|
Name |
Accession |
Description |
Interval |
E-value |
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
1-220 |
4.44e-115 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 327.59 E-value: 4.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGL---LSGKKVAYVDTEGgFSPERLVQMAETrglNPEEAL 77
Cdd:PRK09361 4 RLPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVeaaKNGKKVIYIDTEG-LSPERFKQIAGE---DFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 SRFILFTPSDFKEQRRVIGSLKKTVDSNFALVVVDSITAHYRAE----ENRSGLIAELSRQLQVLLWIARKHNIPVIVIN 153
Cdd:PRK09361 80 SNIIIFEPSSFEEQSEAIRKAEKLAKENVGLIVLDSATSLYRLEledeEDNSKLNRELGRQLTHLLKLARKHDLAVVITN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2CVH_B 154 QVHFDSRTEMTKPVAEQTLGYRCKDILRLDKLPkPGLRVAVLERHRFRPEGLMAYFRITERGIEDVE 220
Cdd:PRK09361 160 QVYSDIDSDGLRPLGGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEIID 225
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
2-217 |
1.90e-107 |
|
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: 307.70 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGLLS---GKKVAYVDTEGgFSPERLVQMAETRglnPEEALS 78
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAakqGKKVVYIDTEG-LSPERFQQIAGER---FESIAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 79 RFILFTPSDFKEQRRVIGSLKKTVDSN-FALVVVDSITAHYRAEENR-SGLIAELSRQLQVLLWIARKHNIPVIVINQVH 156
Cdd:cd01394 77 NIIVFEPYSFDEQGVAIQEAEKLLKSDkVDLVVVDSATALYRLELGDdSEANRELSRQMSKLLSIARKYDIPVVITNQVY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
2CVH_B 157 FDSRTEMTKPVAEQTLGYRCKDILRLDKLPkPGLRVAVLERHRFRPEGLMAYFRITERGIE 217
Cdd:cd01394 157 SDIDDDRLKPVGGTLLEHWSKAIIRLEKSP-PGLRRATLEKHRSRPEGQSAGFRITDRGIR 216
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
9-217 |
4.51e-79 |
|
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: 235.77 E-value: 4.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 9 LDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGLL---SGKKVAYVDTEgGFSPERLVQMAETRglnPEEALSRFILFTP 85
Cdd:TIGR02237 1 IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNaarQGKKVVYIDTE-GLSPERFKQIAEDR---PERALSNFIVFEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 86 SDFKEQRRVIGSLKKTVDSN-FALVVVDSITAHYRAEE--NRSGLIAELSRQLQVLLWIARKHNIPVIVINQVHFDSRTE 162
Cdd:TIGR02237 77 FDFDEQGVAIQKTSKFIDRDsASLVVVDSFTALYRLELsdDRISRNRELARQLTLLLSLARKKNLAVVITNQVYTDVNNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
2CVH_B 163 MTKPVAEQTLGYRCKDILRLDKLpkPGLRVAVLERHRFRPEGLMAYFRITERGIE 217
Cdd:TIGR02237 157 TLRPLGGHLLEHWSKVILRLEKF--RGRRLATLEKHRSRPEGESVYFRITDDGIE 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
20-184 |
2.04e-55 |
|
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: 174.85 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 20 GVLTQVYGPYASGKTTLALQTG---LLSGKKVAYVDTEGGFSPERLVQMAE---TRGLNPEEALSRFILFTPSDFKEQRR 93
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAanaLLLGGGVVWIDTEGAFPPSRLVQILEaspSSELELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 94 VIGSLKKTVDS--NFALVVVDSITAHYRAEENR--------SGLIAELSRQLQVLLWIARKHNIPVIVINQVHFDSRT-- 161
Cdd:cd01393 81 ALDSLPESLFPppNTSLVVVDSVSALFRKAFPRggdgdsssSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGgs 160
|
170 180
....*....|....*....|....*
2CVH_B 162 --EMTKPVAEQTLGYRCKDILRLDK 184
Cdd:cd01393 161 gaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
2-219 |
3.38e-43 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 147.33 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQT----------GLLSGKKVaYVDTEGGFSPERLVQMAETRGL 71
Cdd:PRK04301 84 ITTGSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLavnvqlpeekGGLEGKAV-YIDTEGTFRPERIEQMAEALGL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFIL---FTpSDfkEQRRVIGSLKKTV--DSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIA 142
Cdd:PRK04301 163 DPDEVLDNIHVaraYN-SD--HQMLLAEKAEELIkeGENIKLVIVDSLTAHFRAEYVGRGNLAErqqkLNKHLHDLLRLA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 143 RKHNIPVIVINQVHfdSRTEM-----TKPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIE 217
Cdd:PRK04301 240 DLYNAAVVVTNQVM--ARPDAffgdpTQPIGGHILGHTATFRIYLRK-SKGNKRIARLVDSPHLPEG-EAVFRITEEGIR 315
|
..
