|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-248 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 542.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 1 DDRTMDIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVD 80
Cdd:PRK09354 32 DDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 81 IDNLLVSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMI 160
Cdd:PRK09354 112 IDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 161 FINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQIMYGEGINL 240
Cdd:PRK09354 192 FINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDIMYGEGISR 271
|
....*...
gi 290795135 241 YGELIDLG 248
Cdd:PRK09354 272 EGELIDLG 279
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-248 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 528.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 1 DDRTMDIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVD 80
Cdd:COG0468 35 DKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 81 IDNLLVSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMI 160
Cdd:COG0468 115 IDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 161 FINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQIMYGEGINL 240
Cdd:COG0468 195 FINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGISK 274
|
....*...
gi 290795135 241 YGELIDLG 248
Cdd:COG0468 275 EGELLDLA 282
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-248 |
4.29e-178 |
|
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: 491.89 E-value: 4.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 1 DDRTMDIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVD 80
Cdd:TIGR02012 27 EKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 81 IDNLLVSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMI 160
Cdd:TIGR02012 107 IDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 161 FINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQIMYGEGINL 240
Cdd:TIGR02012 187 FINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFDILYGEGISK 266
|
....*...
gi 290795135 241 YGELIDLG 248
Cdd:TIGR02012 267 LGEIIDLA 274
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-239 |
4.15e-172 |
|
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: 474.19 E-value: 4.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 1 DDRTMDIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVD 80
Cdd:pfam00154 24 DEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 81 IDNLLVSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMI 160
Cdd:pfam00154 104 IDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 290795135 161 FINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQIMYGEGIN 239
Cdd:pfam00154 184 FINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
6-239 |
6.04e-167 |
|
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: 460.10 E-value: 6.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 6 DIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVDIDNLL 85
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 86 VSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMIFINQI 165
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290795135 166 RMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQIMYGEGIN 239
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGIS 234
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-223 |
1.39e-107 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 327.82 E-value: 1.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 1 DDRTMDIDTVSTGSLSLDIALGAGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVD 80
Cdd:PRK09519 32 DEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 81 IDNLLVSQPDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMI 160
Cdd:PRK09519 112 TDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAI 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 290795135 161 FINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGSIKEGDEIVGNDTRVKVVKNKIAA 223
Cdd:PRK09519 192 FINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCLA 254
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
29-197 |
3.18e-58 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 182.94 E-value: 3.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 29 GRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYA-----------GKLGVDIDNLLVSQPDTGEQALE 97
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 98 IADALTRSGA----VDVIIIDSVAALTPKAEIEGEMGDSHMGLQARMLSQAMRKLTANIKNSNTLMIFINQIRMKIGVMF 173
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 290795135 174 G-NPETTTGGNALKFYASVRLDIRR 197
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
10-232 |
2.00e-18 |
|
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: 80.82 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEhALDP-----VYAGKLGVDIDNL 84
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 85 LVSQP-DTGEQALEIADA--LTRSGAVDVIIIDSVAALTpKAEiegEMGDSHMglqARMLSQAMRKLTANIKNSNTLMIF 161
