|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-336 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 682.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 1 MDDNKKKALAAALGQIERQFGKGAVMRMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIA 80
Cdd:PRK09354 3 MDEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 81 QAQKMGATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGD 160
Cdd:PRK09354 83 EAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 161 MHVGLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSE 240
Cdd:PRK09354 163 SHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 241 TRVKVVKNKVAPPFRQAEFQILYGKGIYLNGEIVDLAVLHGFVEKSGAWYSYQGSKIGQGKANSAKFLADNPEICKALEK 320
Cdd:PRK09354 243 TKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEK 322
|
330
....*....|....*.
gi 639470730 321 QIRDKLLTPGVDTKAV 336
Cdd:PRK09354 323 KIREKLGLSAAAAEEE 338
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-335 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 660.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 1 MDDNKKKALAAALGQIERQFGKGAVMRMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIA 80
Cdd:COG0468 6 ASSEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 81 QAQKMGATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGD 160
Cdd:COG0468 86 EAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 161 MHVGLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSE 240
Cdd:COG0468 166 SHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 241 TRVKVVKNKVAPPFRQAEFQILYGKGIYLNGEIVDLAVLHGFVEKSGAWYSYQGSKIGQGKANSAKFLADNPEICKALEK 320
Cdd:COG0468 246 TRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEA 325
|
330
....*....|....*
gi 639470730 321 QIRDKLLTPGVDTKA 335
Cdd:COG0468 326 KIREKLGLGAVSEAA 340
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
4-324 |
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: 588.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 4 NKKKALAAALGQIERQFGKGAVMRMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQ 83
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 84 KMGATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGDMHV 163
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 164 GLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSETRV 243
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 244 KVVKNKVAPPFRQAEFQILYGKGIYLNGEIVDLAVLHGFVEKSGAWYSYQGSKIGQGKANSAKFLADNPEICKALEKQIR 323
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVR 320
|
.
gi 639470730 324 D 324
Cdd:TIGR02012 321 E 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
7-267 |
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: 516.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 7 KALAAALGQIERQFGKGAVMRMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMG 86
Cdd:pfam00154 1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 87 ATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGDMHVGLQ 166
Cdd:pfam00154 81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 167 ARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSETRVKVV 246
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVV 240
|
250 260
....*....|....*....|.
gi 639470730 247 KNKVAPPFRQAEFQILYGKGI 267
Cdd:pfam00154 241 KNKVAPPFKEAEFDIMYGEGI 261
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
36-268 |
2.24e-168 |
|
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: 468.57 E-value: 2.24e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 36 IPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDPEYAGKLGVNVDDLLV 115
Cdd:cd00983 2 VEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 116 SQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGDMHVGLQARLMSQALRKITGNIKNANCLVIFINQIR 195
Cdd:cd00983 82 SQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQLR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639470730 196 MKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSETRVKVVKNKVAPPFRQAEFQILYGKGIY 268
Cdd:cd00983 162 EKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGIS 234
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
4-249 |
1.47e-121 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 368.65 E-value: 1.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 4 NKKKALAAALGQIERQFGKGAVMRMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQ 83
Cdd:PRK09519 6 DREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 84 KMGATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIEGEMGDMHV 163
Cdd:PRK09519 86 AAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 164 GLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSETRV 243
Cdd:PRK09519 166 GLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRV 245
|
....*.
gi 639470730 244 KVVKNK 249
Cdd:PRK09519 246 KVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
58-226 |
7.93e-54 |
|
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: 175.23 E-value: 7.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 58 GRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDPEYA-----------GKLGVNVDDLLVSQPDTGEQALE 126
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 127 ITDMLVRSNA----IDVIVVDSVAALVPKAEIEGEMGDMHVGLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMF 202
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 639470730 203 G-SPETTTGGNALKFYASVRLDIRR 226
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
245-326 |
1.41e-22 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 99.01 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 245 VVKNKVAPPFRQAEFQILYGKGIYLNGEIVDLAVLHGFVEKSGAWYSYQGSKIGQGKANSAKFLADNPEICKALEKQIRD 324
Cdd:PRK09519 687 VVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKE 766
|
..
