|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-215 |
1.40e-176 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 487.76 E-value: 1.40e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:PRK09354 41 ISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:PRK09354 121 DTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKI 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAAP 215
Cdd:PRK09354 201 GVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPP 255
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-215 |
4.02e-170 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 471.19 E-value: 4.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:COG0468 44 ISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:COG0468 124 DTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKI 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAAP 215
Cdd:COG0468 204 GVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPP 258
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-215 |
5.05e-158 |
|
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: 439.50 E-value: 5.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:TIGR02012 36 ISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:TIGR02012 116 DTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTTAIFINQIREKI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAAP 215
Cdd:TIGR02012 196 GVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPP 250
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-215 |
2.87e-155 |
|
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: 430.28 E-value: 2.87e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:pfam00154 33 ISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:pfam00154 113 DTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTTVIFINQIREKI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAAP 215
Cdd:pfam00154 193 GVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPP 247
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
1-215 |
1.32e-154 |
|
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: 427.74 E-value: 1.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:cd00983 5 IPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLVSQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:cd00983 85 DTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLREKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAAP 215
Cdd:cd00983 165 GVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPP 219
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-214 |
1.12e-103 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 316.26 E-value: 1.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQP 80
Cdd:PRK09519 41 IPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 81 DTGEQALEICDALSRSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKI 160
Cdd:PRK09519 121 DTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKI 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 405779587 161 GVMFGNPETTTGGNALKFYASVRLDIRRTGSVKNSDEVVGSETRVKVVKNKVAA 214
Cdd:PRK09519 201 GVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCLA 254
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
20-188 |
1.37e-60 |
|
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: 187.56 E-value: 1.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 20 GRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYA-----------KKLGVDIDNLLCSQPDTGEQALE 88
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 89 ICDALSRSGA----VDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKNSNTLLIFINQIRMKIGVMF 164
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 405779587 165 G-NPETTTGGNALKFYASVRLDIRR 188
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
1-191 |
1.21e-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: 80.44 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEhALDP-----VYAKKLGVDIDNL 75
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 76 LCSQP-DTGEQALEICDA--LSRSGAVDVIVVDSVAALTpKAEIEGEIGdshmglAARMMSQAMRKLAGNLKNSNTLLIF 152
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLELGDDSE------ANRELSRQMSKLLSIARKYDIPVVI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 405779587 153 INQIRMKIGVMFGNPettTGGNALKfYAS---VRLDIRRTGS 191
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLE-HWSkaiIRLEKSPPGL 189
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
1-168 |
2.94e-15 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 71.49 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPV--YAKKLGVDIDNLLCS 78
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 79 -------------QPDTGEQALEICDALSRSGAvDVIVVDSVAALTPKAEIEGEIgdshmglaaRMMsqaMRKLAGNLKN 145
Cdd:COG0467 81 gllriidlspeelGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPERL---------REF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 405779587 146 SNTLLIFINQIRMKIGVMFGNPE 168
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
1-188 |
4.51e-15 |
|
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: 71.56 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQ-------REGRtCAFIDAEHALDPV----YAKKLG 69
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLCHTLCVTCQlplemggGEGK-ALYIDTEGTFRPErlvaIAERYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICDALSR---SGAVDVIVVDSVAALTpKAEIE--GEIGDSHMGLAARMMSqaMRKLA 140
Cdd:pfam08423 97 LDpedvLDNVAYARAYNSEHQMQLLQQAAAmmsESRFALLIVDSATALY-RTDFSgrGELAERQQHLAKFLRT--LQRLA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 405779587 141 GNLknsNTLLIFINQIRMKIG---VMF-GNPETTTGGNALKFYASVRLDIRR 188
Cdd:pfam08423 174 DEF---GVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
1-114 |
5.91e-15 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 70.73 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPE-SSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSQ 79
Cdd:COG4544 29 LPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPERLLLVR 108
|
90 100 110
....*....|....*....|....*....|....*.
