|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-349 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 694.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 1 MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQV 80
Cdd:PRK09354 1 MAMDEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 81 IASAQRKGKTCAFIDAEHALDPVYAKKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEI 160
Cdd:PRK09354 81 IAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 161 GDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVG 240
Cdd:PRK09354 161 GDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 241 SETRVKVVKNKIAAPFKQAEFQIMYGEGINTFGELVDLGVKHKLVEKAGAWYSYNGEKIGQGKANSTNFLKENPAIANEI 320
Cdd:PRK09354 241 NRTKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEI 320
|
330 340
....*....|....*....|....*....
gi 2509134732 321 DKKLRDLLLSGEVAAADTAKISADDREEA 349
Cdd:PRK09354 321 EKKIREKLGLSAAAAEEEEEEDEEEEEEE 349
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-348 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 665.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 1 MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQV 80
Cdd:COG0468 4 KVASSEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 81 IASAQRKGKTCAFIDAEHALDPVYAKKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEI 160
Cdd:COG0468 84 IAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 161 GDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVG 240
Cdd:COG0468 164 GDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 241 SETRVKVVKNKIAAPFKQAEFQIMYGEGINTFGELVDLGVKHKLVEKAGAWYSYNGEKIGQGKANSTNFLKENPAIANEI 320
Cdd:COG0468 244 NRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEI 323
|
330 340
....*....|....*....|....*...
gi 2509134732 321 DKKLRDLLLSGEVAAADTAKISADDREE 348
Cdd:COG0468 324 EAKIREKLGLGAVSEAAAAEEEEDEEEE 351
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
6-326 |
0e+00 |
|
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: 607.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 6 NKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIASAQ 85
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 86 RKGKTCAFIDAEHALDPVYAKKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEIGDSHM 165
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 166 GLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVGSETRV 245
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 246 KVVKNKIAAPFKQAEFQIMYGEGINTFGELVDLGVKHKLVEKAGAWYSYNGEKIGQGKANSTNFLKENPAIANEIDKKLR 325
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVR 320
|
.
gi 2509134732 326 D 326
Cdd:TIGR02012 321 E 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
9-270 |
0e+00 |
|
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: 515.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 9 KALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKG 88
Cdd:pfam00154 1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 89 KTCAFIDAEHALDPVYAKKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEIGDSHMGLA 168
Cdd:pfam00154 81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 169 ARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVGSETRVKVV 248
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVV 240
|
250 260
....*....|....*....|..
gi 2509134732 249 KNKIAAPFKQAEFQIMYGEGIN 270
Cdd:pfam00154 241 KNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
37-270 |
2.85e-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: 465.88 E-value: 2.85e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 37 DVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVYAKKLGVDIDNLL 116
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 117 CSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQI 196
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509134732 197 RMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVGSETRVKVVKNKIAAPFKQAEFQIMYGEGIN 270
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGIS 234
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-254 |
5.68e-116 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 354.40 E-value: 5.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 1 MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQV 80
Cdd:PRK09519 1 MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 81 IASAQRKGKTCAFIDAEHALDPVYAKKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIEGEI 160
Cdd:PRK09519 81 VANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 161 GDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAIKEGDEVVG 240
Cdd:PRK09519 161 GDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVG 240
|
250
....*....|....
gi 2509134732 241 SETRVKVVKNKIAA 254
Cdd:PRK09519 241 NRTRVKVVKNKCLA 254
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
60-228 |
2.98e-61 |
|
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: 194.49 E-value: 2.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 60 GRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVYA-----------KKLGVDIDNLLCSQPDTGEQALE 128
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 129 ICDALARSGA----VDVIIVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMF 204
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 2509134732 205 G-NPETTTGGNALKFYASVRLDIRR 228
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
247-339 |
3.86e-24 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 103.63 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 247 VVKNKIAAPFKQAEFQIMYGEGINTFGELVDLGVKHKLVEKAGAWYSYNGEKIGQGKANSTNFLKENPAIANEIDKKLRD 326
Cdd:PRK09519 687 VVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKE 766
|
90
....*....|...
