|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
80-310 |
7.79e-100 |
|
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: 294.61 E-value: 7.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 80 DRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQSRFPEFFSV---- 155
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFSGfmee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 156 KERLLEMAARVHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFDTSLpGNLTHRSNFLGQEAAVLKYLS 235
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153678 236 QEFCIPVVLTNQITTHVGEKLHcpqwnqtdasfeeDSGFVTAALGNTWSHSVNTRLIVQYEDS-ERRQIVIAKSPV 310
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDAGD-------------GSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKSPL 222
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
79-316 |
4.43e-49 |
|
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: 165.54 E-value: 4.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 79 LDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQS-RFPEFFSVKE 157
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSlPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 158 RLLEmaaRVHLFR--ELTCQDVL--KRLERLEEDIiacRAGLVILDSVASVVRKEFDTSlPGNLTHRSNFLGQEAAVLKY 233
Cdd:cd19491 81 NFLD---NIFVEHvaDLETLEHClnYQLPALLERG---PIRLVVIDSIAALFRSEFDTS-RSDLVERAKYLRRLADHLKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 234 LSQEFCIPVVLTNQITTHVGE-----KLHCPQWNQTDASFEEDSGF--VTAALGNTWSHSVNTRLIVQYEDSERRQIVIA 306
Cdd:cd19491 154 LADKYNLAVVVVNQVTDRFDSssdasGLGVLDYLSQFSSFSGGVSGnrKVPALGLTWANLVNTRLMLSRTPKRITDSSAA 233
|
250
....*....|
gi 1207153678 307 KSPVAPFAVL 316
Cdd:cd19491 234 SISVRRLEVV 243
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
58-325 |
1.08e-47 |
|
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: 162.09 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 58 ITALDLW-KRKEELCFSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAF 136
Cdd:pfam08423 4 TTATELHqRRSELIQITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTEGTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 137 SAERLVEMAQsRF---PEffSVKERLleMAARVHlfrelTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSL 213
Cdd:pfam08423 84 RPERLVAIAE-RYgldPE--DVLDNV--AYARAY-----NSEHQMQLLQQAAAMMSESRFALLIVDSATALYRTDF--SG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 214 PGNLTHRSNFLGQEAAVLKYLSQEFCIPVVLTNQITTHVGeklHCPQWNQTDASfeedsgfvTAALGNTWSHSVNTRLIV 293
Cdd:pfam08423 152 RGELAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVD---GAAGMFSGDPK--------KPIGGHIMAHASTTRLSL 220
|
250 260 270
....*....|....*....|....*....|..
gi 1207153678 294 QYEDSERRQIVIAKSPVAPFAVLSYTIQKEGI 325
Cdd:pfam08423 221 RKGRGEQRICKIYDSPCLPESEAVFAIGSGGI 252
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
90-295 |
1.56e-43 |
|
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: 149.04 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 90 GALTEVTGPSGCGKTQLCMMLSVLATLpksLGGldsGVVYIDTESAFSAERLVEMAQSRfpefFSVKERLLEMAARVHLF 169
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL---LGG---GVVWIDTEGAFPPSRLVQILEAS----PSSELELAEALSRLLYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 170 RELTCQDVLKRLE-RLEEDIIACRAGLVILDSVASVVRKEFDTSLPG--NLTHRSNFLGQEAAVLKYLSQEFCIPVVLTN 246
Cdd:cd01393 71 RPPDTLAHLLALDsLPESLFPPPNTSLVVVDSVSALFRKAFPRGGDGdsSSSLRARLLSQLARALQKLAAQFNLAVVVTN 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207153678 247 QITTHVGEklhcpqwnqtdasfEEDSGFVTAALGNTWSHSVNTRLIVQY 295
Cdd:cd01393 151 QVTTKIRG--------------GSGASLVPPALGNTWEHSVSTRLLLYR 185
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
85-308 |
1.06e-32 |
|
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: 121.20 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 85 GGLPRGALTEVTGPSGCGKTQLCMMLSVLATLpkslgGLDSGVVYIDTESAFSAERLVEMAQSRfpefFSVKERLLEMAA 164
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANVAS-----RSGQNVLYIDTKSSFSARRLAQILKSR----AQDAEEIDKALQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 165 RVHLFRELTCQDVLKRLERLEEDI------IACRAGLVILDSVASVVrkefdTSLPGNLTHRSN--FLGQEAAVLKYLSQ 236
Cdd:cd19489 73 RIRVVRVFDPYELLDLLEELRNTLsqqqenLYSRLKLVIIDSLSALI-----SPLLGGSKHSEGhaLLASLARLLKKLAA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153678 237 EFCIPVVLTNQITThvgeklhcpqWNQTDASFEEdsgfvTAALGNTWSHSVNTRLIV-----QYEDSERRQIVIAKS 308
Cdd:cd19489 148 EYQIAVLVTNLTVR----------GGDGGQQGST-----KPALGEYWESVPSTRLLLsrdenDPEESGVCTATLLKS 209
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
5-325 |
1.85e-32 |
|
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: 123.68 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 5 KLRRSGVSADLCERLKRHQLETCQV-------ELSRLAGLSYPAALNLQRLVSKACAPAVITALDLWKRKEEL-CFSTSL 76
Cdd:TIGR02239 3 KLEGNGITAADIKKLQEAGLHTVESvayapkkQLLEIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRQEViQLTTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 77 PALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRF---PEff 153
Cdd:TIGR02239 83 KELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE-RYglnPE-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 154 svkerllEMAARVHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAAVLKY 233
Cdd:TIGR02239 160 -------DVLDNVAYARAYNTDHQLQLLQQAAAMMSESRFALLIVDSATALYRTDF--SGRGELSARQMHLARFLRSLQR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 234 LSQEFCIPVVLTNQITTHVgeklhcpqwNQTDASFEEDSGFVTAalGNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAPF 313
Cdd:TIGR02239 231 LADEFGVAVVITNQVVAQV---------DGAGSMFAGDPKKPIG--GNIMAHASTTRLSLRKGRGEQRICKIYDSPCLPE 299
|
330
....*....|..
