|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-183 |
3.50e-150 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 419.20 E-value: 3.50e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNEL 80
Cdd:PRK09354 36 MDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQ 160
Cdd:PRK09354 116 LVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQ 195
|
170 180
....*....|....*....|...
gi 1104677240 161 IRMKIGVMFGNPETTTGGNALKF 183
Cdd:PRK09354 196 IREKIGVMFGNPETTTGGNALKF 218
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-183 |
2.04e-145 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 407.25 E-value: 2.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNEL 80
Cdd:COG0468 39 QDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQ 160
Cdd:COG0468 119 LVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQ 198
|
170 180
....*....|....*....|...
gi 1104677240 161 IRMKIGVMFGNPETTTGGNALKF 183
Cdd:COG0468 199 LREKIGVMFGNPETTTGGNALKF 221
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
2-183 |
1.34e-132 |
|
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: 370.35 E-value: 1.34e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 2 DIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNELL 81
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 82 VSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 161
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180
....*....|....*....|..
gi 1104677240 162 RMKIGVMFGNPETTTGGNALKF 183
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKF 182
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-183 |
1.69e-132 |
|
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: 371.35 E-value: 1.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNEL 80
Cdd:pfam00154 28 LDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQ 160
Cdd:pfam00154 108 LVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQ 187
|
170 180
....*....|....*....|...
gi 1104677240 161 IRMKIGVMFGNPETTTGGNALKF 183
Cdd:pfam00154 188 IREKIGVMFGNPETTTGGRALKF 210
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-183 |
7.27e-131 |
|
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: 369.39 E-value: 7.27e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNEL 80
Cdd:TIGR02012 31 MDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQ 160
Cdd:TIGR02012 111 LVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQ 190
|
170 180
....*....|....*....|...
gi 1104677240 161 IRMKIGVMFGNPETTTGGNALKF 183
Cdd:TIGR02012 191 IREKIGVMFGNPETTTGGNALKF 213
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-183 |
5.21e-90 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 279.29 E-value: 5.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNEL 80
Cdd:PRK09519 36 QPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQ 160
Cdd:PRK09519 116 LVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQ 195
|
170 180
....*....|....*....|...
gi 1104677240 161 IRMKIGVMFGNPETTTGGNALKF 183
Cdd:PRK09519 196 LRDKIGVMFGSPETTTGGKALKF 218
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
25-183 |
4.39e-48 |
|
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: 154.43 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 25 GRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYA-----------GKLGVNVNELLVSQPDTGEQALE 93
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 94 IADALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 169
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170
....*....|....*
gi 1104677240 170 G-NPETTTGGNALKF 183
Cdd:cd01393 161 GaSLVPPALGNTWEH 175
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
6-166 |
1.37e-20 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 84.67 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEhALDI----QYAG-KLGVNVNEL 80
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqQIAGeRFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 LVSQP-DTGEQALEIADA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIF 157
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151
|
....*....
gi 1104677240 158 INQIRMKIG 166
Cdd:cd01394 152 TNQVYSDID 160
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
3-166 |
3.26e-15 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 70.66 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 3 IQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEhALDI----QYAGKlgvNVN 78
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPerfkQIAGE---DFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 79 ELL----VSQP-DTGEQALEIADA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRT 151
Cdd:PRK09361 77 ELLsniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKH 151
|
170
....*....|....*
gi 1104677240 152 NCLVIFINQIRMKIG 166
Cdd:PRK09361 152 DLAVVITNQVYSDID 166
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
6-173 |
3.28e-15 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 70.33 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALD--IQYAGKLGVNVNELLVS 83
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 84 -------------QPDTGEQALEIADAlVRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKR 150
Cdd:COG0467 81 gllriidlspeelGLDLEELLARLREA-VEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 1104677240 151 TNCLVIFINQIRMKIGVMFGNPE 173
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
13-166 |
3.45e-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: 64.74 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 13 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEhALDI----QYAGKLGVNVNE-LLVSQP-- 85
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkQIAEDRPERALSnFIVFEVfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 86 -DTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMK 164
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
..
gi 1104677240 165 IG 166
Cdd:TIGR02237 153 VN 154
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
1-181 |
1.25e-12 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 64.51 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQK------LGGTAAFIDAEHALD----IQYA 70
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRperiEQMA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 71 GKLGVNVNELL----VSQP-DTGEQAL--EIADALVRSG-SIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLMSQ--A 140
Cdd:PRK04301 158 EALGLDPDEVLdnihVARAyNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQQKLNKHlhD 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1104677240 141 LRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNAL 181
Cdd:PRK04301 235 LLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHIL 272
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
14-166 |
5.50e-12 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 61.95 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 14 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVVAEMQKLGGTAA--FIDAEHALDIQ-------------YAGKLG 74
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 75 VNVNE------LLVSQPDTGEQALEIADAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 145
Cdd:cd19493 80 ENERAeemlkrVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180
....*....|....*....|....*
gi 1104677240 146 GTIKRT----NCLVIFINQIRMKIG 166
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFG 177
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
6-181 |
6.45e-12 |
|
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: 61.61 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQK------LGGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELL----VSQP-DTGEQAL---EIADALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 147
Cdd:cd19515 80 DPDEVLdniyVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190
....*....|....*....|....*....|....