gi 2509134732 327 LLLSGEVAAADTA 339
Cdd:PRK09519 767 KLGIGAVVTDDPS 779
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
41-263 |
1.08e-19 |
|
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: 86.21 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEhALDP-----VYAKKLGVDIDNL 115
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 116 LCSQP-DTGEQALEICDA--LARSGAVDVIIVDSVAALTpKAEIEGEIGdshmglAARMMSQAMRKLAGNLKQSNTLLIF 192
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLELGDDSE------ANRELSRQMSKLLSIARKYDIPVVI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509134732 193 INQIRMKIGVMFGNPettTGGNALKfYASvrldirriGAIKEGDEVVGSETRVKVVKNKIAAPFKQAEFQI 263
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLE-HWS--------KAIIRLEKSPPGLRRATLEKHRSRPEGQSAGFRI 210
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
41-269 |
2.10e-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: 75.03 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQ-------RKGKtCAFIDAEHALDPV----YAKKLG 109
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLCHTLCVTCQlplemggGEGK-ALYIDTEGTFRPErlvaIAERYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 110 VD----IDNLLCSQPDTGEQALEICDALAR---SGAVDVIIVDSVAALTpKAEIE--GEIGDSHMGLAARMMSqaMRKLA 180
Cdd:pfam08423 97 LDpedvLDNVAYARAYNSEHQMQLLQQAAAmmsESRFALLIVDSATALY-RTDFSgrGELAERQQHLAKFLRT--LQRLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 181 gnlKQSNTLLIFINQIRMKIG---VMF-GNPETTTGGNALKFYASVRLDIRRigaiKEGdevvgsETRVKVVKNKIAAPF 256
Cdd:pfam08423 174 ---DEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK----GRG------EQRICKIYDSPCLPE 240
|
250
....*....|...
gi 2509134732 257 KQAEFQImYGEGI 269
Cdd:pfam08423 241 SEAVFAI-GSGGI 252
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
24-154 |
1.32e-14 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 72.27 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 24 KGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPE-SSGKTTLTLQVIASAQRKGKTCAFIDAEHALdp 102
Cdd:COG4544 12 RRRIWRGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL-- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2509134732 103 vYA---KKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIIVDsVAALTPKA 154
Cdd:COG4544 90 -YApglAAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
41-208 |
1.29e-13 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 69.17 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPV--YAKKLGVDIDNLLCS 118
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 119 -------------QPDTGEQALEICDALARSGAvDVIIVDSVAALTPKAEIEGEIgdshmglaaRMMsqaMRKLAGNLKQ 185
Cdd:COG0467 81 gllriidlspeelGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPERL---------REF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 2509134732 186 SNTLLIFINQIRMKIGVMFGNPE 208
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
41-228 |
1.46e-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: 69.48 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IASAQRKGKtCAFIDAEHALDPV----YAKKLG 109
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVtcqlpIDRGGGEGK-AIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 110 VD----IDNLLCSQPDTGEQALEICDALA---RSGAVDVIIVDSVAALTPKAEI-EGEIGDSHMGLaARMMSqAMRKLAg 181
Cdd:cd01123 79 LDpddvLDNVAYARAFNSDHQTQLLDQAAammVESRFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLR-MLQRLA- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2509134732 182 nlKQSNTLLIFINQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 228
Cdd:cd01123 156 --DEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
41-270 |
3.38e-13 |
|
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: 68.15 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQVIASAQRK-----GKTCaFIDAEHALDP----VYAKKLG 109
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 110 VD----IDNLLCSQPDTGEQALEICDALARSGAVD----VIIVDSVAAL-----TPKaeieGEIGDSHMGLaARMMSQaM 176
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMALfrvdfSGR----GELAERQQKL-AQMLSR-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 177 RKLAgnlKQSNTLLIFINQIRMKIG--VMF-GNPETTTGGNALKFYASVRLDIRRIGAikegdevvgsETRVKVVKNKIA 253
Cdd:cd19514 153 QKIS---EEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRKGRG----------EERIAKIYDSPD 219
|
250
....*....|....*..