gi 639470730 325 KL 326
Cdd:PRK09519 767 KL 768
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
39-261 |
3.41e-17 |
|
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: 79.28 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEhALDPE----YAG-KLGVNVDDL 113
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPErfqqIAGeRFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 114 LVSQP-DTGEQALEITDM--LVRSNAIDVIVVDSVAALVpKAEIEGEmgdmhVGLQARLMSQaLRKITGNIKNANCLVIF 190
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLELGDD-----SEANRELSRQ-MSKLLSIARKYDIPVVI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639470730 191 INQIRMKIGVMFGSPettTGGNALKFyasvrldirRTGAVKEGDEVVGSETRVKVVKNKVAPPFRQAEFQI 261
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLEH---------WSKAIIRLEKSPPGLRRATLEKHRSRPEGQSAGFRI 210
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
33-226 |
4.95e-14 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 71.83 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLT--LSVIAQAQK----MGATCAFVDAEHALDPE----Y 102
Cdd:PRK04301 78 RKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQIChqLAVNVQLPEekggLEGKAVYIDTEGTFRPErieqM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVNVDDLL----VSQP-DTGEQAL---EITDMLVRSNAIDVIVVDSVAALVpKAEIEGEmGDMHVgLQARL---MS 171
Cdd:PRK04301 157 AEALGLDPDEVLdnihVARAyNSDHQMLlaeKAEELIKEGENIKLVIVDSLTAHF-RAEYVGR-GNLAE-RQQKLnkhLH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 639470730 172 QALRKITGNiknaNCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRR 226
Cdd:PRK04301 234 DLLRLADLY----NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
39-206 |
9.00e-14 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 69.56 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDP--EYAGKLGVNVDDLL-- 114
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQllRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 115 ----VSQPDTGEQALEITDML------VRSNAIDVIVVDSVAALVPKAEIEGEMGDMhvglqarlmsqaLRKITGNIKNA 184
Cdd:COG0467 81 gllrIIDLSPEELGLDLEELLarlreaVEEFGAKRVVIDSLSGLLLALPDPERLREF------------LHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 639470730 185 NCLVIFINQIRMKIGVMFGSPE 206
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
39-231 |
2.65e-13 |
|
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: 68.54 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQAQK----MGATCAFVDAEHALDPE----YAGKLGV 108
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLchQLAVNVQLPPeeggLNGKAVYIDTENTFRPErimqMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 109 NVDDLL----VSQP-DTGEQAL---EITDMLVRSNAIDVIVVDSVAALVpKAEIEGEmGDMHVGLQ--ARLMSQALRkiT 178
Cdd:cd19515 80 DPDEVLdniyVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR-GTLAERQQklNKHLHDLHR--L 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639470730 179 GNIknANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVK 231
Cdd:cd19515 156 ADL--YNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRKGKGGK 206
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
33-268 |
4.81e-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: 68.10 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQAQK-MGAT---CAFVDAEHALDPE----Y 102
Cdd:pfam08423 13 RSELIQITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRPErlvaI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVNVDDLLVSQP-------DTGEQALEITDMLVRSNAIDVIVVDSVAALVpKAEIE--GEMGD--MHVGlqaRLMS 171
Cdd:pfam08423 92 AERYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAErqQHLA---KFLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 172 qALRKITGNIKNAnclVIFINQIRMKIG---VMF-GSPETTTGGNALKFYASVRLDIRRtgavKEGDEVVgsetrVKVVK 247
Cdd:pfam08423 168 -TLQRLADEFGVA---VVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK----GRGEQRI-----CKIYD 234
|
250 260
....*....|....*....|...