gi 405779587 80 PDTGEQALEIC-DALsRSGAVDVIVVDsVAALTPKA 114
Cdd:COG4544 109 ARRPADALWAAeEAL-RSGACGAVVAW-LERLDLTA 142
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
1-188 |
1.09e-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: 67.56 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IAAAQREGRtCAFIDAEHALDPV----YAKKLG 69
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVtcqlpIDRGGGEGK-AIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICDALS---RSGAVDVIVVDSVAALTPKAEI-EGEIGDSHMGLaARMMSQAMRklag 141
Cdd:cd01123 79 LDpddvLDNVAYARAFNSDHQTQLLDQAAammVESRFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLRMLQR---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 405779587 142 nLKNSNTLLIFI-NQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 188
Cdd:cd01123 154 -LADEFGVAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
1-188 |
5.14e-12 |
|
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: 62.76 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQVIAAAQRE-----GRTCaFIDAEHALDP----VYAKKLG 69
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICDALSRSGAVD----VIVVDSVAAL-----TPKaeieGEIGDSHMGLaARMMSQaM 136
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMALfrvdfSGR----GELAERQQKL-AQMLSR-L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 405779587 137 RKLAgnlKNSNTLLIFINQIRMKIG--VMF-GNPETTTGGNALKFYASVRLDIRR 188
Cdd:cd19514 153 QKIS---EEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK 204
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
8-161 |
2.20e-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: 60.89 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 8 LDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEhALDPVYAKKLGVD-----IDNLLCSQP-D 81
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 82 TGEQALEICDALS--RSGAVDVIVVDSVAALTpKAEIEGEIGDSHMGLAARMmsQAMRKLAgnlKNSNTLLIFINQIRMK 159
Cdd:TIGR02237 79 FDEQGVAIQKTSKfiDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLA---RKKNLAVVITNQVYTD 152
|
..
gi 405779587 160 IG 161
Cdd:TIGR02237 153 VN 154
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
1-188 |
2.86e-11 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 61.43 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQR-------EGRtCAFIDAEHALDP----VYAKKLG 69
Cdd:PRK04301 84 ITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekgglEGK-AVYIDTEGTFRPerieQMAEALG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VDIDNLLCS-----------QPDTGEQALEICdalSRSGAVDVIVVDSVAALTpKAEIEGEiGDshmgLAARM------M 132
Cdd:PRK04301 162 LDPDEVLDNihvaraynsdhQMLLAEKAEELI---KEGENIKLVIVDSLTAHF-RAEYVGR-GN----LAERQqklnkhL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 405779587 133 SQAMRklAGNLknSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 188
Cdd:PRK04301 233 HDLLR--LADL--YNAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
1-161 |
3.32e-11 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 60.26 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEhALDPVYAKKLGVD-----IDNL 75
Cdd:PRK09361 5 LPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIAGEdfeelLSNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 76 LCSQP-DTGEQALEICDALSRSGA-VDVIVVDSVAALTpKAEIEgEIGDShmGLAARMMSQAMRKLAGNLKNSNTLLIFI 153
Cdd:PRK09361 83 IIFEPsSFEEQSEAIRKAEKLAKEnVGLIVLDSATSLY-RLELE-DEEDN--SKLNRELGRQLTHLLKLARKHDLAVVIT 158
|
....*...
gi 405779587 154 NQIRMKIG 161
Cdd:PRK09361 159 NQVYSDID 166
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
9-210 |
1.46e-10 |
|
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: 58.49 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 9 DIALGaGGLPMGRIVEIYGPESSGKT----TLTLQVIAAAQREGRT--CAFIDAEHAL------------DPVYAKK--- 67
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDggVLYIDTESKFsaerlaeiaearFPEAFSGfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 68 ----LGVDIDNLLCSQPDTGEQALEICDAL----SRSGaVDVIVVDSVAALTPKA--EIEGEIGDSHMGLAARMmsQAMR 137
Cdd:cd19493 80 enerAEEMLKRVAVVRVTTLAQLLERLPNLeehiLSSG-VRLVVIDSIAALVRREfgGSDGEVTERHNALAREA--SSLK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405779587 138 KLAgnlKNSNTLLIFINQIRMKIGVMFGNPETTTG--GNALKFYASVRLDIRRTGSvknsdevvgSETRV-KVVKN 210