2CVH_B 218 DV 219
Cdd:PRK04301 316 DA 317
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
2-218 |
4.86e-41 |
|
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: 139.42 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQT----------GLLSGKkVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLavnvqlppeeGGLNGK-AVYIDTENTFRPERIMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVIGSLKKTV--DSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKH 145
Cdd:cd19515 80 DPDEVLDNIYVARAYNSNHQMLLVEKAEDLIkeGNNIKLLIVDSLTSHFRAEYVGRGTLAErqqkLNKHLHDLHRLADLY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2CVH_B 146 NIPVIVINQVHfdSRTEM-----TKPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIED 218
Cdd:cd19515 160 NIAVLVTNQVM--AKPDAffgdpTQAIGGHILGHAATFRVYLRK-GKGGKRIARLVDSPHLPEG-EAVFRITEKGIED 233
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
2-218 |
3.49e-38 |
|
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 131290 [Multi-domain] Cd Length: 310 Bit Score: 134.10 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQT----------GLLSGKKVaYVDTEGGFSPERLVQMAETRGL 71
Cdd:TIGR02236 77 ITTGSKELDELLGGGIETQAITEVFGEFGSGKTQICHQLavnvqlpeekGGLGGKAV-YIDTENTFRPERIMQMAEARGL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRfiLFTPSDFKEQRRVI-----GSLKKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIA 142
Cdd:TIGR02236 156 DPDEVLKN--IYVARAYNSNHQMLlvekaEDLIKELNNPVKLLIVDSLTSHFRAEYVGRGALAErqqkLNKHLHDLLRLA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 143 RKHNIPVIVINQVHfdSRTEM-----TKPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIE 217
Cdd:TIGR02236 234 DLYNAAVVVTNQVM--ARPDAffgdpTRPIGGHILGHAATFRVYLRK-GKGDKRIARLVDSPHLPEG-EAVFRITEKGIE 309
|
.
2CVH_B 218 D 218
Cdd:TIGR02236 310 D 310
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
1-155 |
5.67e-38 |
|
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: 132.43 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLALQTGL---LSG--KKVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:pfam08423 18 QITTGSKELDKLLGGGIETGSITEIFGEFRTGKTqlchTLCVTCQLpleMGGgeGKALYIDTEGTFRPERLVAIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVIGSL-KKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHN 146
Cdd:pfam08423 98 DPEDVLDNVAYARAYNSEHQMQLLQQAaAMMSESRFALLIVDSATALYRTDFSGRGELAErqqhLAKFLRTLQRLADEFG 177
|
....*....
2CVH_B 147 IPVIVINQV 155
Cdd:pfam08423 178 VAVVITNQV 186
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
2-217 |
3.43e-35 |
|
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: 124.56 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLA----------LQTGLLSGkKVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLChtlavtcqlpIDRGGGEG-KAIYIDTEGTFRPERLRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVIGSL-KKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHN 146
Cdd:cd01123 80 DPDDVLDNVAYARAFNSDHQTQLLDQAaAMMVESRFKLLIVDSATALYRTDYSGRGELSArqmhLAKFLRMLQRLADEFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2CVH_B 147 IPVIVINQVHFDSRTEMT------KPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIE 217
Cdd:cd01123 160 VAVVVTNQVVAQVDGAMMfaadpkKPIGGNILAHASTTRLYLRK-GRGETRICKIYDSPCLPEA-EAVFAITADGVG 234
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
1-220 |
1.96e-33 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 122.41 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLALQTGLL-----SGKKVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:PTZ00035 99 RITTGSTQLDKLLGGGIETGSITELFGEFRTGKTqlchTLCVTCQLPieqggGEGKVLYIDTEGTFRPERIVQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVIGSL-KKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHN 146
Cdd:PTZ00035 179 DPEDVLDNIAYARAYNHEHQMQLLSQAaAKMAEERFALLIVDSATALFRVDYSGRGELAErqqhLGKFLRALQKLADEFN 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 147 IPVIVINQVHFDSRTEMT------KPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIEDVE 220
Cdd:PTZ00035 259 VAVVITNQVMADVDGASMfvadpkKPIGGHIIAHASTTRLSLRK-GRGEQRICKIYDSPNLPES-EAVFAISEGGIIDAK 336
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
2-219 |
4.93e-31 |
|
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: 115.65 E-value: 4.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLALQTGLL-----SGKKVAYVDTEGGFSPERLVQMAETRGLN 72
Cdd:TIGR02238 78 ITTGSQALDGILGGGIESMSITEVFGEFRCGKTqlshTLCVTAQLPremggGNGKVAYIDTEGTFRPDRIRAIAERFGVD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 PEEALSRFILFTPSDFKEQRRVIGSL-KKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHNI 147
Cdd:TIGR02238 158 PDAVLDNILYARAYTSEHQMELLDYLaAKFSEEPFRLLIVDSIMALFRVDFSGRGELSErqqkLAQMLSRLNKISEEFNV 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2CVH_B 148 PVIVINQVHFDSRTEMT------KPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIEDV 219
Cdd:TIGR02238 238 AVFVTNQVQADPGATMTfiadpkKPIGGHVLAHASTTRILLRK-GRGEERVAKLYDSPDMPEA-EASFQITEGGIADA 313
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
1-155 |
5.49e-31 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 115.99 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLAL--QTGLLSG---KKVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:PLN03186 104 QITTGSRELDKILEGGIETGSITEIYGEFRTGKTqlchTLCVtcQLPLDQGggeGKAMYIDTEGTFRPQRLIQIAERFGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVI---GSLkkTVDSNFALVVVDSITAHYRAEEN-------RSGLIAELSRQLQVLlwi 141
Cdd:PLN03186 184 NGADVLENVAYARAYNTDHQSELLleaASM--MAETRFALMIVDSATALYRTEFSgrgelsaRQMHLGKFLRSLQRL--- 258
|
170
....*....|....