gi 639470730 248 nkvAP--PFRQAEFQIlYGKGIY 268
Cdd:pfam08423 235 ---SPclPESEAVFAI-GSGGII 253
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
27-261 |
8.32e-13 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 68.61 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 27 RMGDHDRQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ--AQKMGAT--CAFVDAEHALDP 100
Cdd:PLN03186 93 SQLHAQRQEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQlpLDQGGGEgkAMYIDTEGTFRP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 101 E----YAGKLGVNVDDLL-----VSQPDTGEQA---LEITDMLVRSNaIDVIVVDSVAALVpKAEIEGEmGDmhvgLQAR 168
Cdd:PLN03186 172 QrliqIAERFGLNGADVLenvayARAYNTDHQSellLEAASMMAETR-FALMIVDSATALY-RTEFSGR-GE----LSAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 169 --LMSQALRKITGNIKNANCLVIFINQIRMKI--GVMFGSPETT-TGGNALKFYASVRLdirrtgAVKEGDevvgSETRV 243
Cdd:PLN03186 245 qmHLGKFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRL------ALRKGR----GENRI 314
|
250
....*....|....*....
gi 639470730 244 -KVVKNKVAPPfRQAEFQI 261
Cdd:PLN03186 315 cKVISSPCLPE-AEARFSI 332
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
27-143 |
2.15e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 65.72 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 27 RMGDHDRQAIPAISTGSLGLDIALGIGGLPKGRIVEIYGPE-SSGKTTLTLSVIAQAQKMGATCAFVDAEHALDPEYAGK 105
Cdd:COG4544 17 RGEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDLYAPGLAA 96
|
90 100 110
....*....|....*....|....*....|....*...
gi 639470730 106 LGVNVDDLLVSQPDTGEQALEITDMLVRSNAIDVIVVD 143
Cdd:COG4544 97 AGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
46-236 |
3.66e-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: 64.74 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 46 LDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEhALDPEYAGKLGVN-----VDDLLVSQP-- 118
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 119 -DTGEQALEITDMLVRSNAIDVIVVDSVAALVpKAEIEGEMGDMHVGL--QARLMSQALRKitgniknANCLVIFINQIR 195
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELarQLTLLLSLARK-------KNLAVVITNQVY 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 639470730 196 MKIGVMFGSPettTGGNALKFY--ASVRLD---------IRRTGAVKEGDEV 236
Cdd:TIGR02237 151 TDVNNGTLRP---LGGHLLEHWskVILRLEkfrgrrlatLEKHRSRPEGESV 199
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
39-275 |
6.86e-12 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 64.11 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEhALDPEYAGKL-GVNVDDLL--- 114
Cdd:PRK09361 5 LPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELLsni 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 115 -VSQP-DTGEQALEITDM--LVRSNaIDVIVVDSVAALVpKAEIEGEM--GDMHVGLQARLmsQALRKITgniKNANCLV 188
Cdd:PRK09361 83 iIFEPsSFEEQSEAIRKAekLAKEN-VGLIVLDSATSLY-RLELEDEEdnSKLNRELGRQL--THLLKLA---RKHDLAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 189 IFINQIRMKIGVMFGSPettTGGNALKFYASVRLDIRRTGavkegdevvGSETRVKVVKNKVAPPFRQAEFQILyGKGIy 268
Cdd:PRK09361 156 VITNQVYSDIDSDGLRP---LGGHTLEHWSKTILRLEKFR---------NGKRRATLEKHRSRPEGESAEFRIT-DRGI- 221
|
....*..
