|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-190 |
5.03e-158 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 439.61 E-value: 5.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:PRK09354 42 STGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:PRK09354 122 TGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIG 201
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:PRK09354 202 VMFGNPETTTGGNALKFYASVRLDIRRIGT 231
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-190 |
2.37e-155 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 432.67 E-value: 2.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:COG0468 45 STGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:COG0468 125 TGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIG 204
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:COG0468 205 VMFGNPETTTGGNALKFYASVRLDIRRIGT 234
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
1-190 |
2.90e-142 |
|
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: 395.39 E-value: 2.90e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:cd00983 6 PTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:cd00983 86 TGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKIG 165
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:cd00983 166 VMFGNPETTTGGNALKFYASVRLDIRRIEL 195
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-190 |
3.63e-141 |
|
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: 395.97 E-value: 3.63e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:TIGR02012 37 STGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:TIGR02012 117 TGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKIG 196
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:TIGR02012 197 VMFGNPETTTGGNALKFYASVRLDIRRIGT 226
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-190 |
1.77e-140 |
|
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: 391.76 E-value: 1.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:pfam00154 34 STGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:pfam00154 114 TGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKIG 193
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:pfam00154 194 VMFGNPETTTGGRALKFYASVRLDIRRIGQ 223
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-190 |
8.21e-121 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 359.41 E-value: 8.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQPD 80
Cdd:PRK09519 42 PTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 81 TGEQALEIADMLIRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIG 160
Cdd:PRK09519 122 TGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIG 201
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 161 VMFGSPETTTGGRALKFYASVRLDVRRIES 190
Cdd:PRK09519 202 VMFGSPETTTGGKALKFYASVRMDVRRVET 231
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
19-187 |
7.19e-53 |
|
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: 167.14 E-value: 7.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 19 GRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKAL-----------GVDTDAMLVSQPDTGEQALE 87
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVQIleaspsselelAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 88 IADMLIRSGA----LDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIGVMF 163
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 2538887248 164 G-SPETTTGGRALKFYASVRLDVRR 187
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
1-154 |
2.20e-16 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 73.89 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEhALDPE-YAKALGVDTDAML---- 75
Cdd:cd01394 2 STGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPErFQQIAGERFESIAsnii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 76 VSQP-DTGEQALEIADM--LIRSGALDIIVIDSVAALVpRAEiegEMGDShvGLQARLMSQaLRKITGVLSNTGTTAIFI 152
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
..
gi 2538887248 153 NQ 154
Cdd:cd01394 153 NQ 154
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
7-184 |
3.86e-15 |
|
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).
Pssm-ID: 274047 [Multi-domain] Cd Length: 209 Bit Score: 70.14 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 7 LDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEhALDPEYAKALGVD-----TDAMLVSQP-- 79
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 80 -DTGEQALEIADMLIRSGALDIIVIDSVAALVpRAEIEGEMGDSHVGL--QARLMSQALRKitgvlsnTGTTAIFINQLR 156
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELarQLTLLLSLARK-------KNLAVVITNQVY 150
|
170 180 190
....*....|....*....|....*....|
gi 2538887248 157 EKIGVMFGSPettTGGRALKFY--ASVRLD 184
Cdd:TIGR02237 151 TDVNNGTLRP---LGGHLLEHWskVILRLE 177
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
1-118 |
1.18e-12 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 63.73 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEhALDPEYAKAL-GVDTDA----ML 75
Cdd:PRK09361 6 PTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEEllsnII 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2538887248 76 VSQP-DTGEQALEIADM--LIRSGAlDIIVIDSVAALVpRAEIEGE 118
Cdd:PRK09361 84 IFEPsSFEEQSEAIRKAekLAKENV-GLIVLDSATSLY-RLELEDE 127
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
1-167 |
1.34e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 63.78 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDP--EYAKALGVDTDAMLVS- 77
Cdd:COG0467 3 PTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIESg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 78 ------------QPDTGEQALEIADMLIRSGAlDIIVIDSVAALVPRAEIEGEmgdshvglqARLMsqaLRKITGVLSNT 145
Cdd:COG0467 82 llriidlspeelGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 2538887248 146 GTTAIFINQLREKIGVMFGSPE 167
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
1-98 |
1.96e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 60.71 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPE-SSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSQP 79
Cdd:COG4544 30 PTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVRA 109
|
90
....*....|....*....
