|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-229 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 520.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:PRK09354 51 ALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:PRK09354 131 DTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETT 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGISQEGSILDMA 229
Cdd:PRK09354 211 TGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLG 279
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-229 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 513.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:COG0468 54 ALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:COG0468 134 ETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETT 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGISQEGSILDMA 229
Cdd:COG0468 214 TGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLA 282
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-229 |
1.58e-170 |
|
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: 471.85 E-value: 1.58e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:TIGR02012 46 ALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:TIGR02012 126 ETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETT 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGISQEGSILDMA 229
Cdd:TIGR02012 206 TGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFDILYGEGISKLGEIIDLA 274
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
1-221 |
2.45e-165 |
|
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: 455.48 E-value: 2.45e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:cd00983 15 ALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:cd00983 95 DTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIGVMFGNPETT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGISQ 221
Cdd:cd00983 175 TGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-220 |
3.16e-162 |
|
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: 448.39 E-value: 3.16e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:pfam00154 43 ALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:pfam00154 123 DMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETT 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGIS 220
Cdd:pfam00154 203 TGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFDIMYGEGIS 262
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-201 |
2.56e-120 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 360.18 E-value: 2.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIA 80
Cdd:PRK09519 51 ALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 81 DMLIRSGALDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETT 160
Cdd:PRK09519 131 DMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETT 210
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 38455827 161 TGGKALKFYASVRMDIRRIQTLKDKDEPIGNRTRVKVVKNK 201
Cdd:PRK09519 211 TGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
10-178 |
7.46e-58 |
|
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: 181.40 E-value: 7.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 10 GRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYAR-----------HLGVDTDSLIVSQPDNGEQALE 78
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 79 IADMLIRSGA----LDVIVIDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFF 154
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 38455827 155 G-SPETTTGGKALKFYASVRMDIRR 178
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
5-198 |
1.38e-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: 72.45 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEhALDPVYARHLGVD-----TDSLIVSQP---DNGEQA 76
Cdd:TIGR02237 7 GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfdfDEQGVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 77 LEIADMLIRSGALDVIVIDSVAALVpKAEIEGDMGDSHVGLQARLmsQALRKMTgalAQANTTAIFINQLREKIGVFFGS 156
Cdd:TIGR02237 86 IQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLA---RKKNLAVVITNQVYTDVNNGTLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 38455827 157 PettTGGKALKFYASV-----RMDIRRIQTL-KDKDEPIGNRTRVKVV 198
Cdd:TIGR02237 160 P---LGGHLLEHWSKVilrleKFRGRRLATLeKHRSRPEGESVYFRIT 204
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
5-211 |
5.47e-14 |
|
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: 68.11 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEhALDP-----VYARHLGVDTDSLIVSQP-DNGEQALE 78
Cdd:cd01394 14 GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNIIVFEPySFDEQGVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 79 IADM--LIRSGALDVIVIDSVAALVpKAEiegDMGDShvGLQARLMSQaLRKMTGALAQANTTAIFINQLREKIGVFFGS 156
Cdd:cd01394 93 IQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVITNQVYSDIDDDRLK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 38455827 157 PettTGGKALKfYASvrMDIRRIqtlkDKDEPigNRTRVKVVKNKMAPPFKTAEF 211
Cdd:cd01394 166 P---VGGTLLE-HWS--KAIIRL----EKSPP--GLRRATLEKHRSRPEGQSAGF 208
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
5-158 |
3.04e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 63.40 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPV--YARHLGVDTDSLIVS-------------Q 69
Cdd:COG0467 15 GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIESgllriidlspeelG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 70 PDNGEQALEIADMLIRSGAlDVIVIDSVAALVPKAEIEGDmgdshvglqARLMsqaLRKMTGALAQANTTAIFINQLREK 149
Cdd:COG0467 95 LDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKKRGVTTLLTSETGGL 161
|
....*....