gi 2509134732 254 APFKQAEFQIMYGeGIN 270
Cdd:cd19514 220 LPENEATFAITAG-GIA 235
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
48-201 |
1.70e-12 |
|
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: 65.90 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 48 LDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEhALDPVYAKKLGVD-----IDNLLCSQP-D 121
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 122 TGEQALEICDA--LARSGAVDVIIVDSVAALTpKAEIEGEIGDSHMGLAARMmsQAMRKLAgnlKQSNTLLIFINQIRMK 199
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLA---RKKNLAVVITNQVYTD 152
|
..
gi 2509134732 200 IG 201
Cdd:TIGR02237 153 VN 154
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
39-263 |
7.29e-12 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 64.11 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 39 ETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEhALDPVYAKKLGVD-----ID 113
Cdd:PRK09361 3 ERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIAGEdfeelLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 114 NLLCSQP-DTGEQALEICDALARSGA-VDVIIVDSVAALTpKAEIEgEIGDShmGLAARMMSQAMRKLAGNLKQSNTLLI 191
Cdd:PRK09361 81 NIIIFEPsSFEEQSEAIRKAEKLAKEnVGLIVLDSATSLY-RLELE-DEEDN--SKLNRELGRQLTHLLKLARKHDLAVV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2509134732 192 FINQIRMKIGvmfGNPETTTGGNALKfYASvrldirriGAIKEGDEVVGSETRVKVVKNKIAAPFKQAEFQI 263
Cdd:PRK09361 157 ITNQVYSDID---SDGLRPLGGHTLE-HWS--------KTILRLEKFRNGKRRATLEKHRSRPEGESAEFRI 216
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
32-228 |
1.88e-11 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 64.13 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 32 EDRSMDVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQR------KGKTCAFIDAEHALDP--- 102
Cdd:PRK04301 75 LERRKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRPeri 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 103 -VYAKKLGVDIDNLLCS-----------QPDTGEQALEICdalARSGAVDVIIVDSVAALTpKAEIEGEiGDshmgLAAR 170
Cdd:PRK04301 154 eQMAEALGLDPDEVLDNihvaraynsdhQMLLAEKAEELI---KEGENIKLVIVDSLTAHF-RAEYVGR-GN----LAER 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509134732 171 M------MSQAMRklAGNLkqSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 228
Cdd:PRK04301 225 QqklnkhLHDLLR--LADL--YNAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
60-229 |
4.36e-11 |
|
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: 60.46 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 60 GRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVYAKKLGVDIDNLLCSqpDTGEQALEICDALARSGAV 139
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 140 DVIIVDSVAALTPKAEiegeigdshmgLAARMMSQAMRKLAGNLKQSNTLLIFINqirmkigvmfgNPETTTGGNALKFY 219
Cdd:smart00382 80 DVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRRR 137
|
170
....*....|
gi 2509134732 220 ASVRLDIRRI 229
Cdd:smart00382 138 FDRRIVLLLI 147
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
49-250 |
9.85e-11 |
|
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: 60.80 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 49 DIALGaGGLPMGRIVEIYGPESSGKT----TLTLQVIASAQRKGKT--CAFIDAEHAL------------DPVYAKK--- 107