gi 639470730 269 lngEIVD 275
Cdd:PRK09361 222 ---EIID 225
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
39-226 |
8.12e-11 |
|
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: 61.39 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ----AQKMGATCAFVDAEHALDPE----YAGKLGV 108
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQlpidRGGGEGKAIYIDTEGTFRPErlraIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 109 NVDDLL----VSQPDTGEQALEITD----MLVRSnAIDVIVVDSVAALVPKAEI-EGEMGDMHVGLqARLMSqALRKITG 179
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLLDqaaaMMVES-RFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLR-MLQRLAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 639470730 180 NIKNAnclVIFINQIRMKIG---VMFGSPETTTGGNALKFYASVRLDIRR 226
Cdd:cd01123 157 EFGVA---VVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
33-264 |
1.04e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 62.10 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ-AQKMGATC---AFVDAEHALDPE----Y 102
Cdd:PLN03187 102 RKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQlPTEMGGGNgkvAYIDTEGTFRPDrivpI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVN----VDDLLVSQPDTGEQ---ALEITDMLVRSNAIDVIVVDSVAALVPKAEI-EGEMGDMhvglQARLmSQAL 174
Cdd:PLN03187 181 AERFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQML 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 175 RKITGNIKNANCLVIFINQIRMKIG--VMFGSPETTTGGNALKFYASVRLDIRRTGAvkegdevvgsETRV-KVVKnkvA 251
Cdd:PLN03187 256 SRLTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRKGKG----------EQRVcKVFD---A 322
|
250
....*....|....*
gi 639470730 252 PPFRQAE--FQILYG 264
Cdd:PLN03187 323 PNLPEAEaeFQITSG 337
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
39-226 |
1.17e-10 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 60.83 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ-AQKMGATC---AFVDAEHALDPE----YAGKLGV 108
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQlPGSMGGGGgkvAYIDTEGTFRPDrirpIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 109 N----VDDLLVSQPDTGEQALEITDMLVRSNAID----VIVVDSVAALVpKAEI--EGEMGDMHVGLqARLMSQaLRKIT 178
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMALF-RVDFsgRGELAERQQKL-AQMLSR-LQKIS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 639470730 179 gniKNANCLVIFINQIRMKIG--VMFGS-PETTTGGNALKFYASVRLDIRR 226
Cdd:cd19514 157 ---EEYNVAVFITNQVTADPGaaMTFQAdPKKPIGGHILAHASTTRISLRK 204
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
47-226 |
2.98e-10 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 59.64 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 47 DIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQA----QKMGAT--CAFVDAEHALDPE---------YAGKLGVNVD 111
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampaRKGGLDggVLYIDTESKFSAErlaeiaearFPEAFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 112 D----------LLVSQPDTGEQALEITDML---VRSNAIDVIVVDSVAALVPKaeiegEMGDMHVGLQARlmSQALRKIT 178
Cdd:cd19493 80 EneraeemlkrVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 639470730 179 GNIK----NANCLVIFINQIRMKIGVMFGSPETTTG--GNALKFYASVRLDIRR 226
Cdd:cd19493 153 SSLKrlaeEFRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLER 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-226 |
6.47e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 57 KGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDPEYAGKLGVNVDDLLVSqpDTGEQALEITDMLVRSNA 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 137 IDVIVVDSVAALVPKaeiegemgdmhVGLQARLMSQALRKITGNIKNANCLVIFINQirmkigvmfgsPETTTGGNALKF 216
Cdd:smart00382 79 PDVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRR 136
|
170
....*....|
gi 639470730 217 YASVRLDIRR 226
Cdd:smart00382 137 RFDRRIVLLL 146
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
39-206 |
1.25e-09 |
|
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: 57.66 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDP--EYAGKLGVNVDDL--- 113
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERllRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 114 ----LVSQPDTGEQALEITDML------VRSNAIDVIVVDSVAALvpKAEIEGEMgdmhvglQARlmsQALRKITGNIKN 183
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDELLsrilsiIKSFKAKRVVIDSLSGL--RRAKEDQM-------RAR---RIVIALLNELRA 147
|
170 180
....*....|....*....|....*.
