|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-245 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 540.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLG 80
Cdd:PRK09354 30 LGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTI 160
Cdd:PRK09354 110 VDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNISKSNTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 161 AIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGI 240
Cdd:PRK09354 190 VIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDIMYGEGI 269
|
....*
gi 937962009 241 SKEGE 245
Cdd:PRK09354 270 SREGE 274
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-245 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 528.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLG 80
Cdd:COG0468 33 LGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPEYAKKLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTI 160
Cdd:COG0468 113 VDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAISKSNTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 161 AIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGI 240
Cdd:COG0468 193 VIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDIMYGEGI 272
|
....*
gi 937962009 241 SKEGE 245
Cdd:COG0468 273 SKEGE 277
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-245 |
5.28e-180 |
|
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: 496.51 E-value: 5.28e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLG 80
Cdd:TIGR02012 25 LGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYARKLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTI 160
Cdd:TIGR02012 105 VDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGALSKSNTT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 161 AIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGI 240
Cdd:TIGR02012 185 AIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFDILYGEGI 264
|
....*
gi 937962009 241 SKEGE 245
Cdd:TIGR02012 265 SKLGE 269
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-241 |
9.91e-178 |
|
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: 488.45 E-value: 9.91e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLG 80
Cdd:pfam00154 22 LGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPVYAKKLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTI 160
Cdd:pfam00154 102 VDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSISKSNTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 161 AIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGI 240
Cdd:pfam00154 182 VIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFDIMYGEGI 261
|
.
gi 937962009 241 S 241
Cdd:pfam00154 262 S 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
8-242 |
2.48e-175 |
|
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: 481.28 E-value: 2.48e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 8 RISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEELL 87
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 88 LSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQI 167
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937962009 168 REKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGISK 242
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-222 |
1.89e-116 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 350.93 E-value: 1.89e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLG 80
Cdd:PRK09519 30 LGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTI 160
Cdd:PRK09519 110 VDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937962009 161 AIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNK 222
Cdd:PRK09519 190 AIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
31-199 |
1.57e-50 |
|
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: 163.29 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 31 GRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQ-----------KLGVNIEELLLSQPDTGEQALE 99
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 100 IAEALVRSGA----VDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMF 175
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 937962009 176 G-NPETTPGGRALKFYSSVRLEVRR 199
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
12-204 |
3.86e-20 |
|
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: 85.44 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPV-YAQKLGVNIEELL--- 87
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPErFQQIAGERFESIAsni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 88 -LSQP-DTGEQALEI--AEALVRSGAVDIVVVDSVAALVpKAEiegDMGDShvGLQARLMSQaLRKLSGaINKSKTIAIF 163
Cdd:cd01394 79 iVFEPySFDEQGVAIqeAEKLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLS-IARKYDIPVV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 937962009 164 I-NQIREKvgvmFGNPETTP-GGRALKFYSSVRLEVRRAEQLK 204
Cdd:cd01394 151 ItNQVYSD----IDDDRLKPvGGTLLEHWSKAIIRLEKSPPGL 189
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
7-116 |
3.85e-16 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 74.58 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 7 TRISTVPSGSLALDTALGIGGYPRGRIIEVYGPE-SSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEE 85
Cdd:COG4544 24 AARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAAAGLDPER 103
|
90 100 110
....*....|....*....|....*....|.