gi 1104677240 148 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNAL 181
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHIL 189
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
13-161 |
7.03e-12 |
|
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: 61.92 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 13 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQ------KLGGTAAFIDAEHALDIQ----------------YA 70
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 71 GKLGVNVNELLVSQPDTGEQAL-EIADALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 149
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 1104677240 150 RTNCLVIFINQI 161
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
6-162 |
5.44e-11 |
|
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: 59.20 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALD--IQYAGKLGVNVNEL--- 80
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 ----LVSQPDTGEQALEIAD------ALVRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 150
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 1104677240 151 TNCLVIFINQIR 162
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
5-110 |
6.29e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 59.17 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 5 VVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVVAEMQKLGGTAAFIDAEHALdiqYA---GKLGVNVNEL 80
Cdd:COG4544 28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
|
90 100 110
....*....|....*....|....*....|
gi 1104677240 81 LVSQPDTGEQALEIADALVRSGSIDMIVID 110
Cdd:COG4544 105 LLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
6-181 |
1.28e-10 |
|
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: 58.47 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVA----EMQKLGGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCqlplEMGGGEGKALYIDTEGTFRperlVAIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELLVSQP-------DTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 146
Cdd:pfam08423 98 DPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQR 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1104677240 147 TIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNAL 181
Cdd:pfam08423 172 LADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIM 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-166 |
3.58e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 24 RGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYAGKLGVNVNELLVSqpDTGEQALEIADALVRSGS 103
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1104677240 104 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 166
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
6-163 |
1.42e-08 |
|
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: 52.25 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQ-VVAEMQKLGGTAAFIDA-EHALDI-QYAGKLGVNVNEL-- 80
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 --------LVSQP----------DTGEQALEIADAlVRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALR 142
Cdd:pfam06745 80 egklaiidASTSGigiaevedrfDLEELIERLREA-IREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILR 145
|
170 180
....*....|....*....|.
gi 1104677240 143 KLTGTIKRTNCLVIFINQIRM 163
Cdd:pfam06745 146 RLKRVLKGLGVTAIFTSEKPS 166
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
22-158 |
1.86e-08 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 52.60 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 22 LPRGRVVEIYGPESSGKTTLTLQVVAEMQK----LG-----GTAAFIDAE-HALDIQ-----YAGKLGVNVNEL------ 80
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwLGrrvppGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 81 --LVSQPDTGEQALEIADALVRSGsIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVIFI 158
Cdd:COG3598 90 lsLAGDLDDTDDLEALERAIEEEG-PDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVLLV 157
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
25-166 |
2.83e-08 |
|
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: 50.69 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 25 GRVVEIYGPESSGKTTLTLQVVAEMQ------KLGGTAAFIDAEHALDIQYagkLGV-NVNELLvsqpdtgeQALEIADA 97
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEGSFNIHY---FRVhDYVELL--------ALINSLPK 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 98 LVRSGS-IDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 166
Cdd:cd19492 70 FLEDHPkVKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
6-181 |
7.34e-08 |
|
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: 50.61 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVVAEMQKLGGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchtlavTCQLPIDRGGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELL-------VSQPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 146
Cdd:cd01123 80 DPDDVLdnvayarAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1104677240 147 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNAL 181
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNIL 191
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
1-161 |
8.88e-08 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 50.89 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEM--QKLGGT--AAFIDAEHALD----IQYA 70
Cdd:PLN03186 100 QEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLplDQGGGEgkAMYIDTEGTFRpqrlIQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 71 GKLGVNVNELL----VSQPDTGEQALEIadaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--LMS 138
Cdd:PLN03186 179 ERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmHLG 249
|
170 180
....*....|....*....|...
gi 1104677240 139 QALRKLTGTIKRTNCLVIFINQI 161
Cdd:PLN03186 250 KFLRSLQRLADEFGVAVVITNQV 272
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
25-166 |
1.47e-07 |
|
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.
Pssm-ID: 410898 [Multi-domain] Cd Length: 226 Bit Score: 49.65 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 25 GRVVEIYGPESSGKTTLTLQVVA-----------EMQKLGGTAAFIDAEHALDI----QYAGKLGVNVNELLVSQPDTGE 89
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswggvPLGGLEAAVVFIDTDGRFDIlrlrSILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 90 QALEIADALVR----------------------------SGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 138
Cdd:cd19490 81 VEEIARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 1104677240 139 QALRKLTgtiKRTNCLVIFINQIRMKIG 166
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
1-158 |
1.66e-07 |
|
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: 49.45 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDiQY---AGKLGVNV 77
Cdd:cd01121 59 EEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLGS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 78 NELLVsqpdTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCLV 155
Cdd:cd01121 137 DNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIPV 203
|
...