gi 1207153678 314 AVLSYTIQKEGI 325
Cdd:TIGR02239 300 SEAMFAIYEDGI 311
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
5-325 |
3.48e-32 |
|
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: 122.96 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 5 KLRRSGVSADLCERLKRHQLETCQV-------ELSRLAGLSYPAALNLQRLVSKACAPAVITALD-LWKRKEELCFSTSL 76
Cdd:TIGR02238 3 KLQAHGINAADIKKLKSAGICTVNGvimttrrALCKIKGLSEAKVDKIKEAASKIINPGFITAFEiSQKRKKVLKITTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 77 PALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRF---PEff 153
Cdd:TIGR02238 83 QALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAE-RFgvdPD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 154 SVKERLLEMAARVHlfrELTCQDVLKRLERLEEDIIAcragLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAAVLKY 233
Cdd:TIGR02238 160 AVLDNILYARAYTS---EHQMELLDYLAAKFSEEPFR----LLIVDSIMALFRVDF--SGRGELSERQQKLAQMLSRLNK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 234 LSQEFCIPVVLTNQITTHVGeklhcpqwnqtdASFEEDSGFVTAALGNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAPF 313
Cdd:TIGR02238 231 ISEEFNVAVFVTNQVQADPG------------ATMTFIADPKKPIGGHVLAHASTTRILLRKGRGEERVAKLYDSPDMPE 298
|
330
....*....|..
gi 1207153678 314 AVLSYTIQKEGI 325
Cdd:TIGR02238 299 AEASFQITEGGI 310
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
5-325 |
3.87e-32 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 123.18 E-value: 3.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 5 KLRRSGVSADLCERLKR---HQLE----TCQVELSRLAGLSYPAALNLQRLVSKACAPAVITALD-LWKRKEELCFSTSL 76
Cdd:PTZ00035 25 KLQSAGINAADIKKLKEagiCTVEsvayATKKDLCNIKGISEAKVEKIKEAASKLVPMGFISATEyLEARKNIIRITTGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 77 PALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRF---PEff 153
Cdd:PTZ00035 105 TQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAE-RFgldPE-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 154 SVKERLleMAARVHlfrelTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAAVLKY 233
Cdd:PTZ00035 182 DVLDNI--AYARAY-----NHEHQMQLLSQAAAKMAEERFALLIVDSATALFRVDY--SGRGELAERQQHLGKFLRALQK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 234 LSQEFCIPVVLTNQITTHVGeklhcpqwnqTDASFEEDS----GfvtaalGNTWSHSVNTRLIVQYEDSERRQIVIAKSP 309
Cdd:PTZ00035 253 LADEFNVAVVITNQVMADVD----------GASMFVADPkkpiG------GHIIAHASTTRLSLRKGRGEQRICKIYDSP 316
|
330
....*....|....*.
gi 1207153678 310 VAPFAVLSYTIQKEGI 325
Cdd:PTZ00035 317 NLPESEAVFAISEGGI 332
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
4-326 |
4.00e-32 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 123.30 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 4 KKLRRSGVsadlcerlkrHQLE----TCQVELSRLAGLSYPAALNLQRLVSKACAPAVITALDLWKRKEELCFSTSLPA- 78
Cdd:PLN03186 42 KKLKDAGI----------HTVEslayAPKKDLLQIKGISEAKVEKILEAASKLVPLGFTTASQLHAQRQEIIQITTGSRe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 79 LDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRFPEFFSVker 158
Cdd:PLN03186 112 LDKILEGGIETGSITEIYGEFRTGKTQLCHTLCVTCQLPLDQGGGEGKAMYIDTEGTFRPQRLIQIAE-RFGLNGAD--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 159 LLEmaaRVHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAAVLKYLSQEF 238
Cdd:PLN03186 188 VLE---NVAYARAYNTDHQSELLLEAASMMAETRFALMIVDSATALYRTEF--SGRGELSARQMHLGKFLRSLQRLADEF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 239 CIPVVLTNQITTHVgeklhcpqwnqtdasfeEDSGFVTAAL-----GNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAPF 313
Cdd:PLN03186 263 GVAVVITNQVVAQV-----------------DGSAFFAGPQlkpigGNIMAHASTTRLALRKGRGENRICKVISSPCLPE 325
|
330
....*....|...