Cdd:cd19493 157 RLA---EEFRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL---------QLRRVlEIVKS 220
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
1-188 |
2.13e-10 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 59.24 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQVIAA-----AQREGRtCAFIDAEHALDP----VYAKKLG 69
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGK-VLYIDTEGTFRPerivQIAERFG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICDALSRSGAVD---VIVVDSVAALTpkaEIE----GEIGDSHMGLaARMMSqAMRK 138
Cdd:PTZ00035 178 LDpedvLDNIAYARAYNHEHQMQLLSQAAAKMAEErfaLLIVDSATALF---RVDysgrGELAERQQHL-GKFLR-ALQK 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 405779587 139 LAGNLknsNTLLIFINQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 188
Cdd:PTZ00035 253 LADEF---NVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
1-188 |
2.80e-10 |
|
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: 58.14 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQR------EGRTCAFIDAEHALDP----VYAKKLGV 70
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 71 DIDNLL-----CSQPDTGEQAL---EICDALSRSGAVDVIVVDSVAALTpKAEI--EGEIGDSHMGLAaRMMSQAMRklA 140
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKLN-KHLHDLHR--L 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 405779587 141 GNLKNsntLLIFI-NQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 188
Cdd:cd19515 156 ADLYN---IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
1-188 |
5.57e-10 |
|
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: 57.33 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IAAAQREGRtCAFIDAEHALDPV----YAKKLG 69
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQP---DTGEQALEICDALSRSGAVDVIVVDSVAALTpKAEIEGEiGDshmgLAARMM--SQAMRKLA 140
Cdd:cd19513 79 LNgedvLDNVAYARAyntDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 405779587 141 gNLKNSNTLLIFI-NQIRMKI--GVMF-GNPETTTGGNALKFYASVRLDIRR 188
Cdd:cd19513 153 -RLADEFGVAVVItNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
1-188 |
2.61e-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: 55.94 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGrIVEIYGPESSGKTTL--TLQVIAAAQREGR----TCAFIDAEHALDP----VYAKKLGV 70
Cdd:TIGR02238 78 ITTGSQALDGILGGGIESMS-ITEVFGEFRCGKTQLshTLCVTAQLPREMGggngKVAYIDTEGTFRPdrirAIAERFGV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 71 D----IDNLLCSQPDTGEQALEICDALSRSGAVD---VIVVDSVAAL-TPKAEIEGEIGDSHMGLaARMMSQaMRKLAgn 142
Cdd:TIGR02238 157 DpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMALfRVDFSGRGELSERQQKL-AQMLSR-LNKIS-- 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 405779587 143 lKNSNTLLIFINQIRMKIG--VMF-GNPETTTGGNALKFYASVRLDIRR 188
Cdd:TIGR02238 233 -EEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK 280
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
1-188 |
3.55e-09 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 55.55 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQVIAA-AQREGRTC---AFIDAEHALDP----VYAKKLGV 70
Cdd:PLN03187 108 ITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQlPTEMGGGNgkvAYIDTEGTFRPdrivPIAERFGM 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 71 D----IDNLLCSQPDTGEQALEICDALSRSGAVD---VIVVDSVAALTPKAEI-EGEIGDSHMGLaARMMSQaMRKLAGN 142
Cdd:PLN03187 187 DadavLDNIIYARAYTYEHQYNLLLGLAAKMAEEpfrLLIVDSVIALFRVDFTgRGELAERQQKL-AQMLSR-LTKIAEE 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 405779587 143 LknsNTLLIFINQIRMKIG--VMFGNPETTTGGNALKFYASVRLDIRR 188
Cdd:PLN03187 265 F---NVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
20-188 |
7.64e-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: 52.76 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 20 GRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVYAKKLGVDIDNLLCSqpDTGEQALEICDALSRSGAV 99
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 100 DVIVVDSVAALTPKAEiegeigdshmgLAARMMSQAMRKLAGNLKNSNTLLIFINqirmkigvmfgNPETTTGGNALKFY 179
Cdd:smart00382 80 DVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRRR 137
|
....*....