gi 2538887248 80 DTGEQALEIADMLIRSGAL 98
Cdd:COG4544 110 RRPADALWAAEEALRSGAC 128
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
2-187 |
2.34e-11 |
|
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: 60.45 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQR------AGGIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:cd19515 3 TGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRPErimqMAKALGLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML----VSQP-DTGEQAL---EIADMLIRSGALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQALRkitgv 141
Cdd:cd19515 82 DEVLdniyVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR----- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2538887248 142 LSNTGTTAIFI-NQLREKIGVMFGSPETTTGGRALKFYASVRLDVRR 187
Cdd:cd19515 155 LADLYNIAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
2-187 |
5.11e-11 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 60.28 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRA------GGIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:PRK04301 86 TGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLPeekgglEGKAVYIDTEGTFRPErieqMAEALGLDP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML----VSQP-DTGEQAL--EIADMLIRSG-ALDIIVIDSVAALVpRAEiegemgdsHVGL------QARL---MSQA 134
Cdd:PRK04301 165 DEVLdnihVARAyNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLnkhLHDL 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2538887248 135 LRkitgvLSNTGTTAIFI-NQLREKIGVMFGSPETTTGGRALKFYASVRLDVRR 187
Cdd:PRK04301 236 LR-----LADLYNAAVVVtNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
1-158 |
7.53e-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: 58.81 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDP--EYAKALGVDTDAM---- 74
Cdd:cd01124 2 KTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERllRNAKSFGWDFDEMedeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 75 ---LVSQPDTGEQALEIADML------IRSGALDIIVIDSVAALVPRAEiegemgdshvglQARLMSQALRKITGVLSNT 145
Cdd:cd01124 81 kliIVDAPPTEAGRFSLDELLsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRAA 148
|
170
....*....|...
gi 2538887248 146 GTTAIFINQLREK 158
Cdd:cd01124 149 GVTTIFTSEMRSF 161
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
1-187 |
4.52e-10 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 56.98 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQ------RAGGIAAFIDAEHALDPE----YAKALGVD 70
Cdd:cd19514 2 STGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLSHTLCVTAQlpgsmgGGGGKVAYIDTEGTFRPDrirpIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 71 TDAML----VSQPDTGEQALEIADML----IRSGALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQaLRKItg 140
Cdd:cd19514 81 HDAVLdnilYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKI-- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2538887248 141 vlSNTGTTAIFI-NQLREKIG--VMFGS-PETTTGGRALKFYASVRLDVRR 187
Cdd:cd19514 156 --SEEYNVAVFItNQVTADPGaaMTFQAdPKKPIGGHILAHASTTRISLRK 204
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
1-190 |
2.27e-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: 54.94 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALH-AVANAQRAGGIAAFIDA-EHALD-PEYAKALGVDTDA---- 73
Cdd:pfam06745 2 KTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLEKleee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 74 -MLV----SQPDTGEQALEIADML------IRSGALDI----IVIDSVAALvprAEIEGEMgdshvglQARlmsQALRKI 138
Cdd:pfam06745 81 gKLAiidaSTSGIGIAEVEDRFDLeelierLREAIREIgakrVVIDSITTL---FYLLKPA-------VAR---EILRRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2538887248 139 TGVLSNTGTTAIFINQLREKigvmfgspETTTGGRALKFYAS---VRLDVRRIES 190
Cdd:pfam06745 148 KRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
2-187 |
3.43e-09 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 54.46 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQ------RAGGIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:cd01123 3 TGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLCHTLAVTCQlpidrgGGEGKAIYIDTEGTFRPErlraIAQRFGLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML-------VSQPDTGEQALEIADMLIRSGALDIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQALRkitgvL 142
Cdd:cd01123 82 DDVLdnvayarAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALY-RTDYsgRGELSARQMHL-AKFLRMLQR-----L 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2538887248 143 SNTGTTAIFI-NQLREKIG---VMFGSPETTTGGRALKFYASVRLDVRR 187
Cdd:cd01123 155 ADEFGVAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
8-121 |
4.18e-09 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 53.86 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 8 DVALGvGGLPRGRVVEVYGPESSGKTTVALHAVA----NAQRAGGIAA--FIDAEHALDPEYAKALGVDTDAM-LVSQPD 80
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASsaamPARKGGLDGGvlYIDTESKFSAERLAEIAEARFPEaFSGFME 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538887248 81 TGEQALEIADML---------------------IRSGALDIIVIDSVAALVpRAEIEGEMGD 121
Cdd:cd19493 80 ENERAEEMLKRVavvrvttlaqllerlpnleehILSSGVRLVVIDSIAALV-RREFGGSDGE 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
18-189 |
6.33e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 18 RGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDTDAMLVSqpDTGEQALEIADMLIRSGA 97
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 98 LDIIVIDSVAALVPRaeiegemgdshVGLQARLMSQALRKITGVLSNTGTTAIFINQlrekigvmfgsPETTTGGRALKF 177
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRR 136
|
170
....*....|..