2CVH_B 142 ARKHNIPVIVINQV 155
Cdd:PLN03186 259 ADEFGVAVVITNQV 272
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
2-155 |
6.10e-31 |
|
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: 113.57 E-value: 6.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLAL--QTGLLSGK---KVAYVDTEGGFSPERLVQMAETRGLN 72
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTqlchTLAVtcQLPIDQGGgegKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 PEEALSRFILFTPSDFKEQRRVIGSLKKT-VDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHNI 147
Cdd:cd19513 81 GEDVLDNVAYARAYNTDHQMQLLIQASAMmAESRYALLIVDSATALYRTDYSGRGELSArqmhLAKFLRMLQRLADEFGV 160
|
....*...
2CVH_B 148 PVIVINQV 155
Cdd:cd19513 161 AVVITNQV 168
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
2-218 |
8.02e-31 |
|
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: 113.22 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLALQTGL-----LSGKKVAYVDTEGGFSPERLVQMAETRGLN 72
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTqlshTLCVTAQLpgsmgGGGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 PEEALSRFIL---FTpSDFKEQRRVIGSLKKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKH 145
Cdd:cd19514 81 HDAVLDNILYaraYT-SEHQMELLDYVAAKFHEEAVFRLLIIDSIMALFRVDFSGRGELAErqqkLAQMLSRLQKISEEY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2CVH_B 146 NIPVIVINQVHFDSRTEMT------KPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIED 218
Cdd:cd19514 160 NVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISLRK-GRGEERIAKIYDSPDLPEN-EATFAITAGGIAD 236
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
9-155 |
1.62e-28 |
|
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: 107.38 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 9 LDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGL---LS------GKKVAYVDTEGGFSPERLVQMAET-RGLNPEEALS 78
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALtvqLPrelgglGGGAVYICTESSFPSKRLQQLASSlPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 79 RF---ILFTP-SDFKEQRRVigsLKKTV-----DSNFALVVVDSITAHYRAEEN--------RSGLIAELSRQLQVLlwi 141
Cdd:cd19491 81 NFldnIFVEHvADLETLEHC---LNYQLpalleRGPIRLVVIDSIAALFRSEFDtsrsdlveRAKYLRRLADHLKRL--- 154
|
170
....*....|....
2CVH_B 142 ARKHNIPVIVINQV 155
Cdd:cd19491 155 ADKYNLAVVVVNQV 168
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
1-220 |
7.40e-28 |
|
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: 107.12 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLAL--QTGLLSGK---KVAYVDTEGGFSPERLVQMAETRGL 71
Cdd:TIGR02239 77 QLTTGSKELDKLLGGGIETGSITEIFGEFRTGKTqlchTLAVtcQLPIDQGGgegKALYIDTEGTFRPERLLAIAERYGL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 72 NPEEALSRFILFTPSDFKEQRRVIGSLKKTV-DSNFALVVVDSITAHYRAEENRSGLIA----ELSRQLQVLLWIARKHN 146
Cdd:TIGR02239 157 NPEDVLDNVAYARAYNTDHQLQLLQQAAAMMsESRFALLIVDSATALYRTDFSGRGELSarqmHLARFLRSLQRLADEFG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 147 IPVIVINQV--HFDSRTEM-----TKPVAEQTLGYRCKDILRLDKlPKPGLRVAVLERHRFRPEGlMAYFRITERGIEDV 219
Cdd:TIGR02239 237 VAVVITNQVvaQVDGAGSMfagdpKKPIGGNIMAHASTTRLSLRK-GRGEQRICKIYDSPCLPES-EAMFAIYEDGIGDP 314
|
.
2CVH_B 220 E 220
Cdd:TIGR02239 315 K 315
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
2-158 |
2.60e-27 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 106.40 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKT----TLALQTGL---LSG--KKVAYVDTEGGFSPERLVQMAETRGLN 72
Cdd:PLN03187 108 ITTGSQALDELLGGGIETRCITEAFGEFRSGKTqlahTLCVTTQLpteMGGgnGKVAYIDTEGTFRPDRIVPIAERFGMD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 PEEALSRfILFTPSDFKEQRR--VIGSLKKTVDSNFALVVVDSITAHYRAEENRSGLIAE----LSRQLQVLLWIARKHN 146
Cdd:PLN03187 188 ADAVLDN-IIYARAYTYEHQYnlLLGLAAKMAEEPFRLLIVDSVIALFRVDFTGRGELAErqqkLAQMLSRLTKIAEEFN 266
|
170
....*....|..
