cdd:PRK04301 71 ALEVlerRKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeekgGLEGKAVYIDTEGTFR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 103 PE----YAKKLGVDTDSLL----VSQP-DTGEQAL--EIADMLVRSG-ALDIIVIDSVAALVpRAEiegemgdsHVGL-- 168
Cdd:PRK04301 150 PErieqMAEALGLDPDEVLdnihVARAyNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgn 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217035322 169 ----QARL---MSQALRkmTGALNNsgtTAIFI-NNLREKIGVMFGSPETTTGGKALKFYASVRLDVRR 229
Cdd:PRK04301 221 laerQQKLnkhLHDLLR--LADLYN---AAVVVtNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
9-229 |
2.00e-08 |
|
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: 54.78 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 9 EKALELAMAQIDKNFGKGSVMrlgEEVRQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ-- 86
Cdd:TIGR02238 48 DKIKEAASKIINPGFITAFEI---SQKRKKVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLSHTLCVTAQlp 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 87 ----AAGGIAAFIDAEHALDPE----YAKKLGVDTDS----LLVSQPDTGEQALEIADML---VRSGALDIIVIDSVAAL 151
Cdd:TIGR02238 124 remgGGNGKVAYIDTEGTFRPDriraIAERFGVDPDAvldnILYARAYTSEHQMELLDYLaakFSEEPFRLLIVDSIMAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 152 VpRAEI--EGEMGDSHVGLqARLMSQaLRKMTGALNnsgtTAIFINNLREK---IGVMFGS-PETTTGGKALKFYASVRL 225
Cdd:TIGR02238 204 F-RVDFsgRGELSERQQKL-AQMLSR-LNKISEEFN----VAVFVTNQVQAdpgATMTFIAdPKKPIGGHVLAHASTTRI 276
|
....
gi 217035322 226 DVRR 229
Cdd:TIGR02238 277 LLRK 280
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
42-229 |
2.89e-08 |
|
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: 53.90 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVAlHAVA-NAQ------AAGGIAAFIDAEHALDPE----YAKKLG 110
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLCvTAQlpgsmgGGGGKVAYIDTEGTFRPDrirpIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 111 VDT----DSLLVSQPDTGEQALEIADML----VRSGALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQaLRKM 180
Cdd:cd19514 79 VDHdavlDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 217035322 181 TGALNnsgtTAIFINNLREK---IGVMFGS-PETTTGGKALKFYASVRLDVRR 229
Cdd:cd19514 156 SEEYN----VAVFITNQVTAdpgAAMTFQAdPKKPIGGHILAHASTTRISLRK 204
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
36-229 |
6.19e-08 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 53.63 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 36 RQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVAlHAVA-------NAQAAGGIAAFIDAEHALDPE---- 104
Cdd:PLN03187 102 RKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlptEMGGGNGKVAYIDTEGTFRPDrivp 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 105 YAKKLGVDTDSLL----VSQPDTGEQaleIADMLVRSGAL------DIIVIDSVAALVpRAEI--EGEMGDSHVGLqARL 172
Cdd:PLN03187 180 IAERFGMDADAVLdniiYARAYTYEH---QYNLLLGLAAKmaeepfRLLIVDSVIALF-RVDFtgRGELAERQQKL-AQM 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 173 MSQaLRKMTGALNnsgtTAIFINN--LREKIGVMFGS-PETTTGGKALKFYASVRLDVRR 229
Cdd:PLN03187 255 LSR-LTKIAEEFN----VAVYMTNqvIADPGGGMFISdPKKPAGGHVLAHAATIRLMLRK 309
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
42-231 |
1.23e-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: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDvALGIGGLPRGRVIEIYGPESSGKTTVALH-AVANAQAAGGIAAFIDA-EHALD-PEYAKKLGVDTDSL-- 116
Cdd:pfam06745 1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLEKLee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 117 --------LVSQPDTGEQALEIADM---------LVRSGALDIIVIDSVAALvprAEIEGEMgdshvglQARlmsQALRK 179
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreAIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 217035322 180 MTGALNNSGTTAIFINNLREKigvmfgspETTTGGKALKFYAS---VRLDVRRIE 231
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIE 193
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
34-229 |
9.83e-06 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 46.91 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 34 EVRQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ------AAGGIAAFIDAEHALDPE--- 104
Cdd:PTZ00035 92 EARKNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLCHTLCVTCQlpieqgGGEGKVLYIDTEGTFRPEriv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 105 -YAKKLGVDT----DSLLVSQPDTGEQALEiadMLVRSGAL------DIIVIDSVAALVpRAEIEGEmGDshvgLQARlm 173
Cdd:PTZ00035 171 qIAERFGLDPedvlDNIAYARAYNHEHQMQ---LLSQAAAKmaeerfALLIVDSATALF-RVDYSGR-GE----LAER-- 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217035322 174 SQALRKMTGALNNSGTT---AIFINN---LREKIGVMFGS-PETTTGGKALKFYASVRLDVRR 229
Cdd:PTZ00035 240 QQHLGKFLRALQKLADEfnvAVVITNqvmADVDGASMFVAdPKKPIGGHIIAHASTTRLSLRK 302
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
49-195 |
1.25e-05 |
|
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: 46.13 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 49 LDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQ---AAGGI---AAFIDAEHAL----------------DPEYA 106
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprELGGLgggAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 107 KKLGVDTDSLLVSQPDTGEQAL-EIADMLVRSGALDIIVIDSVAALVpRAEIEGEMGDShvGLQARLMSQALRKMTGALN 185
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSDL--VERAKYLRRLADHLKRLAD 156