gi 1207153678 314 AVLSYTIQKEGIR 326
Cdd:PLN03186 326 AEARFSISSEGVT 338
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-309 |
1.19e-31 |
|
RAD51C recombinase; RAD51C 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. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 117.33 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 90 GALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLvemaqsrfpeffsvkerllemaaRVHLF 169
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSFNIHYF-----------------------RVHDY 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 170 RELTCQ-DVLKRLERLEEDIiacraGLVILDSVASVVRKEFDtslpgNLTHRSNFLGQEAAVLKYLSQEFCIPVVLTNQI 248
Cdd:cd19492 58 VELLALiNSLPKFLEDHPKV-----KLIVVDSIAFPFRHDFD-----DLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153678 249 TTHVGEKlhcpqwnqtdasfeeDSGFVTAALGNTWSHSVNTRLIVqYEDSERRQIVIAKSP 309
Cdd:cd19492 128 TTKISED---------------GQSQLVPALGESWSHACTTRLFL-TWDEKQRFAHLYKSP 172
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
73-325 |
4.22e-31 |
|
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: 118.02 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRF--- 149
Cdd:cd01123 2 TTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERLRAIAQ-RFgld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 150 PEffsvkerllEMAARVHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAA 229
Cdd:cd01123 81 PD---------DVLDNVAYARAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDY--SGRGELSARQMHLAKFLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 230 VLKYLSQEFCIPVVLTNQITTHVGeklhcpqwnqTDASFEEDSGFVTAalGNTWSHSVNTRLIVQYEDSERRQIVIAKSP 309
Cdd:cd01123 150 MLQRLADEFGVAVVVTNQVVAQVD----------GAMMFAADPKKPIG--GNILAHASTTRLYLRKGRGETRICKIYDSP 217
|
250
....*....|....*.
gi 1207153678 310 VAPFAVLSYTIQKEGI 325
Cdd:cd01123 218 CLPEAEAVFAITADGV 233
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
30-326 |
2.69e-30 |
|
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 131290 [Multi-domain] Cd Length: 310 Bit Score: 117.54 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 30 ELSRLAGLSYPAALNLQRLVSKAC-APAVITALDLWKRKEELC-FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLC 107
Cdd:TIGR02236 33 ELSEIAGISEGTAAKIIQAARKAAdLGGFETADDVLERRKTIGkITTGSKELDELLGGGIETQAITEVFGEFGSGKTQIC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 108 MMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQSRfpeffsvKERLLEMAARVHLFRELTCQDVLKRLERLEED 187
Cdd:TIGR02236 113 HQLAVNVQLPEEKGGLGGKAVYIDTENTFRPERIMQMAEAR-------GLDPDEVLKNIYVARAYNSNHQMLLVEKAEDL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 188 I--IACRAGLVILDSVASVVRKEFDTSlpGNLTHRSNFLGQEAAVLKYLSQEFCIPVVLTNQITThvgeklhcpqwnQTD 265
Cdd:TIGR02236 186 IkeLNNPVKLLIVDSLTSHFRAEYVGR--GALAERQQKLNKHLHDLLRLADLYNAAVVVTNQVMA------------RPD 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153678 266 ASFeedsGFVTAAL-GNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAPFAVLSYTIQKEGIR 326
Cdd:TIGR02236 252 AFF----GDPTRPIgGHILGHAATFRVYLRKGKGDKRIARLVDSPHLPEGEAVFRITEKGIE 309
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
73-326 |
8.15e-30 |
|
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: 114.38 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQSR--FP 150
Cdd:cd19515 2 STGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERIMQMAKALglDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 151 EffsvkerllEMAARVHLFRELTCQDVLKRLERLEEDIIACR-AGLVILDSVASVVRKEFDTSlpGNLTHRSNFLGQEAA 229
Cdd:cd19515 82 D---------EVLDNIYVARAYNSNHQMLLVEKAEDLIKEGNnIKLLIVDSLTSHFRAEYVGR--GTLAERQQKLNKHLH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 230 VLKYLSQEFCIPVVLTNQITThvgeklhcpqwnQTDASFEEDsgfVTAALGNTWSHSVNTRLIVQYEDSERRQIVIAKSP 309
Cdd:cd19515 151 DLHRLADLYNIAVLVTNQVMA------------KPDAFFGDP---TQAIGGHILGHAATFRVYLRKGKGGKRIARLVDSP 215
|
250
....*....|....*..