2CVH_B 147 IPVIVINQVHFD 158
Cdd:PLN03187 267 VAVYMTNQVIAD 278
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
10-155 |
1.81e-23 |
|
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: 93.54 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 10 DSLLGGGFAPGVLTQVYGPYASGKTTLALQ--TGLLSGKK-------VAYVDTEGGFSPERLVQMAETR----------- 69
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTlaSSAAMPARkggldggVLYIDTESKFSAERLAEIAEARfpeafsgfmee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 70 GLNPEEALSRFILFTPSDFKEQRRVIGSLKKTV-DSNFALVVVDSITAHYRAE-ENRSGLIAE----LSRQLQVLLWIAR 143
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHIlSSGVRLVVIDSIAALVRREfGGSDGEVTErhnaLAREASSLKRLAE 160
|
170
....*....|..
2CVH_B 144 KHNIPVIVINQV 155
Cdd:cd19493 161 EFRIAVLVTNQA 172
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
1-217 |
2.62e-22 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 90.36 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYVDTEGgfSPERLVQMAETRGLNPEEAL 77
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQflaEGLRRGEKGLYVSFEE--SPEQLLRRAESLGLDLEEYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 SR-FILFTPSDFKEQRRVIGSLKKTV-----DSNFALVVVDSITAHYRAEENrsglIAELSRQLQVLLWIARKHNIPVIV 151
Cdd:COG0467 79 ESgLLRIIDLSPEELGLDLEELLARLreaveEFGAKRVVIDSLSGLLLALPD----PERLREFLHRLLRYLKKRGVTTLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2CVH_B 152 INQVHfdsrtEMTKPVAEQTLGYRCKDILRLDKLPKPGLRVAVLERHRFR---PEGLMAYFRITERGIE 217
Cdd:COG0467 155 TSETG-----GLEDEATEGGLSYLADGVILLRYVELGGELRRALSVLKMRgsaHDRTIREFEITDGGIE 218
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
14-155 |
1.14e-21 |
|
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: 88.46 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 14 GGGFAPGVLTQVYGPYASGKT----TLALQTGLLSGKKVAYVDTEGGFSPERLVQMAETRGL---NPEEALSRFI---LF 83
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTqlclTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQdaeEIDKALQRIRvvrVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 84 TPSDFKEQRRVIGSL----KKTVDSNFALVVVDSITA----HYRAEENRSG--LIAELSRQLQVLlwiARKHNIPVIVIN 153
Cdd:cd19489 81 DPYELLDLLEELRNTlsqqQENLYSRLKLVIIDSLSAlispLLGGSKHSEGhaLLASLARLLKKL---AAEYQIAVLVTN 157
|
..
2CVH_B 154 QV 155
Cdd:cd19489 158 LT 159
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-155 |
2.39e-19 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 84.84 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQT---GLLSGKKVAYVDTEGGFSPERlvqmAETRGLNPEEa 76
Cdd:COG0468 43 VISTGSLALDIALGvGGLPRGRIVEIYGPESSGKTTLALHAiaeAQKAGGIAAFIDAEHALDPEY----AKKLGVDIDN- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 77 lsrfILFTPSDFKEQRRVIgsLKKTVDSN-FALVVVDSITAHYRAEE-------NRSGLIAEL-SRQLQVLLWIARKHNI 147
Cdd:COG0468 118 ----LLVSQPDTGEQALEI--AETLVRSGaVDLIVVDSVAALVPKAEiegemgdSHVGLQARLmSQALRKLTGAISKSNT 191
|
....*...
2CVH_B 148 PVIVINQV 155
Cdd:COG0468 192 TVIFINQL 199
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
20-155 |
6.93e-16 |
|
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: 72.26 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 20 GVLTQVYGPYASGKTTLALQT----------GLLSGKKVaYVDTEGGFSPErlvqmaetrglnpeealsrfiLFTPSDFK 89
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLavnvqipkcfGGLAGEAI-YIDTEGSFNIH---------------------YFRVHDYV 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2CVH_B 90 EQRRVIGSLKKTV--DSNFALVVVDSITAHYRAEENRSGLIAE-LSRQLQVLLWIARKHNIPVIVINQV 155
Cdd:cd19492 59 ELLALINSLPKFLedHPKVKLIVVDSIAFPFRHDFDDLAQRTRlLNGLAQLLHSLARQHNLAVVLTNQV 127
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
2-155 |
7.80e-16 |
|
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: 73.36 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQTGL---LSGKKVAYVDTEGGFSPErlvqMAETRGLNPEEal 77
Cdd:cd00983 5 IPTGSLSLDIALGiGGLPRGRIIEIYGPESSGKTTLALHAIAeaqKLGGTAAFIDAEHALDPE----YAKKLGVDIDN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 srFILFTPSDFKEQRRVIGSLKKT--VDsnfaLVVVDSITAHY-RAE------ENRSGLIAEL-SRQLQVLLWIARKHNI 147
Cdd:cd00983 79 --LLVSQPDTGEQALEIADTLIRSgaVD----LIVVDSVAALVpKAEiegemgDSHVGLQARLmSQALRKLTGSLSKSKT 152
|
....*...