gi 2538887248 178 YASVRLDVRRIE 189
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
22-176 |
8.45e-09 |
|
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: 51.35 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 22 VEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAehaldpeyakalgVDTDAMLVSQpdtgeqaleiadmLIRSGALDII 101
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF-------------LDTILEAIED-------------LIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2538887248 102 VIDSVAALVPRAEiegemgdshvGLQARLMSQALRKITGVLSNTGTTAIFINQLREKIGVMFGSPETTTGGRALK 176
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
2-187 |
3.03e-08 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 52.09 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQR------AGGIAAFIDAEHALDPEYAKAL----GVDT 71
Cdd:TIGR02238 80 TGSQALDGILG-GGIESMSITEVFGEFRCGKTQLSHTLCVTAQLpremggGNGKVAYIDTEGTFRPDRIRAIaerfGVDP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML----VSQPDTGEQALEIADML---IRSGALDIIVIDSVAALVpRAEI--EGEMGDShvglQARLmSQALRKITGvL 142
Cdd:TIGR02238 159 DAVLdnilYARAYTSEHQMELLDYLaakFSEEPFRLLIVDSIMALF-RVDFsgRGELSER----QQKL-AQMLSRLNK-I 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2538887248 143 SNTGTTAIFI-NQLREKIG--VMFGS-PETTTGGRALKFYASVRLDVRR 187
Cdd:TIGR02238 232 SEEFNVAVFVtNQVQADPGatMTFIAdPKKPIGGHVLAHASTTRILLRK 280
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
2-187 |
7.56e-08 |
|
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.
Pssm-ID: 462471 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQR------AGGIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:pfam08423 21 TGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLCHTLCVTCQLplemggGEGKALYIDTEGTFRPErlvaIAERYGLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAMLVSQP-------DTGEQALEIADMLIRSGALDIIVIDSVAALVpRAEIE--GEMGDSHVGLqARLMSqALRKitgvL 142
Cdd:pfam08423 100 EDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-TLQR----L 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2538887248 143 SNTGTTAIFI-NQLREKIG---VMF-GSPETTTGGRALKFYASVRLDVRR 187
Cdd:pfam08423 173 ADEFGVAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
2-187 |
8.24e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 48.19 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKT----TVALHA-VANAQRAG-GIAAFIDAEHALDPE------------- 62
Cdd:PLN03186 107 TGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCqLPLDQGGGeGKAMYIDTEGTFRPQrliqiaerfglng 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 63 --------YAKALGVDTDAMLVsqpdtgeqaLEIADMLIRSgALDIIVIDSVAALVpRAEIEGEmGDshvgLQAR--LMS 132
Cdd:PLN03186 186 advlenvaYARAYNTDHQSELL---------LEAASMMAET-RFALMIVDSATALY-RTEFSGR-GE----LSARqmHLG 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2538887248 133 QALRKITGVLSNTGTTAIFINQLREKI--GVMFGSPETT-TGGRALKFYASVRLDVRR 187
Cdd:PLN03186 250 KFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK 307
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
7-160 |
1.98e-06 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 46.52 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 7 LDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQ---RAGGI---AAFIDAEHAL----------------DPEYA 64
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprELGGLgggAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 65 KALGVDTDAMLVSQPDTGEQAL-EIADMLIRSGALDIIVIDSVAALVpRAEIEGEMGDShvGLQARLMSQALRKITGVLS 143
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF-RSEFDTSRSDL--VERAKYLRRLADHLKRLAD 156
|
170
....*....|....*..