gi 1207153678 310 VAPFAVLSYTIQKEGIR 326
Cdd:cd19515 216 HLPEGEAVFRITEKGIE 232
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
30-326 |
2.23e-29 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 115.36 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 30 ELSRLAGLSYPAAlnlQRLVSKACAPAVI----TALDLWKRKEELC-FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKT 104
Cdd:PRK04301 40 ELSEAAGIGESTA---AKIIEAAREAADIggfeTALEVLERRKNVGkITTGSKELDELLGGGIETQSITEFYGEFGSGKT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 105 QLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQSR--FPEffsvkerllEMAARVHLFRELTCQ------D 176
Cdd:PRK04301 117 QICHQLAVNVQLPEEKGGLEGKAVYIDTEGTFRPERIEQMAEALglDPD---------EVLDNIHVARAYNSDhqmllaE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 177 VLKRLERLEEDIiacraGLVILDSVASVVRKEFdtslPG--NLTHRSNFLGQEAAVLKYLSQEFCIPVVLTNQITThvge 254
Cdd:PRK04301 188 KAEELIKEGENI-----KLVIVDSLTAHFRAEY----VGrgNLAERQQKLNKHLHDLLRLADLYNAAVVVTNQVMA---- 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 255 klhcpqwnQTDASFeedsGFVTAAL-GNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAPFAVLSYTIQKEGIR 326
Cdd:PRK04301 255 --------RPDAFF----GDPTQPIgGHILGHTATFRIYLRKSKGNKRIARLVDSPHLPEGEAVFRITEEGIR 315
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
72-325 |
7.12e-29 |
|
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: 112.03 E-value: 7.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 72 FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRFPe 151
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE-RYG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 152 fFSVKERLLEMA-ARVHlfrelTCQDVLKRLERLEEDIIACRAGLVILDSVASVVRKEFdtSLPGNLTHRSNFLGQEAAV 230
Cdd:cd19513 79 -LNGEDVLDNVAyARAY-----NTDHQMQLLIQASAMMAESRYALLIVDSATALYRTDY--SGRGELSARQMHLAKFLRM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 231 LKYLSQEFCIPVVLTNQITTHVgeklhcpqwnQTDASFEEDS----GfvtaalGNTWSHSVNTRLIVQYEDSERRQIVIA 306
Cdd:cd19513 151 LQRLADEFGVAVVITNQVVAQV----------DGAAMFAGDPkkpiG------GNIMAHASTTRLYLRKGRGETRICKIY 214
|
250
....*....|....*....
gi 1207153678 307 KSPVAPFAVLSYTIQKEGI 325
Cdd:cd19513 215 DSPCLPEAEAVFAITEDGI 233
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
73-325 |
7.86e-29 |
|
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: 111.68 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQSrfpef 152
Cdd:cd19514 2 STGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRIRPIAER----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 153 FSV-KERLLE--MAARV----HLFRELTCqdVLKRLErlEEDIIAcragLVILDSVASVVRKEFdtSLPGNLTHRSNFLG 225
Cdd:cd19514 77 FGVdHDAVLDniLYARAytseHQMELLDY--VAAKFH--EEAVFR----LLIIDSIMALFRVDF--SGRGELAERQQKLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 226 QEAAVLKYLSQEFCIPVVLTNQITTHVGeklhcpqwnqTDASFEEDS----GfvtaalGNTWSHSVNTRLIVQYEDSERR 301
Cdd:cd19514 147 QMLSRLQKISEEYNVAVFITNQVTADPG----------AAMTFQADPkkpiG------GHILAHASTTRISLRKGRGEER 210
|
250 260
....*....|....*....|....
gi 1207153678 302 QIVIAKSPVAPFAVLSYTIQKEGI 325
Cdd:cd19514 211 IAKIYDSPDLPENEATFAITAGGI 234
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
5-325 |
6.38e-28 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 111.79 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 5 KLRRSGVSADLCERLKRHQLETCQV-------ELSRLAGLSYPAALNLQRLVSKACAPAVITALD-LWKRKEELCFSTSL 76
Cdd:PLN03187 33 KLISQGINAGDVKKLQDAGIYTCNGlmmhtkkNLTGIKGLSEAKVDKICEAAEKLLNQGFITGSDaLLKRKSVVRITTGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 77 PALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDTESAFSAERLVEMAQsRF---PEff 153
Cdd:PLN03187 113 QALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGGGNGKVAYIDTEGTFRPDRIVPIAE-RFgmdAD-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 154 SVKERLleMAARVHLFRELTcqDVLKRL-ERLEEDIIAcragLVILDSVASVVRKEFDTSlpGNLTHRSNFLGQEAAVLK 232
Cdd:PLN03187 190 AVLDNI--IYARAYTYEHQY--NLLLGLaAKMAEEPFR----LLIVDSVIALFRVDFTGR--GELAERQQKLAQMLSRLT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 233 YLSQEFCIPVVLTNQITTHVGeklhcpqwnqtDASFEEDSGfvTAALGNTWSHSVNTRLIVQYEDSERRQIVIAKSPVAP 312
Cdd:PLN03187 260 KIAEEFNVAVYMTNQVIADPG-----------GGMFISDPK--KPAGGHVLAHAATIRLMLRKGKGEQRVCKVFDAPNLP 326
|
330
....*....|...