2CVH_B 148 PVIVINQV 155
Cdd:cd00983 153 TVIFINQL 160
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
2-217 |
1.44e-14 |
|
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: 69.60 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYVDTEGgfSPERLVQMAETRG--LNPEEA 76
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQflyAGAKNGEPGLFFTFEE--SPERLLRNAKSFGwdFDEMED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 77 LSRFIL-------FTPSDFKEQRRVIGSLKKtvDSNFALVVVDSITAHYRAEENRSGLIAELSRQLQVLlwiaRKHNIPV 149
Cdd:cd01124 79 EGKLIIvdappteAGRFSLDELLSRILSIIK--SFKAKRVVIDSLSGLRRAKEDQMRARRIVIALLNEL----RAAGVTT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2CVH_B 150 IVINQVHFDSRTEMTKPVAEQTLGyrckD-ILRLDKLPKPGLRVAVLERHRFRPEGLM---AYFRITERGIE 217
Cdd:cd01124 153 IFTSEMRSFLSSESAGGGDVSFIV----DgVILLRYVEIEGELRRTIRVLKMRGTGHDtgtHPFEITDKGIV 220
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
2-155 |
1.64e-14 |
|
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: 70.12 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQTGLLSGKK---VAYVDTEGGFSPerlvQMAETRGLNPEEal 77
Cdd:pfam00154 33 ISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAggtAAFIDAEHALDP----VYAKKLGVDIDN-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 srfILFTPSDFKEQRRVIgsLKKTVDSN-FALVVVDSITAHY-RAE------ENRSGLIAEL-SRQLQVLLWIARKHNIP 148
Cdd:pfam00154 107 ---LLVSQPDTGEQALEI--ADMLVRSGaIDLIVVDSVAALVpKAEiegemgDSHVGLQARLmSQALRKLTGSISKSNTT 181
|
....*..
2CVH_B 149 VIVINQV 155
Cdd:pfam00154 182 VIFINQI 188
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
2-155 |
3.17e-13 |
|
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: 67.40 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQT---GLLSGKKVAYVDTEGGFSPErlvqMAETRGLNPEEal 77
Cdd:TIGR02012 36 ISTGSLALDLALGvGGLPKGRIIEIYGPESSGKTTLALHAiaeAQKAGGTAAFIDAEHALDPV----YARKLGVDIDN-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 srfILFTPSDFKEQRRVIGSL---KKTVDsnfaLVVVDSITAHY-RAE------ENRSGLIAEL-SRQLQVLLWIARKHN 146
Cdd:TIGR02012 110 ---LLVSQPDTGEQALEIAETlvrSGAVD----IIVVDSVAALVpKAEiegemgDSHVGLQARLmSQALRKLTGALSKSN 182
|
....*....
2CVH_B 147 IPVIVINQV 155
Cdd:TIGR02012 183 TTAIFINQI 191
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
9-152 |
3.47e-13 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 67.23 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 9 LDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGLL--SGK----------KVAYVDTEGGFSP--ERLVQMAETRGLNPE 74
Cdd:COG3598 2 RRWLVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAvaAGGpwlgrrvppgKVLYLAAEDDRGElrRRLKALGADLGLPFA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2CVH_B 75 EALSRFILFTPSDFKEQRRVIGSLKKTVDS-NFALVVVDSITAHYRAEENRSGLIAELsrqLQVLLWIARKHNIPVIVI 152
Cdd:COG3598 82 DLDGRLRLLSLAGDLDDTDDLEALERAIEEeGPDLVVIDPLARVFGGDENDAEEMRAF---LNPLDRLAERTGAAVLLV 157
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
20-199 |
1.12e-10 |
|
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: 59.28 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 20 GVLTQVYGPYASGKTTLALQ---TGLLS-----------GKKVAYVDTEGGFSPERLVQMAETRGLNP------------ 73
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHlaaRCILPsswggvplgglEAAVVFIDTDGRFDILRLRSILEARIRAAiqaanssddeed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 74 -----EEALSRFILFTPSDFKEQRRVIGSLKKTVDSNF-----ALVVVDSITAHY---RAEENRSGLIAELSRQ-----L 135
Cdd:cd19490 81 veeiaRECLQRLHIFRCHSSLQLLATLLSLENYLLSLSanpelGLLLIDSISAFYwqdRFSAELARAAPLLQEAalraiL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
2CVH_B 136 QVLLWIARKHNIPVIVINQVHFDSRTEMTKPVAEQTLGYRCKDILRLDKLPKPGLRVAvleRHR 199
Cdd:cd19490 161 RELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHREYLPRPWQRLV---THR 221
|
|
| recA |
PRK09354 |
recombinase A; Provisional |
3-155 |
1.45e-10 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 59.81 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 3 STGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQT---GLLSGKKVAYVDTEGGFSPerlvQMAETRGLNPEEals 78
Cdd:PRK09354 42 STGSLALDIALGiGGLPRGRIVEIYGPESSGKTTLALHAiaeAQKAGGTAAFIDAEHALDP----VYAKKLGVDIDN--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 79 rFILFTPsDFKEQR-RVIGSLKKT--VDsnfaLVVVDSITAHY-RAE------ENRSGLIAEL-SRQLQVLLWIARKHNI 147
Cdd:PRK09354 115 -LLVSQP-DTGEQAlEIADTLVRSgaVD----LIVVDSVAALVpKAEiegemgDSHVGLQARLmSQALRKLTGNISKSNT 188
|
....*...