gi 405779587 180 ASVRLDIRR 188
Cdd:smart00382 138 FDRRIVLLL 146
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
1-192 |
1.61e-08 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 53.02 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQ-VIAAAQREGRTCAFIDA-EHALDPVY-AKKLGVDIDNLLc 77
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 78 sqpDTGEqaLEICDAL-SRSGAVDVIVVDSVAALTPK-AEIEGEIG------DSHMGLAAR----MMSQAMRKLAGNLKN 145
Cdd:pfam06745 79 ---EEGK--LAIIDAStSGIGIAEVEDRFDLEELIERlREAIREIGakrvviDSITTLFYLlkpaVAREILRRLKRVLKG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 405779587 146 SNTLLIFINQIRMKigvmfgnpETTTGGNALKFYAS---VRLDIRRTGSV 192
Cdd:pfam06745 154 LGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEEE 195
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
1-157 |
4.84e-08 |
|
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: 51.50 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVY--AKKLGVDID----- 73
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 74 -NLLCSQPDTGEQALEICDALS-------RSGAVDVIVVDSVAALTPKAEiegeigdshmglAARMMSQAMRKLAGNLKN 145
Cdd:cd01124 80 gKLIIVDAPPTEAGRFSLDELLsrilsiiKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 405779587 146 SNTLLIFINQIR 157
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
1-188 |
4.93e-08 |
|
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: 52.03 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IAAAQREGRtCAFIDAEHALDPV----YAKKLG 69
Cdd:TIGR02239 78 LTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIAERYG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICD---ALSRSGAVDVIVVDSVAALTpKAEIEGEiGDshmgLAARMMSQA--MRKLA 140
Cdd:TIGR02239 156 LNpedvLDNVAYARAYNTDHQLQLLQqaaAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArfLRSLQ 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 405779587 141 GNLKNSNTLLIFINQIRMKI---GVMF-GNPETTTGGNALKFYASVRLDIRR 188
Cdd:TIGR02239 230 RLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
8-156 |
1.98e-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: 49.98 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 8 LDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQR------EGRTCAFIDAEHAL-------------DPVYAKKL 68
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelggLGGGAVYICTESSFpskrlqqlasslpKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 69 GVDIDN-LLCSQPDTgeQALEIC-----DALSRSGAVDVIVVDSVAALtpkaeIEGEIGDSHMGLAARmmSQAMRKLAGN 142
Cdd:cd19491 80 KNFLDNiFVEHVADL--ETLEHClnyqlPALLERGPIRLVVIDSIAAL-----FRSEFDTSRSDLVER--AKYLRRLADH 150
|
170
....*....|....*...
gi 405779587 143 LK----NSNTLLIFINQI 156
Cdd:cd19491 151 LKrladKYNLAVVVVNQV 168
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
1-201 |
2.76e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 50.12 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IAAAQREGRtCAFIDAEHALDP----VYAKKLG 69
Cdd:PLN03186 105 ITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVtcqlpLDQGGGEGK-AMYIDTEGTFRPqrliQIAERFG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 70 VD----IDNLLCSQPDTGEQALEICDALSRSGA---VDVIVVDSVAALTpKAEIEGEiGDshmgLAARMMSQA--MRKLA 140
Cdd:PLN03186 183 LNgadvLENVAYARAYNTDHQSELLLEAASMMAetrFALMIVDSATALY-RTEFSGR-GE----LSARQMHLGkfLRSLQ 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 405779587 141 GNLKNSNTLLIFINQIRMKI--GVMFGNPETT-TGGNALKFYASVRLDIRRTGSVKNSDEVVGS 201
Cdd:PLN03186 257 RLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRKGRGENRICKVISS 320
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
1-75 |
3.29e-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: 46.19 E-value: 3.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFI---DAEHALDPVyAKKLGVDIDNL 75
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAV-ALSHGWSLDGI 76
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
1-111 |
7.29e-06 |
|
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: 45.01 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVY--AKKLGVD-----ID 73
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDleqmeRK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 405779587 74 NLL---CSQPDTG--EQALEICDALSRSGAVDVIVVDSVAALT 111
Cdd:cd19484 81 GLLkiiCARPELYglEDHLIIIKSEINEFKPSRVIVDPLSALA 123
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
1-107 |
8.78e-06 |
|
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: 45.21 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPV--YAKKLGVDIDNLLCs 78
Cdd:cd01121 64 ISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSDNLYL- 141
|
90 100 110
....*....|....*....|....*....|
gi 405779587 79 qpdTGEQALE-ICDALSRSGAvDVIVVDSV 107
Cdd:cd01121 142 ---LAETNLEaILAEIEELKP-SLVVIDSI 167
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
17-140 |
1.09e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 45.28 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 17 LPMGRIVEIYGPESSGKTTLTLQVIAAA---------QREGRTCAFIDAE---------------HALDPVYAKKLGVDI 72
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEddrgelrrrlkalgaDLGLPFADLDGRLRL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405779587 73 DNLLCSQPDTGEQAlEICDALSRSGaVDVIVVDSVAALTPkaeiegeiGDSHMGLAARMMSQAMRKLA 140
Cdd:COG3598 90 LSLAGDLDDTDDLE-ALERAIEEEG-PDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLA 147
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
1-58 |
2.04e-05 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 44.05 E-value: 2.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEH 58
Cdd:COG2874 3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTEL 59
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
20-161 |
3.01e-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: 43.49 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 20 GRIVEIYGPESSGKTTLTLQVIAAA---------QREGRTCA--FIDAEHALDP-----VYAKKLGVDIDNLLCSQPDTG 83
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpsswggvPLGGLEAAvvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 84 -EQALEIC--------------------------DALSRSGAVDVIVVDSVAALTPKAEIEGEIGdshmGLAARMMSQAM 136
Cdd:cd19490 81 vEEIAREClqrlhifrchsslqllatllslenylLSLSANPELGLLLIDSISAFYWQDRFSAELA----RAAPLLQEAAL 156
|
170 180
....*....|....*....|....*....