gi 937962009 86 LLLSQPDTGEQALEIAEALVRSGAVDIVVVD 116
Cdd:COG4544 104 LLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
19-219 |
4.62e-16 |
|
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: 73.99 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 19 LDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPVYAQKLGVNIEELLLSQP------- 91
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNFivfevfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 92 -DTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGDMGDSHVGLQARlmsqaLRKLSGAINKSKTIAIFINQIREK 170
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 937962009 171 VgvmfGNPETTP-GGRALKFYSS--VRLE----VRRAEQLKQGNDVMGNKTKIKVV 219
Cdd:TIGR02237 153 V----NNGTLRPlGGHLLEHWSKviLRLEkfrgRRLATLEKHRSRPEGESVYFRIT 204
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
9-200 |
1.44e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 70.28 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 9 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEhALDPV-YAQKLGVNIEELL 87
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPErFKQIAGEDFEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 88 ----LSQP-DTGEQ--ALEIAEALVRSGaVDIVVVDSVAALVpKAEIEGDMGDShvGLQARLMSQaLRKLSGaINKSKTI 160
Cdd:PRK09361 80 sniiIFEPsSFEEQseAIRKAEKLAKEN-VGLIVLDSATSLY-RLELEDEEDNS--KLNRELGRQ-LTHLLK-LARKHDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 937962009 161 AIFI-NQIREKVgvmfGNPETTP-GGRALKFYSS--VRLE-----VRRA 200
Cdd:PRK09361 154 AVVItNQVYSDI----DSDGLRPlGGHTLEHWSKtiLRLEkfrngKRRA 198
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
8-202 |
1.70e-13 |
|
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: 67.71 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 8 RISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQG--GQAAFIDAEHALDPV----YAQ 77
Cdd:pfam08423 18 QITT---GSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFRPErlvaIAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 78 KLGVNIEELLLSQP-------DTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIE--GDMGDSHVGLqARLMSqALR 148
Cdd:pfam08423 94 RYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-TLQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937962009 149 KLSGAINksktIAIFI-NQIREKVG---VMF-GNPETTPGGRALKFYSSVRLEVR--RAEQ 202
Cdd:pfam08423 171 RLADEFG----VAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRkgRGEQ 227
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
12-179 |
1.41e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 61.86 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPV--YAQKLGVNIEELL-- 87
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 88 -----------LSQPDTGEQALEIAEALVRSGAvDIVVVDSVAALVPKAEIEGDmgdshvglqARLMsqaLRKLSGAINK 156
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREAVEEFGA-KRVVIDSLSGLLLALPDPER---------LREF---LHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 937962009 157 SKTIAIFINQIREKVGVMFGNPE 179
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-201 |
1.65e-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: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 30 RGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSqpDTGEQALEIAEALVRSGA 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 110 VDIVVVDSVAALVPKaeiegdmgdshVGLQARLMSQALRKLSGAINKSKTIAIFINqirekvgvmfgNPETTPGGRALKF 189
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|..
gi 937962009 190 YSSVRLEVRRAE 201
Cdd:smart00382 137 RFDRRIVLLLIL 148
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
12-202 |
7.90e-11 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 60.06 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ-------QGGQAAFIDAEHALDP----VYAQKLG 80
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLS-HTLCVTAQlpgsmggGGGKVAYIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VN----IEELLLSQPDTGEQALEI----AEALVRSGAVDIVVVDSVAALVpKAEI--EGDMGDSHVGLqARLMSQaLRKL 150
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELldyvAAKFHEEAVFRLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 937962009 151 SGAINksktIAIFI-NQIREKVG--VMF-GNPETTPGGRALKFYSSVRLEVR--RAEQ 202
Cdd:cd19514 156 SEEYN----VAVFItNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRkgRGEE 209
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
12-199 |
4.62e-10 |
|
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: 57.93 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ-------QGGQAAFIDAEHALDPV----YAQKLG 80
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLAVTCQlpidrggGEGKAIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEI-EGDMGDSHVGLqARLMSqALRKLSG 152
Cdd:cd01123 79 LDPDDVLDNvayarafNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLR-MLQRLAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 937962009 153 AINksktIAIFI-NQIREKVG---VMFGNPETTPGGRALKFYSSVRLEVRR 199
Cdd:cd01123 157 EFG----VAVVVtNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
14-202 |
2.42e-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: 55.79 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 14 SGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQGGQ--AAFIDAEHALDPV----YAQKLGVNI 83
Cdd:cd19513 3 TGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVTCQLPIDQGGGEgkALYIDTEGTFRPErllaIAERYGLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 84 EELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQARLMS-----QALRKLS 151
Cdd:cd19513 82 EDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSG-RGE----LSARQMHlakflRMLQRLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 937962009 152 GAINksktIAIFI-NQIREKV--GVMFGNPETTP-GGRALKFYSSVRLEVR--RAEQ 202
Cdd:cd19513 156 DEFG----VAVVItNQVVAQVdgAAMFAGDPKKPiGGNIMAHASTTRLYLRkgRGET 208
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
8-200 |
4.31e-09 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 55.65 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 8 RISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ---QQGG---QAAFIDAEHALDP----VYAQ 77
Cdd:PRK04301 83 KITT---GSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeEKGGlegKAVYIDTEGTFRPerieQMAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 78 KLGVNIEELL-----LSQPDTGEQAL--EIAEALVRSG-AVDIVVVDSVAALVpKAEiegdmgdsHVGL------QARLM 143
Cdd:PRK04301 159 ALGLDPDEVLdnihvARAYNSDHQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAE--------YVGRgnlaerQQKLN 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 937962009 144 SQ--ALRKLSGAINkskTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRA 200
Cdd:PRK04301 230 KHlhDLLRLADLYN---AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRKS 285
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
20-172 |
1.59e-08 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 53.48 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 20 DTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEV---QQQGGQAA---FIDAEHALDP-------------VYAQKLG 80
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampARKGGLDGgvlYIDTESKFSAerlaeiaearfpeAFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 81 VNIEELLLSQ------PDTGEQALEIAEAL---VRSGAVDIVVVDSVAALVPKA--EIEGDMGDSHVGLqARLMSqALRK 149
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRREfgGSDGEVTERHNAL-AREAS-SLKR 157
|
170 180
....*....|....*....|...