2CVH_B 148 PVIVINQV 155
Cdd:PRK09354 189 TVIFINQI 196
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
9-157 |
1.03e-09 |
|
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: 55.85 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 9 LDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGL--LSGK------------KVAYVDTEGGFS--PERLVQMAETRGLN 72
Cdd:pfam13481 22 RRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAavATGKpwlggprvpeqgKVLYVSAEGPADelRRRLRAAGADLDLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 PEEAL-----SRFILFTPSDFKEQRRVIGSLKKTVD--SNFALVVVDSITAHYRAEENRSgliAELSRQLQVLLWIARKH 145
Cdd:pfam13481 102 ARLLFlslveSLPLFFLDRGGPLLDADVDALEAALEevEDPDLVVIDPLARALGGDENSN---SDVGRLVKALDRLARRT 178
|
170
....*....|..
2CVH_B 146 NIPVIVInqVHF 157
Cdd:pfam13481 179 GATVLLV--HHV 188
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
2-217 |
5.55e-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: 54.17 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLS-GKKVAYVDTEGgfSPERLVQMAETRGLNPEEAL 77
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQflyNGALKyGEPGVFVTLEE--PPEDLRENARSFGWDLEKLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 78 SRFILF--------TPSDFKEQRRVIGSLKKTV-----DSNFALVVVDSITAH-YRAEEnrsgliAELSRQLQVLLWIAR 143
Cdd:pfam06745 79 EEGKLAiidastsgIGIAEVEDRFDLEELIERLreairEIGAKRVVIDSITTLfYLLKP------AVAREILRRLKRVLK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2CVH_B 144 KHNIPVIVINQVHFDSRTEMTKPVAEqtlgYRCKDILRLDKLPKPGLRVAVLE--RHRFRPEGLMAY-FRITERGIE 217
Cdd:pfam06745 153 GLGVTAIFTSEKPSGEGGIGGYGVEE----FIVDGVIRLDLKEIEEERVRTIEivKMRGTPHSMKRYpFEITDNGIV 225
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
1-127 |
2.24e-08 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 52.53 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYVDTEGGfSPERLVQMAETrGLNPEEAL 77
Cdd:COG2874 2 IISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQfayGALENGLSVTYISTELT-TKEFIKQMKSL-SYDISDYL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
2CVH_B 78 SR-FILFTPSDFK------EQRR----VIGSLKKTVDSNFALVVVDSITAHYRAEENRSGL 127
Cdd:COG2874 80 LRgRLLFLPVHPLgfewnsKQRKdllkRLMKYIASNLWEADVIIIDSLSALLRNAEESAIL 140
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
2-167 |
3.19e-08 |
|
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: 51.92 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYVDTEGGFspERLVQMAETRGLNPEEALS 78
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQfakAAAARGERSVLFSFDESI--GTLFERSEALGIDLRAMVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 79 RFIL---------FTPSDFKEQRRvigslKKTVDSNFALVVVDSITAHYRAEENRSGLIaelsRQLQVLLWIARKHNIPV 149
Cdd:cd19487 79 KGLLsieqidpaeLSPGEFAQRVR-----TSVEQEDARVVVIDSLNGYLNAMPDERFLI----LQMHELLSYLNNQGVTT 149
|
170
....*....|....*...
2CVH_B 150 IVINQVHFDSRTEMTKPV 167
Cdd:cd19487 150 LLIVAQHGLLGGDMGTPV 167
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
2-155 |
3.29e-08 |
|
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: 52.53 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQTGLL---SGKKVAYVDTEGgfSPERLVQMAETRGLNPEEALs 78
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARlaqRGGKVLYVSGEE--SLSQIKLRAERLGLGSDNLY- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 79 rfiLFTPSDFKEqrrVIGSLKKTvdsNFALVVVDSITAHYRAEENRS-GLIAelsrqlQV------LLWIARKHNIPVIV 151
Cdd:cd01121 141 ---LLAETNLEA---ILAEIEEL---KPSLVVIDSIQTVYSPELTSSpGSVS------QVrecaaeLLRLAKETGIPVFL 205
|
....