gi 38455827 150 IGVFFGSPE 158
Cdd:COG0467 162 EDEATEGGL 170
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
9-179 |
9.01e-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: 58.15 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 9 RGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSqpDNGEQALEIADMLIRSGA 88
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 89 LDVIVIDSVAALVPKaeiegdmgdshVGLQARLMSQALRKMTGALAQANTTAIFINQlrekigvffgsPETTTGGKALKF 168
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRR 136
|
170
....*....|.
gi 38455827 169 YASVRMDIRRI 179
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
13-167 |
1.09e-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: 57.13 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 13 VEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAehaldpvyarhlgvdtdslivsqpdngeqaLEIADMLIRS----GA 88
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF------------------------------LDTILEAIEDlieeKK 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38455827 89 LDVIVIDSVAALVPKAEiegdmgdshvGLQARLMSQALRKMTGALAQANTTAIFINQLREKIGVFFGSPETTTGGKALK 167
Cdd:cd01120 51 LDIIIIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
5-149 |
1.50e-10 |
|
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: 58.81 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHL--------GVDTDSLIVSQPDNGEQA 76
Cdd:cd01124 14 GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNAKsfgwdfdeMEDEGKLIIVDAPPTEAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 77 LE-----IADML--IRSGALDVIVIDSVAALvpKAEIEGDMgdshvglQARlmsQALRKMTGALAQANTTAIFINQLREK 149
Cdd:cd01124 94 RFsldelLSRILsiIKSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRAAGVTTIFTSEMRSF 161
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
1-95 |
7.31e-10 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 56.86 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGIGGLPRGRIVEIYGPE-SSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEI 79
Cdd:COG4544 39 ALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRARRPADALWA 118
|
90
....*....|....*.
gi 38455827 80 ADMLIRSGALDVIVID 95
Cdd:COG4544 119 AEEALRSGACGAVVAW 134
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
5-211 |
8.85e-10 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 56.79 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEhALDPVYARHL-GVDTDSL----IVSQP---DNGEQA 76
Cdd:PRK09361 18 GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELlsniIIFEPssfEEQSEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 77 LEIADMLIRSGAlDVIVIDSVAALVpKAEIEGDMGDShvglqaRLMSQALRKMTGALAQA---NTTAIFINQLREKIGVF 153
Cdd:PRK09361 97 IRKAEKLAKENV-GLIVLDSATSLY-RLELEDEEDNS------KLNRELGRQLTHLLKLArkhDLAVVITNQVYSDIDSD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 38455827 154 FGSPettTGGKALKfYASvrMDIRRIqtlkDKDEPiGNRtRVKVVKNKMAPPFKTAEF 211
Cdd:PRK09361 169 GLRP---LGGHTLE-HWS--KTILRL----EKFRN-GKR-RATLEKHRSRPEGESAEF 214
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
5-179 |
4.62e-09 |
|
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: 54.56 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALH-VVANAQKNGGVAAFIDA-EHALDPVY-ARHLGVDTDSLI--------------- 66
Cdd:pfam06745 14 GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLEeegklaiidastsgi 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 67 ----VSQPDNGEQALEIADMLIRSGALDVIVIDSVAALvpkAEIEGDMgdshvglQARlmsQALRKMTGALAQANTTAIF 142