gi 405779587 137 RKLAGNLKNS----NTLLIFINQIRMKIG 161
Cdd:cd19490 157 RAILRELRRLrrrfQLVVIATKQALFPGK 185
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
21-114 |
3.53e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.94 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 21 RIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEH-----ALDPVYAKKLGVDIDNLLCSQPDTGeqalEICDALSR 95
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSgtspkDLLRALLRALGLPLSGRLSKEELLA----ALQQLLLA 81
|
90
....*....|....*....
gi 405779587 96 SGAVDVIVVDSVAALTPKA 114
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEA 100
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
15-140 |
7.54e-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: 42.24 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 15 GGLPMGRIVEIYGPESSGKTTLTLQVIA-AAQREGRTCAFIDAEHALdpvYAKKLGvdidNLLCSQPDTGEQALEICDAL 93
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAAnVASRSGQNVLYIDTKSSF---SARRLA----QILKSRAQDAEEIDKALQRI 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 405779587 94 SRSGAVD---------------------------VIVVDSVAAL-TPkaeIEGeiGDSHMGLAARMMSQA--MRKLA 140
Cdd:cd19489 75 RVVRVFDpyelldlleelrntlsqqqenlysrlkLVIIDSLSALiSP---LLG--GSKHSEGHALLASLArlLKKLA 146
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
1-72 |
8.93e-05 |
|
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: 41.90 E-value: 8.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQ-VIAAAQREGRTCAFI-DAEHALDPVYAKKLGVDI 72
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQfAKAAAARGERSVLFSfDESIGTLFERSEALGIDL 73
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
19-170 |
1.39e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 41.16 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 19 MGRIVEIYGPESSGKTTLTLQViaaaqreGRTcAFIDAEHALDPVYAKKlGVDIDNllcsqPDTGEQALEICDALSRSGA 98
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL-------PKP-LFLDTEKGSKALDGDR-FPDIVI-----RDSWQDFLDAIDELTAAEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 99 V--DVIVVDSVAALTP--------KAEIEGEIGDSHM----GLAARMMSQAMRKLAgNLKNsNTLLIFINQIRmKIGVMF 164
Cdd:pfam13479 67 AdyKTIVIDTVDWLERlclayickQNGKGSSIEDGGYgkgyGELGEEFRRLLDALQ-ELGK-NVIFTAHAKTR-KDEDPD 143
|
....*.
gi 405779587 165 GNPETT 170
Cdd:pfam13479 144 GEKYTR 149
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
1-111 |
2.89e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.02 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDPVY--AKKLGVDI-----D 73
Cdd:PRK09302 255 ISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIrnARSWGIDLekmeeK 333
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 405779587 74 NLL---CSQPD-TG-EQALEICDALSRSGAVDVIVVDSVAALT 111
Cdd:PRK09302 334 GLLkiiCARPEsYGlEDHLIIIKREIEEFKPSRVAIDPLSALA 376
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
1-57 |
4.40e-04 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 39.96 E-value: 4.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 405779587 1 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAE 57
Cdd:PRK06067 7 ISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTE 62
|
|
| PRK08903 |
PRK08903 |
DnaA regulatory inactivator Hda; Validated |
11-62 |
2.11e-03 |
|
DnaA regulatory inactivator Hda; Validated
Pssm-ID: 236347 [Multi-domain] Cd Length: 227 Bit Score: 38.03 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 405779587 11 ALGAGGLPmGRIVEIYGPESSGKTTLTLQVIAAAQREGRTCAFIDAEHALDP 62
Cdd:PRK08903 34 ELAAGPVA-DRFFYLWGEAGSGRSHLLQALVADASYGGRNARYLDAASPLLA 84
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
17-140 |
5.75e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.59 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405779587 17 LPMGRIVEIYGPESSGKTTLTLQVIAA-----------AQREGRTCAFIDAE--------------HALDPVYAKKLGVD 71
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAAvatgkpwlggpRVPEQGKVLYVSAEgpadelrrrlraagADLDLPARLLFLSL 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 405779587 72 IDNLLCSQPDTGEQAL-----EICDALSRSGAVDVIVVDSVAALTPkaeiegeiGDSHMGLAARMMSQAMRKLA 140
Cdd:pfam13481 110 VESLPLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRLA 175
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
21-39 |
6.45e-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: 6.45e-03
|
| |