gi 639470730 184 ANCLVIFINQ---IRMKIGVMFGSPE 206
Cdd:cd01124 148 AGVTTIFTSEmrsFLSSESAGGGDVS 173
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
39-226 |
2.96e-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: 56.49 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDiALGIGGLPKGRIVEIYGPESSGKTTLTLS-VIAQAQKMGATCAFVDA-EHALD-PEYAGKLGVNVDDLL- 114
Cdd:pfam06745 1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 115 --------VSQPDTGEQALEITDML----------VRSNAIDVIVVDSVAALvpkAEIEGEMgdmhvglQARlmsQALRK 176
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639470730 177 ITGNIKNANCLVIFINQIRMKigvmfgspETTTGGNALKFYAS---VRLDIRR 226
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKE 191
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
33-226 |
5.80e-09 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 56.93 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ-AQKMGAT---CAFVDAEHALDPE----Y 102
Cdd:PTZ00035 94 RKNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlPIEQGGGegkVLYIDTEGTFRPErivqI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVN----VDDLLVSQPDTGEQALEITDMLVRSNAID---VIVVDSVAALVpkaEIE----GEMGD--MHVGlqaRL 169
Cdd:PTZ00035 173 AERFGLDpedvLDNIAYARAYNHEHQMQLLSQAAAKMAEErfaLLIVDSATALF---RVDysgrGELAErqQHLG---KF 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 170 MSqALRKITGNIknaNCLVIFINQIRMKIG---VMFGSPETTTGGNALKFYASVRLDIRR 226
Cdd:PTZ00035 247 LR-ALQKLADEF---NVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
39-261 |
2.15e-08 |
|
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: 54.25 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ-AQKMGAT---CAFVDAEHALDPE----YAGKLGV 108
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQlPIDQGGGegkALYIDTEGTFRPErllaIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 109 NVDDLL--VSQP---DTGEQaleiTDMLVRSNAI------DVIVVDSVAALVpKAEIEGEmGDmhvgLQARLM--SQALR 175
Cdd:cd19513 80 NGEDVLdnVAYArayNTDHQ----MQLLIQASAMmaesryALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 176 KITGNIKNANCLVIFINQIRMKI--GVMF-GSPETTTGGNALKFYASVRLDIRRTGAvkegdevvgsETRVKVVKNKVAP 252
Cdd:cd19513 150 MLQRLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRKGRG----------ETRICKIYDSPCL 219
|
....*....
gi 639470730 253 PFRQAEFQI 261
Cdd:cd19513 220 PEAEAVFAI 228
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
33-261 |
2.21e-08 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 54.78 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQAQK-MG---ATCAFVDAEHALDPE----Y 102
Cdd:TIGR02238 72 RKKVLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPReMGggnGKVAYIDTEGTFRPDriraI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVN----VDDLLVSQPDTGEQALEITDMLVRSNAID---VIVVDSVAALVpKAEI--EGEMGDMhvglQARLmSQA 173
Cdd:TIGR02238 151 AERFGVDpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMALF-RVDFsgRGELSER----QQKL-AQM 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 174 LRKITGNIKNANCLVIFINQIRMKIG--VMFGS-PETTTGGNALKFYASVRLDIRRTGAvkegdevvgsETRVKVVKNKV 250
Cdd:TIGR02238 225 LSRLNKISEEFNVAVFVTNQVQADPGatMTFIAdPKKPIGGHVLAHASTTRILLRKGRG----------EERVAKLYDSP 294
|
250
....*....|.
gi 639470730 251 APPFRQAEFQI 261
Cdd:TIGR02238 295 DMPEAEASFQI 305
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
33-226 |
3.09e-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: 54.35 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 33 RQAIPAISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTL--TLSVIAQ---AQKMG-ATCAFVDAEHALDPE----Y 102
Cdd:TIGR02239 72 RQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQlpiDQGGGeGKALYIDTEGTFRPErllaI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 103 AGKLGVNVDDLL--VS-----QPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEI-EGEMGD--MHVGLQARlmsq 172
Cdd:TIGR02239 151 AERYGLNPEDVLdnVAyarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALYRTDFSgRGELSArqMHLARFLR---- 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 639470730 173 ALRKITGNIKNAnclVIFINQIRMKI---GVMF-GSPETTTGGNALKFYASVRLDIRR 226
Cdd:TIGR02239 227 SLQRLADEFGVA---VVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
46-194 |
5.99e-07 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 49.98 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 46 LDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQ------KMGATCAFVDAEHAL----------------DPEYA 103
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 104 GKLGVNVDDLLVSQPDTGEQALEITD-MLVRSNAIDVIVVDSVAALVpKAEIEGEMGDMhvGLQARLMSQALRKITGNIK 182
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF-RSEFDTSRSDL--VERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 639470730 183 NANCLVIFINQI 194