gi 1104677240 156 IFI 158
Cdd:cd01121 204 FLV 206
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
2-181 |
7.07e-07 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 48.23 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 2 DIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVVAEMQKLGGTAAFIDAEHALD----IQYAG 71
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahtlcvTTQLPTEMGGGNGKVAYIDTEGTFRpdriVPIAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 72 KLGVNVNELL----VSQPDTGEQ---ALEIADALVRSGSIDMIVIDSVAALVPKAEI-EGEMGDSlpglQARLmSQALRK 143
Cdd:PLN03187 183 RFGMDADAVLdniiYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSR 257
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1104677240 144 LTGTIKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNAL 181
Cdd:PLN03187 258 LTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVL 297
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
6-179 |
7.68e-07 |
|
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: 47.70 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVVAEMQKLGGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchtlavTCQLPIDQGGGEGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELL--VS-----QPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 146
Cdd:cd19513 80 NGEDVLdnVAyarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1104677240 147 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGN 179
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGN 189
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
6-181 |
8.12e-07 |
|
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: 47.35 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVAEMQKL----GGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELL----VSQPDTGEQALEIADAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 145
Cdd:cd19514 80 DHDAVLdnilYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1104677240 146 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNAL 181
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHIL 192
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
28-182 |
1.85e-06 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 44.80 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 28 VEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAehaLDIqyagklgvnvnellvsqpdtgeqALEIADALVRSGSIDMI 107
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF---LDT-----------------------ILEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1104677240 108 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 182
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
6-59 |
2.90e-06 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 45.80 E-value: 2.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFI 59
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
2-179 |
5.50e-06 |
|
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: 45.49 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 2 DIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL------TLQVVAEMQKLGGTAAFIDAEHALD----IQYAG 71
Cdd:TIGR02239 74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchtlavTCQLPIDQGGGEGKALYIDTEGTFRperlLAIAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 72 KLGVNVNELL--VS-----QPDTGEQALEIADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA--LR 142
Cdd:TIGR02239 153 RYGLNPEDVLdnVAyarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArfLR 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1104677240 143 KLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGN 179
Cdd:TIGR02239 227 SLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGN 267
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
5-181 |
1.57e-05 |
|
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: 44.00 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 5 VVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVA----EMQKLGGTAAFIDAEHALD----IQYAGKLG 74
Cdd:TIGR02238 77 KITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAqlprEMGGGNGKVAYIDTEGTFRpdriRAIAERFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 75 VN----VNELLVSQPDTGEQALEIAD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 147
Cdd:TIGR02238 156 VDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLNKI 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 1104677240 148 IKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNAL 181
Cdd:TIGR02238 232 SEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVL 268
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
20-116 |
7.44e-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: 41.47 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 20 GGLPRGRVVEIYGPESSGKTTLTLQVVAEM-QKLGGTAAFID------AEHALDI-QYAGKLGVNVNELL-------VSQ 84
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVaSRSGQNVLYIDtkssfsARRLAQIlKSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1104677240 85 PDTGEQALEIADALVR------SGSIDMIVIDSVAALV 116
Cdd:cd19489 82 PYELLDLLEELRNTLSqqqenlYSRLKLVIIDSLSALI 119
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
6-181 |
8.59e-05 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 41.91 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVVA----EMQKLGGTAAFIDAEHALD----IQYAGKLGV 75
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCqlpiEQGGGEGKVLYIDTEGTFRperiVQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 76 NVNELL----VSQPDTGEQALEI---ADALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 146
Cdd:PTZ00035 179 DPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlGKFLRALQK 252
|
170 180 190
....*....|....*....|....*....|....*...
gi 1104677240 147 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNAL 181
Cdd:PTZ00035 253 LADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHII 290
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
24-158 |
6.80e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.85 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 24 RGRVVEIYGPESSGKTTLTLQVvaemqklgGTAAFIDAEHALDIQYAGKLGVNVNELlvSQPDTGEQALEIADALVRsgS 103
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPDIVIRD--SWQDFLDAIDELTAAELA--D 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1104677240 104 IDMIVIDSVAALV-----------PKAEIEGEMGDSLP-GLQARLMSQALRKLTGTIKRtnclVIFI 158
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGKN----VIFT 131
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
1-122 |
1.61e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 38.03 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 1 EDIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEH------------ALDIQ 68
Cdd:PRK06067 2 GKKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENtsksylkqmesvKIDIS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 69 --YA-GKLGV---NVNELLVSqPDTGEQALEIADALVRSGSIDMIVIDSVAALVPKAEIE 122
Cdd:PRK06067 81 dfFLwGYLRIfplNTEGFEWN-STLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
30-70 |
1.81e-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: 37.69 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1104677240 30 IYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDIQYA 70
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKL 65
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
6-113 |
2.81e-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: 37.28 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTAAFIDAEHALDI--QYAGKLGVNVNELLvs 83
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTlfERSEALGIDLRAMV-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1104677240 84 qpDTGEQALEIADAL--------------VRSGSIDMIVIDSVA 113
Cdd:cd19487 78 --EKGLLSIEQIDPAelspgefaqrvrtsVEQEDARVVVIDSLN 119
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
6-44 |
5.31e-03 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 36.35 E-value: 5.31e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1104677240 6 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQ 44
Cdd:COG2874 3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQ 40
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
26-44 |
5.86e-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: 35.95 E-value: 5.86e-03
|
| |