gi 937962009 150 LSgaiNKSKTIAIFINQIREKVG 172
Cdd:cd19493 158 LA---EEFRIAVLVTNQATTHFG 177
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
9-199 |
3.48e-08 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 53.20 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 9 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQG--GQAAFIDAEHALDP----VYAQK 78
Cdd:PLN03186 102 IIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGgeGKAMYIDTEGTFRPqrliQIAER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 79 LGVN----IEELLLSQPDTGEQALEI---AEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQAR--LMSQALRK 149
Cdd:PLN03186 181 FGLNgadvLENVAYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSG-RGE----LSARqmHLGKFLRS 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 937962009 150 LSgAINKSKTIAIFI-NQIREKV--GVMFGNPETTP-GGRALKFYSSVRLEVRR 199
Cdd:PLN03186 255 LQ-RLADEFGVAVVItNQVVAQVdgSAFFAGPQLKPiGGNIMAHASTTRLALRK 307
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
9-199 |
5.01e-08 |
|
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: 51.98 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 9 ISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQQ-------GGQAAFIDAEHALDP----VYAQ 77
Cdd:cd19515 1 IST---GSKELDKLLG-GGIETQAITEVFGEFGSGKTQLC-HQLAVNVQLppeegglNGKAVYIDTENTFRPerimQMAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 78 KLGVNIEELL-----LSQPDTGEQAL--EIAEALVRSG-AVDIVVVDSVAALVpKAEI--EGDMGDSHVGLqARLMSQaL 147
Cdd:cd19515 76 ALGLDPDEVLdniyvARAYNSNHQMLlvEKAEDLIKEGnNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHD-L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 937962009 148 RKLSGAINksktIAIFI-NQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRR 199
Cdd:cd19515 153 HRLADLYN----IAVLVtNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
9-199 |
9.39e-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: 51.65 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 9 ISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKT----TVALHAIAEVQQQGGQ--AAFIDAEHALDPV----YAQK 78
Cdd:TIGR02239 75 VIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGGEgkALYIDTEGTFRPErllaIAER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 79 LGVNIEELLLS-------QPDTGEQALEIAEALVRSGAVDIVVVDSVAALVpKAEIEGdMGDshvgLQARLMSQA--LRK 149
Cdd:TIGR02239 154 YGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSG-RGE----LSARQMHLArfLRS 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 937962009 150 LSGAINKSKTIAIFINQIREKV---GVMFGNPETTP-GGRALKFYSSVRLEVRR 199
Cdd:TIGR02239 228 LQRLADEFGVAVVITNQVVAQVdgaGSMFAGDPKKPiGGNIMAHASTTRLSLRK 281
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
19-172 |
1.13e-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: 51.14 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 19 LDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQ---QQGGQ---AAFIDAEHAL----------------DPVYA 76
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprELGGLgggAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 77 QKLGVNIEELLLSQPDTGEQAL-EIAEALVRSGAVDIVVVDSVAALVpkaEIEGDMGDSHVGLQARLMSQALRKLSGAIN 155
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLnYQLPALLERGPIRLVVIDSIAALF---RSEFDTSRSDLVERAKYLRRLADHLKRLAD 156
|
170
....*....|....*..