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDggVLYIDTESKFsaerlaeiaearFPEAFSGfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 108 ----LGVDIDNLLCSQPDTGEQALEICDAL---ARSGAVDVIIVDSVAALTPKA--EIEGEIGDSHMGLaARMMSqAMRK 178
Cdd:cd19493 80 enerAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS-SLKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2509134732 179 LAgnlKQSNTLLIFINQIRMKIGVMFGNPETTTG--GNALKFYASVRLDIRRIgaikegdevVGSETRV-KVVKN 250
Cdd:cd19493 158 LA---EEFRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERC---------LLQLRRVlEIVKS 220
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
3-266 |
1.27e-10 |
|
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: 61.72 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 3 IDENKQKALAAALGQIEkQFGKGSIMRLGEDRSMdVETISTGSLSLDIALGAGGLPMGrIVEIYGPESSGKTTL--TLQV 80
Cdd:TIGR02238 42 LSEAKVDKIKEAASKII-NPGFITAFEISQKRKK-VLKITTGSQALDGILGGGIESMS-ITEVFGEFRCGKTQLshTLCV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 81 IASAQRKGK----TCAFIDAEHALDP----VYAKKLGVD----IDNLLCSQPDTGEQALEICDALARSGAVD---VIIVD 145
Cdd:TIGR02238 119 TAQLPREMGggngKVAYIDTEGTFRPdrirAIAERFGVDpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 146 SVAAL-TPKAEIEGEIGDSHMGLaARMMSQaMRKLAgnlKQSNTLLIFINQIRMKIG--VMF-GNPETTTGGNALKFYAS 221
Cdd:TIGR02238 199 SIMALfRVDFSGRGELSERQQKL-AQMLSR-LNKIS---EEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHAST 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2509134732 222 VRLDIRRigaiKEGDEvvgsetRVKVVKNKIAAPFKQAEFQIMYG 266
Cdd:TIGR02238 274 TRILLRK----GRGEE------RVAKLYDSPDMPEAEASFQITEG 308
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
41-228 |
2.80e-10 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 60.78 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQVIAS-----AQRKGKtCAFIDAEHALDP----VYAKKLG 109
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGK-VLYIDTEGTFRPerivQIAERFG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 110 VD----IDNLLCSQPDTGEQALEICDALARSGAVD---VIIVDSVAALTpkaEIE----GEIGDSHMGLaARMMSqAMRK 178
Cdd:PTZ00035 178 LDpedvLDNIAYARAYNHEHQMQLLSQAAAKMAEErfaLLIVDSATALF---RVDysgrGELAERQQHL-GKFLR-ALQK 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2509134732 179 LAgnlKQSNTLLIFINQIRMKIG---VMFGNPETTTGGNALKFYASVRLDIRR 228
Cdd:PTZ00035 253 LA---DEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
34-272 |
5.64e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 59.79 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 34 RSMDVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQ---RKGKTC---AFIDAEHALDP----V 103
Cdd:PLN03187 101 KRKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLAHTLCVTTQlptEMGGGNgkvAYIDTEGTFRPdrivP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 104 YAKKLGVD----IDNLLCSQPDTGEQALEICDALARSGAVD---VIIVDSVAALTPKAEI-EGEIGDSHMGLaARMMSQa 175
Cdd:PLN03187 180 IAERFGMDadavLDNIIYARAYTYEHQYNLLLGLAAKMAEEpfrLLIVDSVIALFRVDFTgRGELAERQQKL-AQMLSR- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 176 MRKLAgnlKQSNTLLIFINQIRMKIG--VMFGNPETTTGGNALKFYASVRLDIRRIGAikegdevvgsETRVKVVKNKIA 253
Cdd:PLN03187 258 LTKIA---EEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRKGKG----------EQRVCKVFDAPN 324
|
250
....*....|....*....