2CVH_B 152 INQV 155
Cdd:cd01121 206 VGHV 209
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
2-125 |
6.53e-07 |
|
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: 48.09 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLL-GGGFAPGVLTQVYGPYASGKTTLA---LQTGLLSGKKVAYVDTEGgfSPERLVQMAETRGLNPEEA- 76
Cdd:cd19484 1 ISTGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLLAasfADAACRRGERCLYFAFEE--SPAQLIRNAKSIGIDLEQMe 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
2CVH_B 77 ---LSRFILFTPSDFKEQRRVIGSLKKTVDSNFALVVVDSITAHYRAEENRS 125
Cdd:cd19484 79 rkgLLKIICARPELYGLEDHLIIIKSEINEFKPSRVIVDPLSALARGGSLNE 130
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
2-154 |
9.90e-07 |
|
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 427509 [Multi-domain] Cd Length: 254 Bit Score: 48.18 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLgGGFAPGVLTQVYGPYASGKTTLAL----QTGLLSGKKVAYVDTEggFSPERLVQ-M--AETR----- 69
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLIIIAARPSMGKTAFALniarNAAVKHKKPVAIFSLE--MSAEQLVMrLlaSEAGvdsqk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 70 ----GLNPEE---------ALSRFILF-------TPSDFKEQ-RRvigsLKKTvdSNFALVVVDS---ITAHYRAeENRS 125
Cdd:pfam03796 79 lrtgQLTDEDweklakaagRLSEAPLYiddtpglSIAEIRAKaRR----LKRE--HGLGLIVIDYlqlMSGGSRG-ENRQ 151
|
170 180
....*....|....*....|....*....
2CVH_B 126 GLIAELSRQLQVLlwiARKHNIPVIVINQ 154
Cdd:pfam03796 152 QEISEISRSLKAL---AKELNVPVIALSQ 177
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-155 |
1.52e-06 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 48.17 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 1 MLSTGTKSLDSLLG-GGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYVDTEGGFSPErlvqMAETRGLNPEEa 76
Cdd:PRK09519 40 VIPTGSIALDVALGiGGLPRGRVIEIYGPESSGKTTVALHavaNAQAAGGVAAFIDAEHALDPD----YAKKLGVDTDS- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 77 lsrfILFTPSDFKEQRRVIGSLkKTVDSNFALVVVDSITAHY-RAE------ENRSGLIAEL-SRQLQVLLWIARKHNIP 148
Cdd:PRK09519 115 ----LLVSQPDTGEQALEIADM-LIRSGALDIVVIDSVAALVpRAElegemgDSHVGLQARLmSQALRKMTGALNNSGTT 189
|
....*..
2CVH_B 149 VIVINQV 155
Cdd:PRK09519 190 AIFINQL 196
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
2-217 |
2.34e-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: 46.57 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQ---TGLLSGKKVAYV---DTEggfspERLVQMAETRGLN--- 72
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQfllEGAANGETGLYItlsETE-----QELRAVALSHGWSldg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 73 --------PEEALSR---FILFTPSDFK--EQRRVIGSLKKTVDSnfALVVVDSITahyraeENRsgLIAELS----RQL 135
Cdd:cd19488 76 ihifelspSESALDAaqqYTILHPSELElsETTRLIFERVERLKP--SRVVIDSLS------ELR--LLAQDSlryrRQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 136 QVLLWIARKHNIPVIVINqvhfdsrtEMTKPVAEQTLGYRCKDILRLDKL-PKPG-----LRVAVLERHRFRpEGLMAyF 209
Cdd:cd19488 146 LALKQFFAGRNTTVLLLD--------DLTSDAADLDLHSIAHGVIRLEQLeSDYGaarrrLRVSKMRGSSFR-GGYHD-F 215
|
....*...