gi 2538887248 144 NTGTTAIFINQLREKIG 160
Cdd:cd19491 157 KYNLAVVVVNQVTDRFD 173
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
2-187 |
9.41e-06 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 44.99 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQ------RAGGIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:PTZ00035 102 TGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLCHTLCVTCQlpieqgGGEGKVLYIDTEGTFRPErivqIAERFGLDP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML----VSQPDTGEQALEiadMLIRSGAL------DIIVIDSVAALVpRAEI--EGEMGDSHVGLqARLMSQALRkit 139
Cdd:PTZ00035 181 EDVLdniaYARAYNHEHQMQ---LLSQAAAKmaeerfALLIVDSATALF-RVDYsgRGELAERQQHL-GKFLRALQK--- 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2538887248 140 gvLSNTGTTAIFI-NQLREKIG---VMFGSPETTTGGRALKFYASVRLDVRR 187
Cdd:PTZ00035 253 --LADEFNVAVVItNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
14-190 |
3.74e-05 |
|
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410897 [Multi-domain] Cd Length: 209 Bit Score: 42.62 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 14 GGLPRGRVVEVYGPESSGKTTVALHAVAN-AQRAGGIAAFIDAEHALDPE-------YAKALGVDTDAML-------VSQ 78
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANvASRSGQNVLYIDTKSSFSARrlaqilkSRAQDAEEIDKALqrirvvrVFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 79 PDTGEQAL-EIADMLIR-----SGALDIIVIDSVAALVprAEIEGemGDSHVGLQARLMSQA--LRKITG------VLSN 144
Cdd:cd19489 82 PYELLDLLeELRNTLSQqqenlYSRLKLVIIDSLSALI--SPLLG--GSKHSEGHALLASLArlLKKLAAeyqiavLVTN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2538887248 145 TGTTAIFINQLREkigvmfgspETTTGGRALKFYASVRLDVRRIES 190
Cdd:cd19489 158 LTVRGGDGGQQGS---------TKPALGEYWESVPSTRLLLSRDEN 194
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
19-143 |
5.95e-05 |
|
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.
Pssm-ID: 410898 [Multi-domain] Cd Length: 226 Bit Score: 42.34 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 19 GRVVEVYGPESSGKTTVALHAVANA----------QRAGGIAA-FIDAEHALD-----------------PEYAKALGVD 70
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpsswggvpLGGLEAAVvFIDTDGRFDilrlrsileariraaiqAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 71 TDAMLVS--------QPDTGEQALEIADML-------IRSGALDIIVIDSVAALVPRAEIEGEMGdshvGLQARLMSQAL 135
Cdd:cd19490 81 VEEIAREclqrlhifRCHSSLQLLATLLSLenyllslSANPELGLLLIDSISAFYWQDRFSAELA----RAAPLLQEAAL 156
|
....*...
gi 2538887248 136 RKITGVLS 143
Cdd:cd19490 157 RAILRELR 164
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
2-187 |
1.06e-04 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 41.53 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKT----TVALHAVANAQRAG--GIAAFIDAEHALDPE----YAKALGVDT 71
Cdd:cd19513 3 TGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFRPErllaIAERYGLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 72 DAML----VSQPDTGEQALEiadMLIRSGAL------DIIVIDSVAALVpRAEIEGEmGDshvgLQARLM--SQALRKIT 139
Cdd:cd19513 82 EDVLdnvaYARAYNTDHQMQ---LLIQASAMmaesryALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2538887248 140 GVLSNTGTTAIFINQLREKI--GVMF-GSPETTTGGRALKFYASVRLDVRR 187
Cdd:cd19513 153 RLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
24-110 |
2.00e-04 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 40.77 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 24 VYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPEYAKALGVDT----DAMLVSQPDTG------EQALEIADMLI 93
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKLDRFEEVRrlaeALGIAVPKAELeesklaFLAIELLLEAL 104
|
90
....*....|....*...