gi 2509134732 254 APFKQAEFQIMYGeGINTF 272
Cdd:PLN03187 325 LPEAEAEFQITSG-GIMDA 342
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
41-228 |
1.08e-09 |
|
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: 58.10 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IASAQRKGKtCAFIDAEHALDPV----YAKKLG 109
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 110 VD----IDNLLCSQP---DTGEQALEICDALARSGAVDVIIVDSVAALTpKAEIEGEiGDshmgLAARMM--SQAMRKLA 180
Cdd:cd19513 79 LNgedvLDNVAYARAyntDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2509134732 181 GNLKQSNTLLIFINQIRMKI--GVMF-GNPETTTGGNALKFYASVRLDIRR 228
Cdd:cd19513 153 RLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
41-228 |
2.90e-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: 56.60 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRK------GKTCAFIDAEHALDP----VYAKKLGV 110
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPpeegglNGKAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 111 DIDNLL-----CSQPDTGEQAL---EICDALARSGAVDVIIVDSVAALTpKAEI--EGEIGDSHMGLAaRMMSQAMRklA 180
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKLN-KHLHDLHR--L 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2509134732 181 GNLkqSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRR 228
Cdd:cd19515 156 ADL--YNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
41-230 |
5.01e-09 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 56.10 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQ-VIASAQRKGKTCAFIDA-EHALDPVY-AKKLGVDIDNLLc 117
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 118 sqpDTGEqaLEICDALA-RSGAVDVIIVDSVAALTPK-AEIEGEIG------DSHMGLAAR----MMSQAMRKLAGNLKQ 185
Cdd:pfam06745 79 ---EEGK--LAIIDASTsGIGIAEVEDRFDLEELIERlREAIREIGakrvviDSITTLFYLlkpaVAREILRRLKRVLKG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2509134732 186 SNTLLIFINQIRMKigvmfgnpETTTGGNALKFYAS---VRLDIRRIG 230
Cdd:pfam06745 154 LGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIE 193
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
48-196 |
1.28e-08 |
|
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: 54.99 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 48 LDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQR------KGKTCAFIDAEHAL-------------DPVYAKKL 108
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelggLGGGAVYICTESSFpskrlqqlasslpKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 109 GVDIDN-LLCSQPDTgeQALEIC-----DALARSGAVDVIIVDSVAALtpkaeIEGEIGDSHMGLAARmmSQAMRKLAGN 182
Cdd:cd19491 80 KNFLDNiFVEHVADL--ETLEHClnyqlPALLERGPIRLVVIDSIAAL-----FRSEFDTSRSDLVER--AKYLRRLADH 150
|
170
....*....|....*...
gi 2509134732 183 LKQ----SNTLLIFINQI 196
Cdd:cd19491 151 LKRladkYNLAVVVVNQV 168
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
34-274 |
4.41e-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: 53.96 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 34 RSMDVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTL--TLQV-----IASAQRKGKtCAFIDAEHALDPV--- 103
Cdd:TIGR02239 71 RRQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErll 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 104 -YAKKLGVD----IDNLLCSQPDTGEQALEICD---ALARSGAVDVIIVDSVAALTpKAEIEGEiGDshmgLAARMMSQA 175
Cdd:TIGR02239 149 aIAERYGLNpedvLDNVAYARAYNTDHQLQLLQqaaAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 176 --MRKLAGNLKQSNTLLIFINQIRMKI---GVMF-GNPETTTGGNALKFYASVRLDIRRigaiKEGdevvgsETRVKVVK 249
Cdd:TIGR02239 223 rfLRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK----GRG------EQRICKIY 292
|
250 260
....*....|....*....|....*
gi 2509134732 250 NKIAAPFKQAEFQImYGEGINTFGE 274
Cdd:TIGR02239 293 DSPCLPESEAMFAI-YEDGIGDPKE 316
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
37-269 |
1.41e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 52.43 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 37 DVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQ-------RKGKtCAFIDAEHALDP----VYA 105
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLCHTLCVTCQlpldqggGEGK-AMYIDTEGTFRPqrliQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 106 KKLGVD----IDNLLCSQPDTGEQALEICDALARSGA---VDVIIVDSVAALTpKAEIEGEiGDshmgLAARMMSQA--M 176
Cdd:PLN03186 179 ERFGLNgadvLENVAYARAYNTDHQSELLLEAASMMAetrFALMIVDSATALY-RTEFSGR-GE----LSARQMHLGkfL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 177 RKLAGNLKQSNTLLIFINQIRMKI--GVMFGNPETT-TGGNALKFYASVRLdirrigAIKEGDevvgSETRVKVVKNKIA 253
Cdd:PLN03186 253 RSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRL------ALRKGR----GENRICKVISSPC 322
|
250
....*....|....*.