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
55-254 |
1.94e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 45.66 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 55 LPKGRIVEIYGPESSGKTTLTL----SVIAQAQKMGATCA-----FVDAE----------------HALDPEYAGKlGVN 109
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALqlaaAVAAGGPWLGRRVPpgkvlYLAAEddrgelrrrlkalgadLGLPFADLDG-RLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 110 VDDLLVSQPDTGEQAlEITDmLVRSNAIDVIVVDSVAALVPkaeiegemGDMHVGLQARLMSQALRKItgnIKNANCLVI 189
Cdd:COG3598 89 LLSLAGDLDDTDDLE-ALER-AIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL---AERTGAAVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639470730 190 FINQIRmKIGVMFGSPETTTGGNALKFYASVRLDIRRtgaVKEGDEVVgsetrVKVVKNKVAPPF 254
Cdd:COG3598 156 LVHHTG-KGGAGKDSGDRARGSSALRGAARSVLVLSR---EKGEDLRV-----LTRAKSNYGPEI 211
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
53-93 |
9.34e-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: 43.01 E-value: 9.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 639470730 53 GGLPKGRIVEIYGPESSGKTTLTLSVIAQ-AQKMGATCAFVD 93
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANvASRSGQNVLYID 43
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
39-92 |
9.63e-05 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 43.11 E-value: 9.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFV 92
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
39-145 |
3.14e-04 |
|
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: 41.75 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDP--EYAGKLGVNVDDLLVs 116
Cdd:cd01121 64 ISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQikLRAERLGLGSDNLYL- 141
|
90 100
....*....|....*....|....*....
gi 639470730 117 qpdTGEQALEITDMLVRSNAIDVIVVDSV 145
Cdd:cd01121 142 ---LAETNLEAILAEIEELKPSLVVIDSI 167
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
39-149 |
7.19e-04 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 40.59 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAE----------HALD----PEYA- 103
Cdd:COG2874 3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTElttkefikqmKSLSydisDYLLr 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 639470730 104 GKLGVNVDDLLVSQPDTGE--QALEITDMLVRSNAI--DVIVVDSVAALV 149
Cdd:COG2874 82 GRLLFLPVHPLGFEWNSKQrkDLLKRLMKYIASNLWeaDVIIIDSLSALL 131
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
39-155 |
1.22e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 39.96 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 39 ISTGSLGLDIALGiGGLPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAE--------------HALDPEYA- 103
Cdd:PRK06067 7 ISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTEntsksylkqmesvkIDISDFFLw 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 639470730 104 GKLGV---NVDDLLVSqPDTGEQALEITDMLVRSNAIDVIVVDSVAALVPKAEIE 155
Cdd:PRK06067 86 GYLRIfplNTEGFEWN-STLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
59-152 |
2.48e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 59 RIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAEHALDP-EYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAI 137
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkDLLRALLRALGLPLSGRLSKEELLAALQQLLLALAVA 85
|
90
....*....|....*
gi 639470730 138 DVIVVDSVAALVPKA 152
Cdd:pfam13401 86 VVLIIDEAQHLSLEA 100
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
58-82 |
3.20e-03 |
|
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: 38.48 E-value: 3.20e-03
10 20
....*....|....*....|....*
gi 639470730 58 GRIVEIYGPESSGKTTLTLSVIAQA 82
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARC 25
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
55-191 |
3.37e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.51 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639470730 55 LPKGRIVEIYGPESSGKTTLTLSVIAQAQKMGATCAFVDAehaldPEYAGKLGVNVDDllvsqpdtGEQALEITDMLVRS 134
Cdd:cd00009 16 LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNA-----SDLLEGLVVAELF--------GHFLVRLLFELAEK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 639470730 135 NAIDVIVVDsvaalvpkaeiegEMGDMHVGLQARLMSQALRKITGNIKNANCLVIFI 191
Cdd:cd00009 83 AKPGVLFID-------------EIDSLSRGAQNALLRVLETLNDLRIDRENVRVIGA 126
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
59-103 |
4.45e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 37.49 E-value: 4.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 639470730 59 RIVeIYGPESSGKTTLTlsvIAQAQKMGATCAfvdaehaldPEYA 103
Cdd:COG3172 10 KIV-LLGAESTGKTTLA---RALAAHYNTPWV---------PEYG 41
|
|
| |