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDSEA---NRELSRQMSKLLSIARKYDIPVVI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290795135 162 INQIRMKIGVMFGNPettTGGNALKfYASvrldirriGSIKEGDEIVGNDTRVKVVKNKIAAPFKQAEFQI 232
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLE-HWS--------KAIIRLEKSPPGLRRATLEKHRSRPEGQSAGFRI 210
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
10-177 |
1.87e-13 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 67.25 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPV--YAGKLGVDIDNLLVS 87
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 88 -------------QPDTGEQALEIADALTRSGAvDVIIIDSVAALTpkaeiegemgdsHMGLQARMLSQAMRKLTANIKN 154
Cdd:COG0467 81 gllriidlspeelGLDLEELLARLREAVEEFGA-KRVVIDSLSGLL------------LALPDPERLREFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 290795135 155 SNTLMIFINQIRMKIGVMFGNPE 177
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
10-197 |
2.98e-13 |
|
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: 67.17 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL------TLQVVAEAQKIGKTCAFIDAEHALDPV----YAGKLGV 79
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchtlavTCQLPIDRGGGEGKAIYIDTEGTFRPErlraIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 80 D----IDNLLVSQPDTGEQALEI---ADALTRSGAVDVIIIDSVAALTPKAEI-EGEMGDSHMGLqARMLSQAMRkltan 151
Cdd:cd01123 80 DpddvLDNVAYARAFNSDHQTQLldqAAAMMVESRFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLRMLQR----- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 290795135 152 IKNSNTLMIFI-NQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 197
Cdd:cd01123 154 LADEFGVAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
9-123 |
5.81e-13 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 66.11 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 9 TVSTGSLSLDIALGAGGLPFGRIVEIYGPE-SSGKTTLTLQVVAEAQKIGKTCAFIDAEHALdpvYA---GKLGVDIDNL 84
Cdd:COG4544 28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 290795135 85 LVSQPDTGEQALEIA-DALtRSGAVDVIIIDsVAALTPKA 123
Cdd:COG4544 105 LLVRARRPADALWAAeEAL-RSGACGAVVAW-LERLDLTA 142
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
10-197 |
2.65e-12 |
|
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: 64.63 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAEAQK----IGKTCAFIDAEHALDPV----YAGKLGV 79
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLemggGEGKALYIDTEGTFRPErlvaIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 80 D----IDNLLVSQPDTGE---QALEIADALTRSGAVDVIIIDSVAALTpKAEIE--GEMGDSHMglqarMLSQAMRKLtA 150
Cdd:pfam08423 98 DpedvLDNVAYARAYNSEhqmQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQ-----HLAKFLRTL-Q 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 290795135 151 NIKNSNTLMIFI-NQIRMKIG---VMF-GNPETTTGGNALKFYASVRLDIRR 197
Cdd:pfam08423 171 RLADEFGVAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
18-200 |
6.31e-12 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 63.11 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 18 DIALGaGGLPFGRIVEIYGPESSGKT----TLTLQVVAEAQKIGKT--CAFIDAEHAL------------DPVY------ 73
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDggVLYIDTESKFsaerlaeiaearFPEAfsgfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 74 -AGKLGVDIDNLLVSQPDTGEQALEIADAL---TRSGAVDVIIIDSVAALTPKaeiegEMGDSHMGLQARM--LSQAMRK 147
Cdd:cd19493 80 eNERAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTERHnaLAREASS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 290795135 148 LTANIKNSNTLMIFINQIRMKIGVMFGNPETTTG--GNALKFYASVRLDIRRIGS 200
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
7-232 |
1.41e-11 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 62.19 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 7 IDTVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEhALDP-----VYAGKLGVDI 81
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPerfkqIAGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 82 DNLLVSQP-DTGEQALEIADALTRSGA-VDVIIIDSVAALTpKAEIEGEMGDSHMglqARMLSQAMRKLTANIKNSNTLM 159
Cdd:PRK09361 80 SNIIIFEPsSFEEQSEAIRKAEKLAKEnVGLIVLDSATSLY-RLELEDEEDNSKL---NRELGRQLTHLLKLARKHDLAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 290795135 160 IFINQIRMKIGvmfGNPETTTGGNALKfYAS---VRLDIRRigsikegdeivGNDTRVKVVKNKIAAPFKQAEFQI 232
Cdd:PRK09361 156 VITNQVYSDID---SDGLRPLGGHTLE-HWSktiLRLEKFR-----------NGKRRATLEKHRSRPEGESAEFRI 216
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
17-170 |
1.81e-11 |
|
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: 61.66 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 17 LDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEhALDP-----VYAGKLGVDIDNLLVSQP-D 90
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkqIAEDRPERALSNFIVFEVfD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 91 TGEQALEIADALT--RSGAVDVIIIDSVAALTpKAEIEGEMGDSHMGLQARM--LSQAMRKltaniknSNTLMIFINQIR 166
Cdd:TIGR02237 79 FDEQGVAIQKTSKfiDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQLtlLLSLARK-------KNLAVVITNQVY 150
|
....