gi 1207153678 313 FAVLSYTIQKEGI 325
Cdd:PLN03187 327 EAEAEFQITSGGI 339
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
73-253 |
2.16e-26 |
|
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: 104.70 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATlpkSLGGldsGVVYIDTEsAFSAERLVEMAQSRFPef 152
Cdd:cd01394 2 STGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAA---KQGK---KVVYIDTE-GLSPERFQQIAGERFE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 153 fsvkerllEMAARVHLFRELTCQD---VLKRLERLEEDiiaCRAGLVILDSVASVVRKEFDtslpgNLTHRSNFLGQEAA 229
Cdd:cd01394 73 --------SIASNIIVFEPYSFDEqgvAIQEAEKLLKS---DKVDLVVVDSATALYRLELG-----DDSEANRELSRQMS 136
|
170 180
....*....|....*....|....
gi 1207153678 230 VLKYLSQEFCIPVVLTNQITTHVG 253
Cdd:cd01394 137 KLLSIARKYDIPVVITNQVYSDID 160
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
73-253 |
1.96e-25 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 102.25 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLpkslggLDSGVVYIDTESaFSAERLVEMAQSRFPEF 152
Cdd:PRK09361 6 PTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAK------NGKKVIYIDTEG-LSPERFKQIAGEDFEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 153 FSvkeRLLemAARVHLFREltcQDV-LKRLERLEEDiiacRAGLVILDSVASVVRKEFDTSLPGNLTHRSnfLGQEAAVL 231
Cdd:PRK09361 79 LS---NII--IFEPSSFEE---QSEaIRKAEKLAKE----NVGLIVLDSATSLYRLELEDEEDNSKLNRE--LGRQLTHL 144
|
170 180
....*....|....*....|..
gi 1207153678 232 KYLSQEFCIPVVLTNQITTHVG 253
Cdd:PRK09361 145 LKLARKHDLAVVITNQVYSDID 166
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
79-253 |
1.50e-23 |
|
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: 96.72 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 79 LDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATlpkSLGGLdsgVVYIDTEsAFSAERLVEMAQSRFpeffsvkER 158
Cdd:TIGR02237 1 IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNAA---RQGKK---VVYIDTE-GLSPERFKQIAEDRP-------ER 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 159 LLEM--AARVHLFREltcQDVLkrLERLEEDIIACRAGLVILDSVASVVRKEfdtsLPGNLTHRSNFLGQEAAVLKYLSQ 236
Cdd:TIGR02237 67 ALSNfiVFEVFDFDE---QGVA--IQKTSKFIDRDSASLVVVDSFTALYRLE----LSDDRISRNRELARQLTLLLSLAR 137
|
170
....*....|....*..
gi 1207153678 237 EFCIPVVLTNQITTHVG 253
Cdd:TIGR02237 138 KKNLAVVITNQVYTDVN 154
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
90-294 |
1.45e-22 |
|
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: 94.72 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 90 GALTEVTGPSGCGKTQLCMMLSVLATLPKS-----LGGLDSGVVYIDTESAFSAERLVEMAQSRF-----PEFFSVKERL 159
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCILPSSwggvpLGGLEAAVVFIDTDGRFDILRLRSILEARIraaiqAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 160 LEMAA-----RVHLFReltCQD---VLKRLERLEEDIIAC----RAGLVILDSVASVVR-KEFDTSLPG-NLTHRSNFLG 225
Cdd:cd19490 81 VEEIAreclqRLHIFR---CHSslqLLATLLSLENYLLSLsanpELGLLLIDSISAFYWqDRFSAELARaAPLLQEAALR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 226 QEAAVLKYLSQEFCIPVVLTNQ----ITTHVGEKLHCPQWNQTDasfeeDSGFVTAALGNTWSHSVNTRLIVQ 294
Cdd:cd19490 158 AILRELRRLRRRFQLVVIATKQalfpGKSASTDNPAANNAVSKA-----SAPSHREYLPRPWQRLVTHRLVLS 225
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
72-329 |
1.99e-15 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 74.57 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 72 FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCmmLSVLAtlpkslGGLDSG--VVYIDTESafSAERLVEMAQSR- 148
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLA--LQFLA------EGLRRGekGLYVSFEE--SPEQLLRRAESLg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 149 --FPEFfsVKERLLEMaarVHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVasvvrkefdTSLPGNLTHRSNFLGQ 226
Cdd:COG0467 72 ldLEEY--IESGLLRI---IDLSPEELGLDLEELLARLREAVEEFGAKRVVIDSL---------SGLLLALPDPERLREF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 227 EAAVLKYLSQEFCIpVVLTNqitthvgeklhcpqwnqtdasfeEDSGFVTAALGNTWSHSVNTRLIVQYEDSE---RRQI 303
Cdd:COG0467 138 LHRLLRYLKKRGVT-TLLTS-----------------------ETGGLEDEATEGGLSYLADGVILLRYVELGgelRRAL 193
|
250 260
....*....|....*....|....*...