gi 2509134732 254 APFKQAEFQIMyGEGI 269
Cdd:PLN03186 323 LPEAEARFSIS-SEGV 337
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
41-197 |
2.82e-07 |
|
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: 50.73 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVY--AKKLGVDID----- 113
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 114 -NLLCSQPDTGEQALEICDALA-------RSGAVDVIIVDSVAALTPKAEiegeigdshmglAARMMSQAMRKLAGNLKQ 185
Cdd:cd01124 80 gKLIIVDAPPTEAGRFSLDELLsrilsiiKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 2509134732 186 SNTLLIFINQIR 197
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
28-147 |
1.26e-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: 49.07 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 28 MRLGEDRSMDVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPV--YA 105
Cdd:cd01121 51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2509134732 106 KKLGVDIDNLLCsqpdTGEQALEICDALARSGAVDVIIVDSV 147
Cdd:cd01121 130 ERLGLGSDNLYL----LAETNLEAILAEIEELKPSLVVIDSI 167
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
41-115 |
2.47e-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: 47.73 E-value: 2.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFI---DAEHALDPVyAKKLGVDIDNL 115
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAV-ALSHGWSLDGI 76
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
39-151 |
1.63e-05 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 45.59 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 39 ETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHA----LDPVYAkkLGVDID- 113
Cdd:COG2874 1 EIISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTtkefIKQMKS--LSYDISd 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2509134732 114 ------------NLLCSQPDTGE-----QALEICDALARSGAvDVIIVDSVAALT 151
Cdd:COG2874 78 yllrgrllflpvHPLGFEWNSKQrkdllKRLMKYIASNLWEA-DVIIIDSLSALL 131
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
60-201 |
2.42e-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: 45.03 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 60 GRIVEIYGPESSGKTTLTLQVIASA----QRKGKTCA-------FIDAEHALDP-----VYAKKLGVDIDNLLCSQPDTG 123
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpsSWGGVPLGgleaavvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 124 -EQALEIC--------------------------DALARSGAVDVIIVDSVAALTPKAEIEGEIGdshmGLAARMMSQAM 176
Cdd:cd19490 81 vEEIAREClqrlhifrchsslqllatllslenylLSLSANPELGLLLIDSISAFYWQDRFSAELA----RAAPLLQEAAL 156
|
170 180
....*....|....*....|....*....