gi 290795135 167 MKIG 170
Cdd:TIGR02237 151 TDVN 154
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
10-239 |
2.40e-11 |
|
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: 61.60 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAEAQKI-----GKTCaFIDAEHALDP----VYAGKLG 78
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 79 VD----IDNLLVSQPDTGEQALEIADALTRSGAVD----VIIIDSVAAL-----TPKaeieGEMGDSHMGLqARMLSQAM 145
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMALfrvdfSGR----GELAERQQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 146 RkltanIKNSNTLMIFI-NQIRMKIG--VMF-GNPETTTGGNALKFYASVRLDIRRigsiKEGDEivgndtRVKVVKNKI 221
Cdd:cd19514 154 K-----ISEEYNVAVFItNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK----GRGEE------RIAKIYDSP 218
|
250
....*....|....*...
gi 290795135 222 AAPFKQAEFQIMYGeGIN 239
Cdd:cd19514 219 DLPENEATFAITAG-GIA 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-198 |
6.09e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 29 GRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVDIDNLLVSqpDTGEQALEIADALTRSGAV 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 109 DVIIIDSVAALTPKAEiegemgdshmgLQARMLSQAMRKLTANIKNSNTLMIFINqirmkigvmfgNPETTTGGNALKFY 188
Cdd:smart00382 80 DVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRRR 137
|
170
....*....|
gi 290795135 189 ASVRLDIRRI 198
Cdd:smart00382 138 FDRRIVLLLI 147
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
3-197 |
1.26e-09 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 57.19 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 3 RTMDIDTVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQK------IGKTCAFIDAEHALDP----V 72
Cdd:PRK04301 77 RRKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRPerieQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 73 YAGKLGVDID----NLLVSQP-DTGEQAL--EIADALTRSG-AVDVIIIDSVAALTpKAEI--EGEMGDSHMGLqARMLS 142
Cdd:PRK04301 156 MAEALGLDPDevldNIHVARAyNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAEYvgRGNLAERQQKL-NKHLH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 290795135 143 QAMRklTANIknSNTLMIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 197
Cdd:PRK04301 234 DLLR--LADL--YNAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
6-239 |
1.59e-09 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 57.09 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 6 DIDTVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAE-AQKIGKTC---AFIDAEHALDP----VYAG 75
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQlPTEMGGGNgkvAYIDTEGTFRPdrivPIAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 76 KLGVD----IDNLLVSQPDTGEQALEIADALTRSGAVD---VIIIDSVAALTPKAEI-EGEMGDSHMGLqARMLSqamrK 147
Cdd:PLN03187 183 RFGMDadavLDNIIYARAYTYEHQYNLLLGLAAKMAEEpfrLLIVDSVIALFRVDFTgRGELAERQQKL-AQMLS----R 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 148 LTANIKNSNTLMIFINQIRMKIG--VMFGNPETTTGGNALKFYASVRLDIRRiGSikegdeivgNDTRVKVVKNKIAAPF 225
Cdd:PLN03187 258 LTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK-GK---------GEQRVCKVFDAPNLPE 327
|
250
....*....|....