Cdd:pfam06745 94 giaeVEDRFDLEELIERLREAIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRRLKRVLKGLGVTAIF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 38455827 143 INQLREKigvffgspETTTGGKALKFYAS---VRMDIRRI 179
Cdd:pfam06745 161 TSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEI 192
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
1-180 |
7.72e-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: 53.86 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 1 ALGiGGLPRGRIVEIYGPESSGKTTLALHVVANA-------QKNGGVAaFIDAEHALDP----VYARHLGVDTDSLIVSQ 69
Cdd:cd19493 3 ALA-GGLPLGAITEITGASGSGKTQFALTLASSAamparkgGLDGGVL-YIDTESKFSAerlaEIAEARFPEAFSGFMEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 70 PDNGEQAL---------EIADMLIRSGALDV---------IVIDSVAALVPKA--EIEGDMGDSHVGLqARLMSqALRkm 129
Cdd:cd19493 81 NERAEEMLkrvavvrvtTLAQLLERLPNLEEhilssgvrlVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS-SLK-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 38455827 130 tgALAQA-NTTAIFINQLREKIGVFFGSPETTTGGKALKFYASV--RMDIRRIQ 180
Cdd:cd19493 157 --RLAEEfRIAVLVTNQATTHFGDAGDGSSGVTAALGDAWAHAVntRLRLERCL 208
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
169-229 |
2.05e-08 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 53.94 E-value: 2.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38455827 169 YASVR--MDIRRIQTLKDKDEPIGNRTRVKVVKNKMAPPFKTAEFDMLYGQGISQEGSILDMA 229
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMG 719
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
5-178 |
2.82e-08 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 52.96 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQ----KNG--GVAAFIDAEHALDP----VYARHLGVDTDS----LIVSQP 70
Cdd:PRK04301 97 GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeeKGGleGKAVYIDTEGTFRPerieQMAEALGLDPDEvldnIHVARA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGEQALEIADM---LIRSG-ALDVIVIDSVAALVpKAEiegdmgdsHVGL------QARL---MSQALRkmtgaLAQAN 137
Cdd:PRK04301 177 YNSDHQMLLAEKaeeLIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLnkhLHDLLR-----LADLY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 38455827 138 TTAIFI-NQLREKIGVFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:PRK04301 243 NAAVVVtNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
5-178 |
4.33e-07 |
|
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: 49.07 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQ------KNGGVAAFIDAEHALDPV----YARHLGVDTDSLI----VSQP 70
Cdd:cd01123 14 GGIETGSITEMFGEFRTGKTQLCHTLAVTCQlpidrgGGEGKAIYIDTEGTFRPErlraIAQRFGLDPDDVLdnvaYARA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGEQALEI----ADMLIRSgALDVIVIDSVAALVPKAEI-EGDMGDSHVGLqARLMSQALRkmtgaLAQANTTAIFI-N 144
Cdd:cd01123 94 FNSDHQTQLldqaAAMMVES-RFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLRMLQR-----LADEFGVAVVVtN 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 38455827 145 QLREKIG---VFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:cd01123 167 QVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
5-151 |
4.62e-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: 49.21 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQK-------NGGvAAFIDAEHALdPVyaRHLgvdtDSLIVSQPDNGEQAL 77
Cdd:cd19491 7 GGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelgglGGG-AVYICTESSF-PS--KRL----QQLASSLPKRYHLEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 78 EIADM------------------------LIRSGALDVIVIDSVAALVpkaEIEGDMGDSHVGLQARLMSQALRKMTGAL 133
Cdd:cd19491 79 AKNFLdnifvehvadletlehclnyqlpaLLERGPIRLVVIDSIAALF---RSEFDTSRSDLVERAKYLRRLADHLKRLA 155
|
170
....*....|....*...