gi 2509134732 177 RKLAGNLKQS----NTLLIFINQIRMKIG 201
Cdd:cd19490 157 RAILRELRRLrrrfQLVVIATKQALFPGK 185
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
57-180 |
2.87e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 45.28 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 57 LPMGRIVEIYGPESSGKTTLTLQVIASA---------QRKGKTCAFIDAE---------------HALDPVYAKKLGVDI 112
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEddrgelrrrlkalgaDLGLPFADLDGRLRL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134732 113 DNLLCSQPDTGE-QALEicdALARSGAVDVIIVDSVAALTPkaeiegeiGDSHMGLAARMMSQAMRKLA 180
Cdd:COG3598 90 LSLAGDLDDTDDlEALE---RAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRLA 147
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
37-157 |
3.15e-05 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 44.58 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 37 DVETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAE--------------HALDP 102
Cdd:PRK06067 3 KKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTEntsksylkqmesvkIDISD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2509134732 103 VYAK-KLGVDIDNLLCSQ--PDTGEQALEICDALARSGAVDVIIVDSVAALTPKAEIE 157
Cdd:PRK06067 82 FFLWgYLRIFPLNTEGFEwnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
41-151 |
3.18e-05 |
|
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: 44.63 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 41 ISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVY--AKKLGVD-----ID 113
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDleqmeRK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2509134732 114 NLL---CSQPDTG--EQALEICDALARSGAVDVIIVDSVAALT 151
Cdd:cd19484 81 GLLkiiCARPELYglEDHLIIIKSEINEFKPSRVIVDPLSALA 123
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
55-180 |
3.80e-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: 44.16 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 55 GGLPMGRIVEIYGPESSGKTTLTLQVIAS-AQRKGKTCAFIDAEHALdpvYAKKLGvdidNLLCSQPDTGEQALEICDAL 133
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANvASRSGQNVLYIDTKSSF---SARRLA----QILKSRAQDAEEIDKALQRI 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509134732 134 ARSGAVD---------------------------VIIVDSVAAL-TPkaeIEGeiGDSHMGLAARMMSQA--MRKLA 180
Cdd:cd19489 75 RVVRVFDpyelldlleelrntlsqqqenlysrlkLVIIDSLSALiSP---LLG--GSKHSEGHALLASLArlLKKLA 146
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
61-154 |
1.74e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.79 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 61 RIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEH-----ALDPVYAKKLGVDIDNLLCSQPDTGeqalEICDALAR 135
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSgtspkDLLRALLRALGLPLSGRLSKEELLA----ALQQLLLA 81
|
90
....*....|....*....
gi 2509134732 136 SGAVDVIIVDSVAALTPKA 154
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEA 100
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
59-179 |
1.21e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 39.62 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 59 MGRIVEIYGPESSGKTTLtlqvIASAQRKgktcAFIDAEHALDPVYAKKlGVDIDNllcsqPDTGEQALEICDALARSGA 138
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTF----AKTLPKP----LFLDTEKGSKALDGDR-FPDIVI-----RDSWQDFLDAIDELTAAEL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2509134732 139 V--DVIIVDSVAALTP--------KAEIEGEIGDSHM----GLAARMMSQAMRKL 179
Cdd:pfam13479 67 AdyKTIVIDTVDWLERlclayickQNGKGSSIEDGGYgkgyGELGEEFRRLLDAL 121
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
39-151 |
1.39e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.25 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134732 39 ETISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVY--AKKLGVDI---- 112
Cdd:PRK09302 253 ERISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIrnARSWGIDLekme 331
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2509134732 113 -DNLL---CSQPD-TG-EQALEICDALARSGAVDVIIVDSVAALT 151
Cdd:PRK09302 332 eKGLLkiiCARPEsYGlEDHLIIIKREIEEFKPSRVAIDPLSALA 376
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
41-112 |
4.87e-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: 38.05 E-value: 4.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509134732 41 ISTGSLSLDIALGaGGLPMGRIVEIYGPESSGKTTLTLQVIASAQRKGKTCAFIDAEHALDPVY--AKKLGVDI 112
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFerSEALGIDL 73
|
|
| PAXNEB |
pfam05625 |
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is ... |
40-75 |
8.23e-03 |
|
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is an RNA polymerase II Elongator protein subunit. It is part of the HAP subcomplex of Elongator, which is a six-subunit component of the RNA polymerase II holoenzyme. The HAP subcomplex is required for Elongator structural integrity and histone acetyltransferase activity. This protein family has a P-loop-like motif and adopts a RecA-ATPase-like fold, lacking the conserved sequence signature of ATPases.
Pssm-ID: 461696 Cd Length: 359 Bit Score: 37.96 E-value: 8.23e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2509134732 40 TISTGSLSLDIALGaGGLPMGRIVEIygpESSGKTT 75
Cdd:pfam05625 18 TTSTGTPSLDKLLG-GGLPLGSSLLI---EEDGTTD 49
|
|
| |