gi 290795135 226 KQAEFQIMYGeGIN 239
Cdd:PLN03187 328 AEAEFQITSG-GIM 340
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
10-197 |
7.36e-09 |
|
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a homolog of Rad51. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR)
Pssm-ID: 410923 [Multi-domain] Cd Length: 233 Bit Score: 54.68 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQK------IGKTCAFIDAEHALDP----VYAGKLGV 79
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 80 DIDNLL----VSQP-DTGEQAL---EIADALTRSGAVDVIIIDSVAALTpKAEI--EGEMGDSHMGLqARMLSQAMRklT 149
Cdd:cd19515 80 DPDEVLdniyVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR--L 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 290795135 150 ANIKNsntLMIFI-NQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 197
Cdd:cd19515 156 ADLYN---IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
10-235 |
8.73e-09 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 54.78 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAEAQKIGK----TCAFIDAEHALDP----VYAGKLGV 79
Cdd:TIGR02238 78 ITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGggngKVAYIDTEGTFRPdrirAIAERFGV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 80 D----IDNLLVSQPDTGEQALEIADALTRSGAVD---VIIIDSVAAL-TPKAEIEGEMGDshmglQARMLSQAMRKLTAN 151
Cdd:TIGR02238 157 DpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMALfRVDFSGRGELSE-----RQQKLAQMLSRLNKI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 152 IKNSNTLMIFINQIRMKIG--VMF-GNPETTTGGNALKFYASVRLDIRRigsiKEGDEivgndtRVKVVKNKIAAPFKQA 228
Cdd:TIGR02238 232 SEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK----GRGEE------RVAKLYDSPDMPEAEA 301
|
....*..
gi 290795135 229 EFQIMYG 235
Cdd:TIGR02238 302 SFQITEG 308
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
6-238 |
1.28e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 51.66 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 6 DIDTVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAE---AQKIG-KTCAFIDAEHALDP----VYAG 75
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQlplDQGGGeGKAMYIDTEGTFRPqrliQIAE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 76 KLGVD----IDNLLVSQPDTGEQALEI---ADALTRSGAVDVIIIDSVAALTpKAEIEGEmGDshmgLQAR--MLSQAMR 146
Cdd:PLN03186 180 RFGLNgadvLENVAYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKFLR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 147 KLTANIKNSNTLMIFINQIRMKI--GVMFGNPETT-TGGNALKFYASVRLDIRRigsiKEGDEivgndtRVKVVKNKIAA 223
Cdd:PLN03186 254 SLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGEN------RICKVISSPCL 323
|
250
....*....|....*
gi 290795135 224 PFKQAEFQIMyGEGI 238
Cdd:PLN03186 324 PEAEARFSIS-SEGV 337
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
10-197 |
2.54e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 50.77 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAE-----AQKIGKtCAFIDAEHALDP----VYAGKLG 78
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGK-VLYIDTEGTFRPerivQIAERFG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 79 VD----IDNLLVSQPDTGEQALEI---ADALTRSGAVDVIIIDSVAALTpkaEIE----GEMGDSHMGLqARMLSqAMRK 147
Cdd:PTZ00035 178 LDpedvLDNIAYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF---RVDysgrGELAERQQHL-GKFLR-ALQK 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 290795135 148 LtANIKNsntLMIFI-NQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 197
Cdd:PTZ00035 253 L-ADEFN---VAVVItNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
10-200 |
5.86e-07 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 48.78 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQ-VVAEAQKIGKTCAFIDA-EHALDPVY-AGKLGVDIDNL-- 84
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 85 --------LVSQP----------DTGEQALEIADALTRSGAvDVIIIDSVAALtpkAEIEGEMgdshmglqarMLSQAMR 146
Cdd:pfam06745 80 egklaiidASTSGigiaevedrfDLEELIERLREAIREIGA-KRVVIDSITTL---FYLLKPA----------VAREILR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 290795135 147 KLTANIKNSNTLMIFINQIRMKigvmfgnpETTTGGNALKFYAS---VRLDIRRIGS 200
Cdd:pfam06745 146 RLKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
17-165 |
5.98e-07 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 49.21 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 17 LDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQ------KIGKTCAFIDAEHAL-------------DPVYAGKL 77
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 78 GVDIDNLLVSQPDTGEQALEI----ADALTRSGAVDVIIIDSVAALtpkAEIEGEMGDSHMGLQARMLSQAMRKLTANIK 153