gi 38455827 134 AQANTTAIFINQLREKIG 151
Cdd:cd19491 156 DKYNLAVVVVNQVTDRFD 173
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
5-178 |
5.26e-07 |
|
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: 48.90 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKN------GGVAAFIDAEHALDP----VYARHLGVDTDSL----IVSQP 70
Cdd:cd19515 14 GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPpeegglNGKAVYIDTENTFRPerimQMAKALGLDPDEVldniYVARA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGE-QAL---EIADMLIRSGALDVIVIDSVAALVpKAEI--EGDMGDSHVGLqARLMSQALRkmtgaLAQANTTAIFI- 143
Cdd:cd19515 94 YNSNhQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR-----LADLYNIAVLVt 166
|
170 180 190
....*....|....*....|....*....|....*
gi 38455827 144 NQLREKIGVFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:cd19515 167 NQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
5-178 |
5.68e-06 |
|
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: 45.76 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKT----TLALHVVANAQKNG--GVAAFIDAEHALDPV----YARHLGVDTDSLIVSQP---- 70
Cdd:pfam08423 32 GGIETGSITEIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFRPErlvaIAERYGLDPEDVLDNVAyara 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 ---DNGEQALEIADMLIRSGALDVIVIDSVAALVpKAEIEGdMGDshvgLQARLM--SQALRKMTgALAQANTTAIFI-N 144
Cdd:pfam08423 112 ynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSG-RGE----LAERQQhlAKFLRTLQ-RLADEFGVAVVItN 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 38455827 145 QLREKIG----VFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:pfam08423 185 QVVAQVDgaagMFSGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
10-53 |
1.13e-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: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 38455827 10 GRIVEIYGPESSGKTTLALHVVANA---QKNGGVAA--------FIDAEHALDPV 53
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpSSWGGVPLggleaavvFIDTDGRFDIL 55
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
5-45 |
5.83e-05 |
|
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: 42.62 E-value: 5.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAA-FID 45
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVlYID 43
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
9-97 |
6.33e-05 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 42.31 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 9 RGRIVEIYGPESSGKTTLAlhvvANAQKnggvAAFIDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIADMlirsGA 88
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFA----KTLPK----PLFLDTEKGSKALDGDRFPDIVIRDSWQDFLDAIDELTAAEL----AD 68
|
....*....
gi 38455827 89 LDVIVIDSV 97
Cdd:pfam13479 69 YKTIVIDTV 77
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
10-151 |
1.02e-04 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 41.44 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 10 GRIVEIYGPESSGKTTLALHVVANAQKN---GGV---AAFIDAEHALDPVYAR-HLGVDTDSLIVSQPDNGEQALEIAdm 82
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIPkcfGGLageAIYIDTEGSFNIHYFRvHDYVELLALINSLPKFLEDHPKVK-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38455827 83 lirsgaldVIVIDSVAALvpkaeIEGDMGDShvGLQARLMSQALRKMTGALAQANTTAIFINQLREKIG 151
Cdd:cd19492 79 --------LIVVDSIAFP-----FRHDFDDL--AQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
7-206 |
1.43e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 41.81 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 7 LPRGRIVEIYGPESSGKTTLALHV---VANAQK------NGGVAAFIDAEHALDPV------YARHLGVDTDSL-----I 66
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLaaaVAAGGPwlgrrvPPGKVLYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 67 VSQPDNGEQALEIADM--LIRSGALDVIVIDSVAALvpkaeIEGDMGDSHvglQARLMSQALRKMTGALaqaNTTAIFIN 144
Cdd:COG3598 90 LSLAGDLDDTDDLEALerAIEEEGPDLVVIDPLARV-----FGGDENDAE---EMRAFLNPLDRLAERT---GAAVLLVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38455827 145 QLReKIGVFFGSPETTTGGKAlkFYASVRMdirRIQTLKDKDEpigNRTRVKVVKNKMAPPF 206
Cdd:COG3598 159 HTG-KGGAGKDSGDRARGSSA--LRGAARS---VLVLSREKGE---DLRVLTRAKSNYGPEI 211
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
2-178 |
1.83e-04 |
|
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: 41.19 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 2 LGiGGLPRGRIVEIYGPESSGKTTLA--LHVVANAQKN----GGVAAFIDAEHALDP----VYARHLGVDT----DSLIV 67
Cdd:cd19514 12 LG-GGIESMSITEVFGEFRTGKTQLShtLCVTAQLPGSmgggGGKVAYIDTEGTFRPdrirPIAERFGVDHdavlDNILY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 68 SQPDNGEQALEIADML----IRSGALDVIVIDSVAALVpKAEI--EGDMGDShvglQARLmSQALRKMTgALAQANTTAI 141
Cdd:cd19514 91 ARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ-KISEEYNVAV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 38455827 142 FI-NQLREKIG---VFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:cd19514 164 FItNQVTADPGaamTFQADPKKPIGGHILAHASTTRISLRK 204
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
5-178 |
2.36e-04 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 41.30 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQ----KNGGVA--AFIDAEHALDP----VYARHLGVDT----DSLIVSQP 70
Cdd:PLN03187 121 GGIETRCITEAFGEFRSGKTQLAHTLCVTTQlpteMGGGNGkvAYIDTEGTFRPdrivPIAERFGMDAdavlDNIIYARA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGEQaleIADMLIRSGAL------DVIVIDSVAALVPKAEI-EGDMGDShvglQARLmSQALRKMTGALAQANTTAIFI 143
Cdd:PLN03187 201 YTYEH---QYNLLLGLAAKmaeepfRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSRLTKIAEEFNVAVYMT 272
|
170 180 190
....*....|....*....|....*....|....*..