gi 937962009 156 KSKTIAIFINQIREKVG 172
Cdd:cd19491 157 KYNLAVVVVNQVTDRFD 173
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
12-169 |
6.32e-07 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 48.78 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALH-AIAEVQQQGGQAAFIDA-EHALDPVY-AQKLGVNIEELL- 87
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 88 --------LSQPDTGEQALEIAEAL----------VRSGAVDIVVVDSVAALvpkAEIEGDMgdshvglQARlmsQALRK 149
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180
....*....|....*....|
gi 937962009 150 LSGAINKSKTIAIFINQIRE 169
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPS 166
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
8-202 |
7.28e-07 |
|
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: 49.01 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 8 RISTVPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIAEVQQ-------QGGQAAFIDAEHALDP----VYA 76
Cdd:TIGR02238 74 KVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLS-HTLCVTAQlpremggGNGKVAYIDTEGTFRPdrirAIA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 77 QKLGVN----IEELLLSQPDTGEQALEIAE---ALVRSGAVDIVVVDSVAALVpKAEI--EGDMGDSHVGLqARLMSQaL 147
Cdd:TIGR02238 152 ERFGVDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFsgRGELSERQQKL-AQMLSR-L 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937962009 148 RKLSGAINksktIAIFI-NQIREKVG--VMF-GNPETTPGGRALKFYSSVRLEVR--RAEQ 202
Cdd:TIGR02238 229 NKISEEFN----VAVFVtNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRkgRGEE 285
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
1-202 |
7.70e-07 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 49.01 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 1 LGEKTDTRISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVAlHAIA-----EVQQQGG--QAAFIDAEHALDP 73
Cdd:PLN03187 100 LKRKSVVRITT---GSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlPTEMGGGngKVAYIDTEGTFRP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 74 ----VYAQKLGVN----IEELLLSQPDTGEQ---ALEIAEALVRSGAVDIVVVDSVAALVPKAEI-EGDMGDSHVGLqAR 141
Cdd:PLN03187 175 drivPIAERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAERQQKL-AQ 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937962009 142 LMSQaLRKLSGAINksktIAIFI-NQIREKVG--VMFGNPETTPGGRALKFYSSVRLEVR--RAEQ 202
Cdd:PLN03187 254 MLSR-LTKIAEEFN----VAVYMtNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRkgKGEQ 314
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
12-121 |
2.93e-06 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 46.87 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQ------KLGVNIEE 85
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNaksfgwDFDEMEDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 937962009 86 LLLSQPD---------TGEQALEIAEALVRSGAVDIVVVDSVAAL 121
Cdd:cd01124 80 GKLIIVDappteagrfSLDELLSRILSIIKSFKAKRVVIDSLSGL 124
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
26-201 |
3.32e-06 |
|
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: 46.48 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 26 GGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAA-FID-----------------AEHALDPV-YAQKLGV----N 82
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVlYIDtkssfsarrlaqilksrAQDAEEIDkALQRIRVvrvfD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 83 IEELL--LSQPDTGeqaLEIAEALVRSGaVDIVVVDSVAALVpkAEIEGdmGDSHVGLQARLMSQA--LRKLSgainKSK 158
Cdd:cd19489 82 PYELLdlLEELRNT---LSQQQENLYSR-LKLVIIDSLSALI--SPLLG--GSKHSEGHALLASLArlLKKLA----AEY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 937962009 159 TIAIFINQIREKVGVMFGNPETTPG-GRALKFYSSVRLEVRRAE 201
Cdd:cd19489 150 QIAVLVTNLTVRGGDGGQQGSTKPAlGEYWESVPSTRLLLSRDE 193
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
31-166 |
9.22e-06 |
|
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: 45.42 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 31 GRIIEVYGPESSGKTTVALHAIA---------EVQQQGGQAA--FIDAEHALDP-----VYAQKLGVNIEELLLSQPDTG 94
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 95 EQALeIAEALVR----------------------------SGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQA 146
Cdd:cd19490 81 VEEI-ARECLQRlhifrchsslqllatllslenyllslsaNPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAI 159
|
170 180
....*....|....*....|
gi 937962009 147 LRKLSGAINKSKTIAIFINQ 166
Cdd:cd19490 160 LRELRRLRRRFQLVVIATKQ 179
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
34-188 |
1.41e-05 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 43.26 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 34 IEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDaehALDPVyaqklgvnieelllsqpdtgeqaLEIAEALVRSGAVDIV 113
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFIS---FLDTI-----------------------LEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937962009 114 VVDSVAALVPKAEiegdmgdshvGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALK 188
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
12-121 |
2.91e-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: 43.86 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVY--AQKLGVNIEELLLS 89
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 937962009 90 Q---------PDTG-EQALEIAEALVRSGAVDIVVVDSVAAL 121
Cdd:cd19484 81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSAL 122
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
7-164 |
6.32e-05 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 42.90 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 7 TRISTvpsGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPV--YAQKLGVNIE 84