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHClnyqLPALLERGPIRLVVIDSIAAL---FRSEFDTSRSDLVERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 290795135 154 NSNTLMIFINQI 165
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
10-197 |
1.16e-06 |
|
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: 48.08 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQV-----VAEAQKIGKtCAFIDAEHALDPV----YAGKLG 78
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 79 VD----IDNLLVSQP---DTGEQALEIADALTRSGAVDVIIIDSVAALTpKAEIEGEmGDshmgLQARM--LSQAMRKLT 149
Cdd:cd19513 79 LNgedvLDNVAYARAyntDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQmhLAKFLRMLQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 290795135 150 ANIKNSNTLMIFINQIRMKI--GVMF-GNPETTTGGNALKFYASVRLDIRR 197
Cdd:cd19513 153 RLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
10-166 |
1.23e-06 |
|
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: 48.03 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVY--AGKLGVDIDNL--- 84
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 85 ----LVSQPDTGEQALEIADALTR------SGAVDVIIIDSVAALTPKAEiegemgdshmglQARMLSQAMRKLTANIKN 154
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDELLSRilsiikSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 290795135 155 SNTLMIFINQIR 166
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
9-120 |
2.65e-06 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 47.13 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 9 TVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAE----------HAL-----DPVY 73
Cdd:COG2874 2 IISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTElttkefikqmKSLsydisDYLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 290795135 74 AGKLGVDIDNLLVSQPDTGE-----QALEIADALTRSGAvDVIIIDSVAALT 120
Cdd:COG2874 81 RGRLLFLPVHPLGFEWNSKQrkdllKRLMKYIASNLWEA-DVIIIDSLSALL 131
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
3-197 |
4.78e-06 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 46.64 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 3 RTMDIDTVSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTL--TLQVVAE---AQKIGK-TCAFIDAEHALDPV---- 72
Cdd:TIGR02239 71 RRQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQlpiDQGGGEgKALYIDTEGTFRPErlla 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 73 YAGKLGVD----IDNLLVSQPDTGEQALEI---ADALTRSGAVDVIIIDSVAALTPKAEI-EGEMGDSHMGLqARMLsqa 144
Cdd:TIGR02239 150 IAERYGLNpedvLDNVAYARAYNTDHQLQLlqqAAAMMSESRFALLIVDSATALYRTDFSgRGELSARQMHL-ARFL--- 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 290795135 145 mRKLTANIKNSNTLMIFINQIRMKI---GVMF-GNPETTTGGNALKFYASVRLDIRR 197
Cdd:TIGR02239 226 -RSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
10-126 |
6.42e-06 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 45.73 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAE--------------HALDPVYA- 74
Cdd:PRK06067 7 ISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTEntsksylkqmesvkIDISDFFLw 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 290795135 75 GKLGVDIDNLLVSQ--PDTGEQALEIADALTRSGAVDVIIIDSVAALTPKAEIE 126
Cdd:PRK06067 86 GYLRIFPLNTEGFEwnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
10-63 |
1.84e-05 |
|
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: 44.65 E-value: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFI 63
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
10-116 |
2.73e-05 |
|
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: 44.06 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPV--YAGKLGVDIDNLLVs 87
Cdd:cd01121 64 ISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSDNLYL- 141
|
90 100
....*....|....*....|....*....
gi 290795135 88 qpdTGEQALEIADALTRSGAVDVIIIDSV 116
Cdd:cd01121 142 ---LAETNLEAILAEIEELKPSLVVIDSI 167
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
26-148 |
6.87e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 43.35 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 26 LPFGRIVEIYGPESSGKTTLTLQV---VAEAQK-IGKTCA-----FIDAE---------------HALDPVYAGKLGVDI 81
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLaaaVAAGGPwLGRRVPpgkvlYLAAEddrgelrrrlkalgaDLGLPFADLDGRLRL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 290795135 82 DNLLVSQPDTGEQAlEIADALTRSGaVDVIIIDSVAALTPkaeiegemGDSHMGLQARMLSQAMRKL 148
Cdd:COG3598 90 LSLAGDLDDTDDLE-ALERAIEEEG-PDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL 146
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
216-248 |
6.87e-05 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 43.54 E-value: 6.87e-05
10 20 30
....*....|....*....|....*....|...