gi 38455827 144 NQLREKIG--VFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:PLN03187 273 NQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
5-178 |
5.95e-04 |
|
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: 40.15 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLA--LHVVANAQKNGGVA----AFIDAEHALDP----VYARHLGVDTDS----LIVSQP 70
Cdd:TIGR02238 91 GGIESMSITEVFGEFRCGKTQLShtLCVTAQLPREMGGGngkvAYIDTEGTFRPdrirAIAERFGVDPDAvldnILYARA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGEQALEIADML---IRSGALDVIVIDSVAALvpkaeIEGDM-GDSHVGLQARLMSQALRKMTGALAQANTTAIFINQL 146
Cdd:TIGR02238 171 YTSEHQMELLDYLaakFSEEPFRLLIVDSIMAL-----FRVDFsGRGELSERQQKLAQMLSRLNKISEEFNVAVFVTNQV 245
|
170 180 190
....*....|....*....|....*....|....*
gi 38455827 147 REKIG---VFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:TIGR02238 246 QADPGatmTFIADPKKPIGGHVLAHASTTRILLRK 280
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
5-146 |
6.55e-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: 39.64 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTLALHVVANAQKNGGVAAFI---DAEHALDPVYARHlGVDTDSLIV---SQPDNGEQALE 78
Cdd:cd19488 14 GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAVALSH-GWSLDGIHIfelSPSESALDAAQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 79 IADML---------IRSGALDVI--------VIDSVaalvpkAEIEGDMGDShvgLQARLMSQALRKMtgaLAQANTTAI 141
Cdd:cd19488 93 QYTILhpselelseTTRLIFERVerlkpsrvVIDSL------SELRLLAQDS---LRYRRQILALKQF---FAGRNTTVL 160
|
....*
gi 38455827 142 FINQL 146
Cdd:cd19488 161 LLDDL 165
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
12-101 |
7.43e-04 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 39.61 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 12 IVEIYGPESSGKTTLALHVVANAQKNGGVAAFIDAEHALDPVY----------ARHLGVDTDSLIVSQPDNGEQALEIAD 81
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKldrfeevrrlAEALGIAVPKAELEESKLAFLAIELLL 101
|
90 100
....*....|....*....|.