|
170
....*....|
gi 217035322 186 NSGTTAIFIN 195
Cdd:cd19491 157 KYNLAVVVVN 166
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
61-104 |
2.46e-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: 45.03 E-value: 2.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 217035322 61 GRVIEIYGPESSGKTTVALHAVANA---QAAGGIAA--------FIDAEHALDPE 104
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpSSWGGVPLggleaavvFIDTDGRFDIL 55
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
58-347 |
7.64e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 44.12 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 58 LPRGRVIEIYGPESSGKTTVALH---AVAN------AQAAGGIAAFIDAE----------HALDPEYAKKLGVDTDSLLV 118
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAggpwlgRRVPPGKVLYLAAEddrgelrrrlKALGADLGLPFADLDGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 119 SQPDTGEQALEIADML---VRSGALDIIVIDSVAALVPraeiegemGDSHVGLQARLMSQALRKMTGALnnsGTTAIFIN 195
Cdd:COG3598 90 LSLAGDLDDTDDLEALeraIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLAERT---GAAVLLVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 196 NLReKIGVMFGSPETTTGGKALKFYASVRLDVRRIETlkdgtdavGNRTRVKVVKNKVSPPFkqaEFDILYGQGISREGS 275
Cdd:COG3598 159 HTG-KGGAGKDSGDRARGSSALRGAARSVLVLSREKG--------EDLRVLTRAKSNYGPEI---ALRWDNGGRLALEEV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217035322 276 LIDMGVEHGFIRKSGSWFT-YEGEQLGQGKENARKFLLENTDVANEIEKKIKEKLGIGAVVTAEADDVLPAPV 347
Cdd:COG3598 227 AALTAGAGEVELKELVGGVaRTGTDSELEEGLLEVPLAEAESAGEDAELAAKAVADEKDAARAVARLKAGGGK 299
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
42-229 |
1.46e-04 |
|
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: 42.69 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVAlHAVA-NAQ------AAGGIAAFIDAEHALDPE----YAKKLG 110
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLC-HTLAvTCQlpidqgGGEGKALYIDTEGTFRPErllaIAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 111 VDTDSLL----VSQPDTGEQALEiadMLVRSGAL------DIIVIDSVAALVpRAEIEGEmGDshvgLQARLM--SQALR 178
Cdd:cd19513 79 LNGEDVLdnvaYARAYNTDHQMQ---LLIQASAMmaesryALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 217035322 179 KMTGALNNSGTTAIFINNLREKI--GVMF-GSPETTTGGKALKFYASVRLDVRR 229
Cdd:cd19513 150 MLQRLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
34-229 |
1.52e-04 |
|
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: 43.17 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 34 EVRQPISVIPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVAlHAVA------NAQAAG-GIAAFIDAEHALDPE-- 104
Cdd:TIGR02239 70 QRRQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLC-HTLAvtcqlpIDQGGGeGKALYIDTEGTFRPErl 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 105 --YAKKLGVDTDSLL--VS-----QPDTGEQALEIADMLVRSGALDIIVIDSVAALVpRAEIEGEmGDshvgLQARLMSQ 175
Cdd:TIGR02239 148 laIAERYGLNPEDVLdnVAyarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHL 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 176 A--LRKMTGALNNSGTTAIFINNLREKI---GVMF-GSPETTTGGKALKFYASVRLDVRR 229
Cdd:TIGR02239 222 ArfLRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
56-152 |
4.87e-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: 40.70 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 56 GGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAA-FIDAEHALDPE-------YAKKLGVDTDSLL-------VSQ 120
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVlYIDTKSSFSARrlaqilkSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 217035322 121 PDTGEQAL-EIADML-----VRSGALDIIVIDSVAALV 152
Cdd:cd19489 82 PYELLDLLeELRNTLsqqqeNLYSRLKLVIIDSLSALI 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
42-95 |
5.19e-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: 40.80 E-value: 5.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 217035322 42 IPTGSISLDVALGiGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFI 95
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
60-148 |
1.43e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 39.23 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 60 RGRVIEIYGPESSGKTTVALHAvanaqaagGIAAFIDAEHALDPEYAKKLGVDTDSLlvSQPDTGEQALEIADMLVRSga 139
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPDIVIRD--SWQDFLDAIDELTAAELAD-- 68
|
....*....
gi 217035322 140 LDIIVIDSV 148
Cdd:pfam13479 69 YKTIVIDTV 77
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
63-152 |
4.03e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 38.07 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217035322 63 VIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEY----------AKKLGVDTDSLLVSQPDTGEQALEIAD 132
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKldrfeevrrlAEALGIAVPKAELEESKLAFLAIELLL 101
|
90 100
....*....|....*....|.
gi 217035322 133 MLV-RSGALDIIVIDSVAALV 152
Cdd:pfam01637 102 EALkRRGKKIAIIIDEVQQAI 122
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
42-89 |
9.93e-03 |
|
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: 36.92 E-value: 9.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 217035322 42 IPTGSISLDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAG 89
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRG 48
|
|
| |