gi 1207153678 304 VIAKSPVAPF--AVLSYTIQKEGIRLEE 329
Cdd:COG0467 194 SVLKMRGSAHdrTIREFEITDGGIEVGE 221
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
82-332 |
1.66e-11 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 64.54 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 82 LLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLD---SGVVYIDTESAFSA--ERLVEMAQSRFPEFFSVK 156
Cdd:COG3598 5 LVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRvppGKVLYLAAEDDRGElrRRLKALGADLGLPFADLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 157 ERLlemaarvHLFRELTCQDVLKRLERLEEDIIACRAGLVILDSVASVvrkefdtsLPGNLtHRSNFLGQEAAVLKYLSQ 236
Cdd:COG3598 85 GRL-------RLLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARV--------FGGDE-NDAEEMRAFLNPLDRLAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 237 EFCIPVVLtnqiTTHVGeKlhcpqwnqtdASFEEDSGfvTAALGNT-WSHSVNTRLIVQY-EDSERRQIVIAKSPVAPFA 314
Cdd:COG3598 149 RTGAAVLL----VHHTG-K----------GGAGKDSG--DRARGSSaLRGAARSVLVLSReKGEDLRVLTRAKSNYGPEI 211
|
250
....*....|....*...
gi 1207153678 315 VLSYTIQKEGIRLEENMN 332
Cdd:COG3598 212 ALRWDNGGRLALEEVAAL 229
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
73-141 |
3.12e-09 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 57.87 E-value: 3.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 73 STSLPALDRLL-HGGLPRGALTEVTGPSGCGKTQLCmmLSVLATLPKsLGGLdsgVVYIDTESAFS---AERL 141
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLA--LHAIAEAQK-AGGI---AAFIDAEHALDpeyAKKL 111
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
73-204 |
1.22e-08 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvLATlpkslgGLDSG--VVYIDTESafSAERLVEMAQSRFP 150
Cdd:cd01124 2 KTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQF--LYA------GAKNGepGLFFTFEE--SPERLLRNAKSFGW 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153678 151 EFFS--VKERLLEMAARVHLFRELTCQDVLKRLERLEEDIIACRaglVILDSVASV 204
Cdd:cd01124 72 DFDEmeDEGKLIIVDAPPTEAGRFSLDELLSRILSIIKSFKAKR---VVIDSLSGL 124
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
72-206 |
2.09e-08 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 53.54 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 72 FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLSVLATLPKSLGGLDS-----GVVYIDTESAFS--AERL--- 141
Cdd:pfam13481 15 LAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPWLGGPRvpeqgKVLYVSAEGPADelRRRLraa 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153678 142 -VEMAQSRFPEFFSVKERLLEMAARvhlFRELTCQDVLKRLERLEEDIiaCRAGLVILDSVASVVR 206
Cdd:pfam13481 95 gADLDLPARLLFLSLVESLPLFFLD---RGGPLLDADVDALEAALEEV--EDPDLVVIDPLARALG 155
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
73-210 |
1.25e-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: 51.86 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvlatLPKSLGGLDSGVVYIDTESafSAERLVEMAQSrfpef 152
Cdd:pfam06745 2 KTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQF-----LYNGALKYGEPGVFVTLEE--PPEDLRENARS----- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153678 153 FSVKERLLE---MAARVHLFRELTCQDVLKR-------LERLEEDIIACRAGLVILDSVASVVRKEFD 210
Cdd:pfam06745 70 FGWDLEKLEeegKLAIIDASTSGIGIAEVEDrfdleelIERLREAIREIGAKRVVIDSITTLFYLLKP 137
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
47-249 |
2.67e-07 |
|
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: 51.38 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 47 RLVSKACAPAVITALDLWKRKEELCFSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLcmMLSVLATLPKSLGgldsG 126
Cdd:cd01121 39 RRASASPSPSKPLPLSDVEAEEEERISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTL--LLQVAARLAQRGG----K 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 127 VVYIdtesafSAERLVEMAQSRFpeffsvkERLLEMAARVHLFRELTCQDVLKRLERLeediiacRAGLVILDSVASVVR 206
Cdd:cd01121 113 VLYV------SGEESLSQIKLRA-------ERLGLGSDNLYLLAETNLEAILAEIEEL-------KPSLVVIDSIQTVYS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207153678 207 KEFDTSlPGNLTHrsnfLGQEAAVLKYLSQEFCIPVVLTNQIT 249
Cdd:cd01121 173 PELTSS-PGSVSQ----VRECAAELLRLAKETGIPVFLVGHVT 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
89-256 |
3.84e-07 |
|
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: 49.29 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 89 RGALTEVTGPSGCGKTQLCMMLSvlatlpKSLGGLDSGVVYIDTESAFSAERLVEMAQSRFPEFFSVkerllemaarvhl 168
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 169 freltcqDVLKRLERLEEDIIACRAGLVILDSVasvvrkefdTSLPGNLTHRSNFLGQEAAVLKYLSQEFCIPVVLTNQI 248
Cdd:smart00382 62 -------SGELRLRLALALARKLKPDVLILDEI---------TSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTND 125
|
....*...