Cdd:cd01121 62 ERIST---GIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 85 ELLLsqpdTGEQALEIAEALVRSGAVDIVVVDSVAALVPkAEIEGDMGDShvgLQARLMSQALRKLSgainKSKTIAIFI 164
Cdd:cd01121 138 NLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYS-PELTSSPGSV---SQVRECAAELLRLA----KETGIPVFL 205
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
42-114 |
7.02e-05 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 42.52 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 42 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HALDPV-YAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIVV 114
Cdd:cd17992 77 SGKTVVAALAMLAAVENGYQVALmapteILAEqHYDSLKkLLEPLGIRVA--LLTGSTKAKEKREILEKI-ASGEIDIVI 153
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
190-244 |
1.20e-04 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 42.77 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 937962009 190 YSSVR--LEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGISKEG 244
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREG 713
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
6-121 |
1.38e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 42.56 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 6 DTRIST--VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVY--AQKLGV 81
Cdd:PRK09302 247 TQRSSNerISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIrnARSWGI 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 937962009 82 NIEEL----LL----SQPD-TG-EQALEIAEALVRSGAVDIVVVDSVAAL 121
Cdd:PRK09302 326 DLEKMeekgLLkiicARPEsYGlEDHLIIIKREIEEFKPSRVAIDPLSAL 375
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
42-114 |
1.90e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 42.06 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 42 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HA--LDPvYAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIV 113
Cdd:PRK10917 293 SGKTVVAALAALAAIEAGYQAALmapteILAEqHYenLKK-LLEPLGIRVA--LLTGSLKGKERREILEAI-ASGEADIV 368
|
.
gi 937962009 114 V 114
Cdd:PRK10917 369 I 369
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
42-114 |
1.97e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 41.96 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 42 SGKTTVALHAIAEVQQQGGQAAF-----IDAE-HA--LDPvYAQKLGVNIEelLLSQPDTGEQALEIAEALvRSGAVDIV 113
Cdd:COG1200 291 SGKTVVALLAMLAAVEAGYQAALmapteILAEqHYrsLSK-LLEPLGIRVA--LLTGSTKAKERREILAAL-ASGEADIV 366
|
.
gi 937962009 114 V 114
Cdd:COG1200 367 V 367
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
30-181 |
2.78e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.77 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 30 RGRIIEVYGPESSGKTTVALHAiaevqqqgGQAAFIDAEHALDPVYAQKlGVNIEElLLSQPDTGEQALEIAEALVRSga 109
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDR-FPDIVI-RDSWQDFLDAIDELTAAELAD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 110 VDIVVVDSVAALV-----------PKAEIEGDMGDSHV-GLQARLMSQALRKLSGAInksKTIaIFI-NQIREKVGVMFG 176
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELG---KNV-IFTaHAKTRKDEDPDG 144
|
....*
gi 937962009 177 NPETT 181
Cdd:pfam13479 145 EKYTR 149
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
36-73 |
3.26e-04 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 40.27 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 937962009 36 VYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDP 73
Cdd:cd17929 20 LHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTP 57
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
12-119 |
9.46e-04 |
|
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: 39.20 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 12 VPSGSLALDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVY--AQKLGVNIEELLls 89
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFerSEALGIDLRAMV-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 937962009 90 qpDTGEQALEIAEAL----------VRSGAVD----IVVVDSVA 119
Cdd:cd19487 78 --EKGLLSIEQIDPAelspgefaqrVRTSVEQedarVVVIDSLN 119
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
29-150 |
1.85e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.73 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 29 PRGRIIEVYGPESSGKTTVALHAIAEV---------QQQGGQAAFIDAEHALDPV------YAQKLGVNIEEL-----LL 88
Cdd:COG3598 11 PEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlrLL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937962009 89 SQPDTGE--QALEIAEALVRSGAVDIVVVDSVAALvpkaeIEGDMGDSHvglQARLMSQALRKL 150
Cdd:COG3598 91 SLAGDLDdtDDLEALERAIEEEGPDLVVIDPLARV-----FGGDENDAE---EMRAFLNPLDRL 146
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
9-65 |
7.29e-03 |
|
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: 36.56 E-value: 7.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 937962009 9 ISTVPSGslaLDTALGiGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFI 65
Cdd:cd19488 1 ISTGIPG---LDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
32-125 |
7.50e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.78 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937962009 32 RIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPV-YAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAV 110
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKdLLRALLRALGLPLSGRLSKEELLAALQQLLLALAVA 85
|
90
....*....|....*
gi 937962009 111 DIVVVDSVAALVPKA 125
Cdd:pfam13401 86 VVLIIDEAQHLSLEA 100
|
|
| |