gi 290795135 216 VVKNKIAAPFKQAEFQIMYGEGINLYGELIDLG 248
Cdd:PRK09519 687 VVVHNCSPPFKQAEFDILYGKGISREGSLIDMG 719
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
30-123 |
4.53e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 30 RIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEH-----ALDPVYAGKLGVDIDNLLVSQPDTGeqalEIADALTR 104
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSgtspkDLLRALLRALGLPLSGRLSKEELLA----ALQQLLLA 81
|
90
....*....|....*....
gi 290795135 105 SGAVDVIIIDSVAALTPKA 123
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEA 100
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
29-118 |
4.99e-04 |
|
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: 40.02 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 29 GRIVEIYGPESSGKTTLTLQVVA---------EAQKIGKTCA--FIDAEHALDP-----VYAGKLGVDIDNLLVSQPDTG 92
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 290795135 93 EQALeIADALTR----------------------------SGAVDVIIIDSVAA 118
Cdd:cd19490 81 VEEI-ARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISA 133
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
31-117 |
1.75e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 38.46 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 31 IVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVY----------AGKLGVDIDNLLVSQPDTGEQALEIA- 99
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDPLRRYFISKldrfeevrrlAEALGIAVPKAELEESKLAFLAIELLl 101
|
90
....*....|....*...
gi 290795135 100 DALTRSGAVDVIIIDSVA 117
Cdd:pfam01637 102 EALKRRGKKIAIIIDEVQ 119
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
32-186 |
2.07e-03 |
|
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: 37.10 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 32 VEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAehaLDPVyagklgvdidnllvsqpdtgeqaLEIADALTRSGAVDVI 111
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF---LDTI-----------------------LEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290795135 112 IIDSVAALTPKAEiegemgdshmGLQARMLSQAMRKLTANIKNSNTLMIFINQIRMKIGVMFGNPETTTGGNALK 186
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
34-116 |
2.09e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.08 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 34 IYGPESSGKTTLtlqvvaeAQKIGKTcAFIDAEHALDPVYAGKLGVDIDnllvsqPDTGEQALEIADALTRSGAV--DVI 111
Cdd:pfam13479 7 IYGPSGIGKTTF-------AKTLPKP-LFLDTEKGSKALDGDRFPDIVI------RDSWQDFLDAIDELTAAELAdyKTI 72
|
....*
gi 290795135 112 IIDSV 116
Cdd:pfam13479 73 VIDTV 77
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
24-53 |
2.24e-03 |
|
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: 38.00 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|
gi 290795135 24 GGLPFGRIVEIYGPESSGKTTLTLQVVAEA 53
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANV 31
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
10-117 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290795135 10 VSTGSLSLDIALGaGGLPFGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDPVYAGKLGVDID------- 82
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERSEALGIDlramvek 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 290795135 83 -NLLVSQPDT-----GEQALEIADALTRSGAvDVIIIDSVA 117
Cdd:cd19487 80 gLLSIEQIDPaelspGEFAQRVRTSVEQEDA-RVVVIDSLN 119
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
30-48 |
8.21e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 36.34 E-value: 8.21e-03
|
| PRK08903 |
PRK08903 |
DnaA regulatory inactivator Hda; Validated |
20-71 |
8.45e-03 |
|
DnaA regulatory inactivator Hda; Validated
Pssm-ID: 236347 [Multi-domain] Cd Length: 227 Bit Score: 36.49 E-value: 8.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 290795135 20 ALGAGGLPfGRIVEIYGPESSGKTTLTLQVVAEAQKIGKTCAFIDAEHALDP 71
Cdd:PRK08903 34 ELAAGPVA-DRFFYLWGEAGSGRSHLLQALVADASYGGRNARYLDAASPLLA 84
|
|
| |