2CVH_B 210 RITERGIE 217
Cdd:cd19488 216 RITRGGLQ 223
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
2-125 |
4.79e-06 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 46.41 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLA---LQTGLLSGKKVAYVDTEGgfSPERLVQMAETRGLNPEEALS 78
Cdd:PRK09302 255 ISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLAskfAEAACRRGERCLLFAFEE--SRAQLIRNARSWGIDLEKMEE 332
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2CVH_B 79 ----RFILFTPSDFKEQRRVIGSLKKTVDSNFALVVVDSITAHYRAEENRS 125
Cdd:PRK09302 333 kgllKIICARPESYGLEDHLIIIKREIEEFKPSRVAIDPLSALARGGSLNE 383
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
1-65 |
4.48e-05 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 43.04 E-value: 4.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2CVH_B 1 MLSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQT---GLLSGKKVAYVDTEGGfSPERLVQM 65
Cdd:PRK06067 6 IISTGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFvygALKQGKKVYVITTENT-SKSYLKQM 72
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
25-119 |
3.07e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.39 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 25 VYGPYASGKTTLALQTGllsgkKVAYVDTEGGfsperlvqmaeTRGLNPEEALSRFILFTPSDFKEQrrvIGSLKKTVDS 104
Cdd:pfam13479 7 IYGPSGIGKTTFAKTLP-----KPLFLDTEKG-----------SKALDGDRFPDIVIRDSWQDFLDA---IDELTAAELA 67
|
90
....*....|....*
2CVH_B 105 NFALVVVDSITAHYR 119
Cdd:pfam13479 68 DYKTIVIDTVDWLER 82
|
|
| PRK05748 |
PRK05748 |
replicative DNA helicase; Provisional |
2-154 |
4.85e-04 |
|
replicative DNA helicase; Provisional
Pssm-ID: 180232 [Multi-domain] Cd Length: 448 Bit Score: 40.32 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGgFAPGVLTQVYGPYASGKTTLALQ----TGLLSGKKVAYVDTEGGfsPERLVQ-M--AE------- 67
Cdd:PRK05748 186 IPTGFTDLDKMTSG-LQPNDLIIVAARPSVGKTAFALNiaqnVATKTDKNVAIFSLEMG--AESLVMrMlcAEgnidaqr 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 68 --TRGLNPEE---------ALSRFILF-------TPSDFKEQRRvigSLKKTVDsNFALVVVDS---ITAHYRAEENRSG 126
Cdd:PRK05748 263 lrTGQLTDDDwpkltiamgSLSDAPIYiddtpgiKVTEIRARCR---RLAQEHG-GLGLILIDYlqlIQGSGRSGENRQQ 338
|
170 180
....*....|....*....|....*...
2CVH_B 127 LIAELSRQLQVLlwiARKHNIPVIVINQ 154
Cdd:PRK05748 339 EVSEISRSLKAL---AKELKVPVIALSQ 363
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
2-133 |
5.82e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.25 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 2 LSTGTKSLDSLLGGGFAPGVLTQVYGPYASGKTTLALQTgLLSGkkVAYVDTEGGF-----SPERLVQMAETRGLNPEEA 76
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQF-LVNG--IKRFDEPGVFvtfeeSPEDIIRNVASFGWDLQKL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 77 LSR---FILFTPSDFKEQrRVIGS---------LKKTVDSNFA-LVVVDSITAHYRAEENRSGLIAELSR 133
Cdd:PRK09302 90 IDEgklFILDASPDPSEQ-EEAGEydlealfirIEYAIDKIGAkRVVLDSIEALFSGFSNEAVVRRELRR 158
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-175 |
1.30e-03 |
|
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: 38.12 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 25 VYGPYASGKTTLALQTGLL---SGKKVAYVDTEGGFSPERLVQMAETRGLNPEEalsrfilftPSDFKEQRRVIGSLKKt 101
Cdd:smart00382 7 IVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS---------GSGELRLRLALALARK- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2CVH_B 102 vdSNFALVVVDSITAHYRAEENRSGLIAELSRQLQVLLwiaRKHNIPVIVINQVHFDSRTEMTKPVAEQTLGYR 175
Cdd:smart00382 77 --LKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLK---SEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| PAXNEB |
pfam05625 |
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is ... |
3-31 |
3.47e-03 |
|
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is an RNA polymerase II Elongator protein subunit. It is part of the HAP subcomplex of Elongator, which is a six-subunit component of the RNA polymerase II holoenzyme. The HAP subcomplex is required for Elongator structural integrity and histone acetyltransferase activity. This protein family has a P-loop-like motif and adopts a RecA-ATPase-like fold, lacking the conserved sequence signature of ATPases.
Pssm-ID: 461696 Cd Length: 359 Bit Score: 37.58 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|...
2CVH_B 3 STGTKSLDSLLGGGFAPG----VLTQVYGPYAS 31
Cdd:pfam05625 20 STGTPSLDKLLGGGLPLGssllIEEDGTTDFAG 52
|
|
| Elp4 |
cd19494 |
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex ... |
3-56 |
5.66e-03 |
|
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases.
Pssm-ID: 410902 Cd Length: 259 Bit Score: 36.90 E-value: 5.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
2CVH_B 3 STGTKSLDSLLGGGFAPGVLT----QVYGPYAS--GKTTLAlQtGLLSGKKVAYVDTEGG 56
Cdd:cd19494 14 STGIASLDDLLGGGLPLGSLLlieeDSHSSYAKllLKYFLA-E-GLVSGHHVFVASADDD 71
|
|
| DnaE |
COG0587 |
DNA polymerase III, alpha subunit [Replication, recombination and repair]; |
87-157 |
7.78e-03 |
|
DNA polymerase III, alpha subunit [Replication, recombination and repair];
Pssm-ID: 440352 [Multi-domain] Cd Length: 1050 Bit Score: 36.97 E-value: 7.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2CVH_B 87 DFKEQRRVIGSLKKTVDSNFALvvvdSITAHYRAEENRsgliaelsrQLQVLLWIARKHNIPVIVINQVHF 157
Cdd:COG0587 146 QYDEAEAALARLKDIFGDRFYL----ELQRHGLPEDRR---------VNAALLELARELGLPLVATNDVHY 203
|
|
| |