gi 38455827 82 MLI-RSGALDVIVIDSVAALV 101
Cdd:pfam01637 102 EALkRRGKKIAIIIDEVQQAI 122
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
17-215 |
7.83e-04 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 39.48 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 17 GPESSGKTT----LALHVVANAQKNGGVAAF-IDAEHALDPVYARHLGVDTDSLIVSQPDNGEQALEIADMLIRSGAL-- 89
Cdd:cd19483 5 AGSGIGKSTivreLAYHLITEHGEKVGIISLeESVEETAKGLAGKHLGKPEPLELPRDDITEEEEDDAFDNELGSGRFfl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 90 -------------------------DVIVIDSVAALVpkaeiEGDMGDSHVGLQARLMSQaLRKMTgalAQANTTAIFIN 144
Cdd:cd19483 85 ydhfgsldwdnlkekirymvkvlgcKVIVLDHLTILV-----SGLDSSDERKELDEIMTE-LAALV---KELGVTIILVS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38455827 145 QLREKIGV----FFGSPETT--TGGKALKFYASVRMDIRRIQTLKDKDEPigNRTRVKVVKNKMAPpfKTAEFDMLY 215
Cdd:cd19483 156 HLRRPGGGkgheEGGEVSESdlRGSSAIAQLSDYVIGLERNKQADDPVER--NTTRVRVLKNRFTG--ETGIAGTLY 228
|
|
| PRK04296 |
PRK04296 |
thymidine kinase; Provisional |
10-95 |
1.47e-03 |
|
thymidine kinase; Provisional
Pssm-ID: 235272 Cd Length: 190 Bit Score: 38.17 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 10 GRIVEIYGPESSGKTTLALHVVANAQKNG-GVAAF---IDAEHALDPVyARHLGVDTDSLIVSQPDNGEQALEiadmlIR 85
Cdd:PRK04296 2 AKLEFIYGAMNSGKSTELLQRAYNYEERGmKVLVFkpaIDDRYGEGKV-VSRIGLSREAIPVSSDTDIFELIE-----EE 75
|
90
....*....|
gi 38455827 86 SGALDVIVID 95
Cdd:PRK04296 76 GEKIDCVLID 85
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
7-102 |
1.74e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 38.13 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 7 LPRGRIVEIYGPESSGKTTLALHVVA------------NAQKNGGVaAFIDAE--------------HALDPVYARHLGV 60
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpwlggpRVPEQGKV-LYVSAEgpadelrrrlraagADLDLPARLLFLS 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 38455827 61 DTDSLIVSQPDNGEQAL-----EIADMLIRSGALDVIVIDSVAALVP 102
Cdd:pfam13481 109 LVESLPLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG 155
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
5-178 |
2.51e-03 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 38.17 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 5 GGLPRGRIVEIYGPESSGKTTL--ALHV---VANAQKNG-GVAAFIDAEHALDP----VYARHLGVDTDSLI----VSQP 70
Cdd:PLN03186 118 GGIETGSITEIYGEFRTGKTQLchTLCVtcqLPLDQGGGeGKAMYIDTEGTFRPqrliQIAERFGLNGADVLenvaYARA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 71 DNGEQALEI----ADMLIRSgALDVIVIDSVAALVpKAEIEGdMGDshvgLQAR--LMSQALRKMTgALAQANTTAIFI- 143
Cdd:PLN03186 198 YNTDHQSELlleaASMMAET-RFALMIVDSATALY-RTEFSG-RGE----LSARqmHLGKFLRSLQ-RLADEFGVAVVIt 269
|
170 180 190
....*....|....*....|....*....|....*...
gi 38455827 144 NQLREKI---GVFFGSPETTTGGKALKFYASVRMDIRR 178
Cdd:PLN03186 270 NQVVAQVdgsAFFAGPQLKPIGGNIMAHASTTRLALRK 307
|
|
| Tdk |
COG1435 |
Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the ... |
10-95 |
3.02e-03 |
|
Thymidine kinase [Nucleotide transport and metabolism]; Thymidine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 441044 Cd Length: 192 Bit Score: 37.39 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38455827 10 GRIVEIYGPESSGKTTLALHVVANAQKNG-GVAAFIdaeHALDPVYAR-----HLGVDTDSLIVSQPDngeqalEIADML 83
Cdd:COG1435 4 GKLEFIYGPMFSGKSEELLRRAHNYEEAGqKVLLFK---PAIDDRYGEgkivsRIGLSREAIPVDDDT------DILELV 74
|
90
....*....|..
gi 38455827 84 IRSGALDVIVID 95
Cdd:COG1435 75 REGPDVDVVLID 86
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
11-27 |
5.33e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 36.72 E-value: 5.33e-03
|
| |