gi 1207153678 249 TTHVGEKL 256
Cdd:smart00382 126 EKDLGPAL 133
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
73-272 |
1.32e-06 |
|
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: 48.83 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLcmmlsvlatlpkslggldsGVVYIdTESAFSAERLVEMAQSRFPEF 152
Cdd:cd19487 2 SSGVPELDELLGGGLERGTSTLLIGPAGVGKSTL-------------------ALQFA-KAAAARGERSVLFSFDESIGT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 153 FSVKERLLEMAARVHLFRELTCQDVLKRLE--------RLEEDIIACRAGLVILDSVASvvrkeFDTSLPgnltHRSNFL 224
Cdd:cd19487 62 LFERSEALGIDLRAMVEKGLLSIEQIDPAElspgefaqRVRTSVEQEDARVVVIDSLNG-----YLNAMP----DERFLI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207153678 225 GQEAAVLKYLSQEfCIPVVLTNQITTHVGEklhcPQWNQTDASFEEDS 272
Cdd:cd19487 133 LQMHELLSYLNNQ-GVTTLLIVAQHGLLGG----DMGTPVDISYLADT 175
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
71-253 |
6.40e-06 |
|
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: 46.78 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 71 CFSTSLPALDRLL-HGGLPRGALTEVTGPSGCGKTQLCmmLSVLATLPKsLGGLdsgVVYIDTESAFS---AERL----- 141
Cdd:cd00983 4 VIPTGSLSLDIALgIGGLPRGRIIEIYGPESSGKTTLA--LHAIAEAQK-LGGT---AAFIDAEHALDpeyAKKLgvdid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 142 -VEMAQsrfPEFfsvKERLLEMAarvhlfreltcqDVLkrlerleediiaCRAG---LVILDSVASVVRK-----EFDTS 212
Cdd:cd00983 78 nLLVSQ---PDT---GEQALEIA------------DTL------------IRSGavdLIVVDSVAALVPKaeiegEMGDS 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207153678 213 LPGnLTHR--SNFLGQEAAVLKYlSQefCIpVVLTNQITTHVG 253
Cdd:cd00983 128 HVG-LQARlmSQALRKLTGSLSK-SK--TT-VIFINQLREKIG 165
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
72-206 |
2.77e-05 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 44.82 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 72 FSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvlatlpkSLGGLDSG--VVYIDTESAfSAERLVEMAQSRF 149
Cdd:COG2874 3 ISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQF--------AYGALENGlsVTYISTELT-TKEFIKQMKSLSY 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153678 150 P--EFFsVKERLL--EMAARVHLFRELTCQDVLKRLERLEEDIIaCRAGLVILDSVASVVR 206
Cdd:COG2874 74 DisDYL-LRGRLLflPVHPLGFEWNSKQRKDLLKRLMKYIASNL-WEADVIIIDSLSALLR 132
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
74-208 |
1.25e-04 |
|
N-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: 410893 [Multi-domain] Cd Length: 226 Bit Score: 42.74 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 74 TSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvlatLPKSLGGLDSGVVYIDTESafSAERLVEMAQS---RFP 150
Cdd:cd19485 3 TGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQF-----LVNGIKEFGEPGVFVTFEE--SPEDIIKNMASfgwDLP 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 151 EFfsVKERLLemaARVHLFRELTCQDVLKR------LERLEEDIIACRAGLVILDSV---------ASVVRKE 208
Cdd:cd19485 76 KL--VAEGKL---LILDASPEPSEEEVTGEydlealLIRIEYAIRKIGAKRVSLDSLeavfsglsdSAVVRAE 143
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
73-136 |
2.78e-04 |
|
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: 42.36 E-value: 2.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153678 73 STSLPALDRLLH-GGLPRGALTEVTGPSGCGKTQLCmmLSVLATLPKsLGGLdsgVVYIDTESAF 136
Cdd:TIGR02012 37 STGSLALDLALGvGGLPKGRIIEIYGPESSGKTTLA--LHAIAEAQK-AGGT---AAFIDAEHAL 95
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
73-104 |
3.14e-04 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 41.84 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|..