gi 2538887248 94 -RSGALDIIVIDSVAALV 110
Cdd:pfam01637 105 kRRGKKIAIIIDEVQQAI 122
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
18-146 |
3.34e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 39.62 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 18 RGRVVEVYGPESSGKTTVALHAvanaqragGIAAFIDAEHALdpeyaKALGVDtDAMLVSQPDTGEQALEIADmLIRSGA 97
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGS-----KALDGD-RFPDIVIRDSWQDFLDAID-ELTAAE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2538887248 98 L---DIIVIDSVAALVpraeiegemgdSHVGLQARLMSQALRKITGVLSNTG 146
Cdd:pfam13479 66 LadyKTIVIDTVDWLE-----------RLCLAYICKQNGKGSSIEDGGYGKG 106
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
2-53 |
3.38e-04 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 40.02 E-value: 3.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFI 53
Cdd:cd19488 3 TGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
2-187 |
6.69e-04 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 39.32 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 2 TGSIALDVALGvGGLPRGRVVEVYGPESSGKT----TVALHAVANAQRAG--GIAAFIDAE--------------HALDP 61
Cdd:TIGR02239 80 TGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEgtfrperllaiaerYGLNP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 62 E-------YAKALGVDTDAMLVSQPdtgeqaleiADMLIRSgALDIIVIDSVAALVpRAEIEGEmGDshvgLQARLMSQA 134
Cdd:TIGR02239 159 EdvldnvaYARAYNTDHQLQLLQQA---------AAMMSES-RFALLIVDSATALY-RTDFSGR-GE----LSARQMHLA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2538887248 135 --LRKITGVLSNTGTTAIFINQLREKI---GVMF-GSPETTTGGRALKFYASVRLDVRR 187
Cdd:TIGR02239 223 rfLRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
16-189 |
1.04e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.73 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 16 LPRGRVVEVYGPESSGKTTVALH---AVANAQRAGGI------AAFIDAE---HALDP---EYAKALGVDTDA-----ML 75
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAGGPWLGRrvppgkVLYLAAEddrGELRRrlkALGADLGLPFADldgrlRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 76 VSQPDTGEQALEIADM--LIRSGALDIIVIDSVAALVPraeiegemGDSHVGLQARLMSQALRKItgvLSNTGTTAIFIN 153
Cdd:COG3598 90 LSLAGDLDDTDDLEALerAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL---AERTGAAVLLVH 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 2538887248 154 QLReKIGVMFGSPETTTGGRALKFYASVRLDVRRIE 189
Cdd:COG3598 159 HTG-KGGAGKDSGDRARGSSALRGAARSVLVLSREK 193
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
1-145 |
1.70e-03 |
|
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410892 [Multi-domain] Cd Length: 218 Bit Score: 37.69 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538887248 1 PTGSIALDVALGVGGLPRGRVVEVYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDP--EYAKALGVDTDAMLVSQ 78
Cdd:cd19484 2 STGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQliRNAKSIGIDLEQMERKG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2538887248 79 ---------PDTG-EQALEIADMLIRSGALDIIVIDSVAALVpRAEIEGEMGDSHVGLQARLMSQalrKITGVLSNT 145
Cdd:cd19484 82 llkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSALA-RGGSLNEVKEFVIRLIDYLKSQ---EITGLFTNL 154
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
1-75 |
3.79e-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: 36.89 E-value: 3.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2538887248 1 PTGSIALDVALGvGGLPRGRVVEVYGPESSGKTTVAL-HAVANAQRAGGIAAFI-DAEHALDPEYAKALGVDTDAML 75
Cdd:cd19487 2 SSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALqFAKAAAARGERSVLFSfDESIGTLFERSEALGIDLRAMV 77
|
|
| |