gi 1207153678 73 STSLPALDRLLhGGLPRGALTEVTGPSGCGKT 104
Cdd:cd01122 27 WKRFPSLNKLL-KGHRRGELTIFTGPTGSGKT 57
|
|
| recA |
PRK09354 |
recombinase A; Provisional |
72-136 |
3.74e-04 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 42.09 E-value: 3.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153678 72 FST-SLpALDRLL-HGGLPRGALTEVTGPSGCGKTQLCmmLSVLATLPKsLGGLdsgVVYIDTESAF 136
Cdd:PRK09354 41 ISTgSL-ALDIALgIGGLPRGRIVEIYGPESSGKTTLA--LHAIAEAQK-AGGT---AAFIDAEHAL 100
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
74-108 |
4.59e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 42.17 E-value: 4.59e-04
10 20 30
....*....|....*....|....*....|....*
gi 1207153678 74 TSLPALDRLLHGGLPRGALTEVTGPSGCGKTQLCM 108
Cdd:PRK09302 15 TGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFAL 49
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
78-165 |
6.43e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.93 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 78 ALDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvLATLPKSLggldsGVVYIdTESAFSAERLVEM----------AQS 147
Cdd:COG3267 31 ALARLEYALAQGGGFVVLTGEVGTGKTTLLRRL--LERLPDDV-----KVAYI-PNPQLSPAELLRAiadelglepkGAS 102
|
90
....*....|....*...
gi 1207153678 148 RFPEFFSVKERLLEMAAR 165
Cdd:COG3267 103 KADLLRQLQEFLLELAAA 120
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
72-135 |
7.78e-04 |
|
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: 40.85 E-value: 7.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153678 72 FSTSLPALDRLLH-GGLPRGALTEVTGPSGCGKTQLCmmLSVLATLPKsLGGLdsgVVYIDTESA 135
Cdd:pfam00154 33 ISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTTLA--LHAIAEAQK-AGGT---AAFIDAEHA 91
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
58-110 |
1.17e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 39.91 E-value: 1.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1207153678 58 ITALDLWKRKEELCFSTSLPALDRLL-HGGLPRGALTEVTGPS-GCGKTQLCMML 110
Cdd:COG4544 15 IWRGEGLAAAARAVLPTGFAALDAALpGGGLPRGALHEILGPApGIGELGLLLPL 69
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
79-200 |
1.25e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 39.96 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 79 LDRLLHGGLPRGALTEVTGPSGCGKTQLCMMLsvlatlpkSLGGLDSG--VVYIDTESAfSAERLVEMAqsrfpeffSVK 156
Cdd:PRK06067 14 LDRKLGGGIPFPSLILIEGDHGTGKSVLSQQF--------VYGALKQGkkVYVITTENT-SKSYLKQME--------SVK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207153678 157 ERLLEMAAR-------VHLFR-ELTCQDVLKRLERLEEDIIACRAGLVILDS 200
Cdd:PRK06067 77 IDISDFFLWgylrifpLNTEGfEWNSTLANKLLELIIEFIKSKREDVIIIDS 128
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
97-244 |
1.41e-03 |
|
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.
Pssm-ID: 428547 Cd Length: 189 Bit Score: 39.11 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 97 GPSGCGKTQLCMMLSVLATLPKSLGGLDSGVVYIDT-----ESAFSAERLvemAQSRFPefFSVKERLLEMAARV-HLFR 170
Cdd:pfam05621 42 GDSNNGKTMIVERFARLHPPTDDEDAEIVPVVVVQMppkpdEKRLYVAIL---EALGAP--FRPRDRLSKLEQQVlRLLR 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153678 171 eltcqdvlkrlerleediiACRAGLVILDsvasvvrkEFDTSLPGNLTHRSNFLgqeaAVLKYLSQEFCIPVVL 244
Cdd:pfam05621 117 -------------------AVGVRMLIID--------EFHNLLAGSARKQREFL----NVLKSLGNELRIPIVG 159
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
58-106 |
1.83e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.25 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207153678 58 ITALDLWKRKEELCFSTSLPALDRLLHGGLPRGALTEVTGPSGCGKTQL 106
Cdd:PRK09302 241 LTAMRLTQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLL 289
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
58-134 |
1.84e-03 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 39.38 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153678 58 ITALDLWKRKEELcfSTSLPALDRL-LHggLPRGALTEVTGPSGCGKTQLcmmLSVLATLPKslggLDSGVVYIDTES 134
Cdd:cd03293 1 LEVRNVSKTYGGG--GGAVTALEDIsLS--VEEGEFVALVGPSGCGKSTL---LRIIAGLER----PTSGEVLVDGEP 67
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
87-133 |
2.33e-03 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 39.02 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1207153678 87 LPRGALTEVTGPSGCGKTqlcmmlsvlaTLPKSLGGL---DSGVVYIDTE 133
Cdd:cd03261 23 VRRGEILAIIGPSGSGKS----------TLLRLIVGLlrpDSGEVLIDGE 62
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
73-106 |
2.49e-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: 38.87 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....
gi 1207153678 73 STSLPALDRLLHGGLPRGALTEVTGPSGCGKTQL 106
Cdd:cd19488 2 STGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTL 35
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
87-131 |
2.96e-03 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 38.62 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207153678 87 LPRGALTEVTGPSGCGKTQLcmmLSVLATLPKSlgglDSGVVYID 131
Cdd:cd03255 27 IEKGEFVAIVGPSGSGKSTL---LNILGGLDRP----TSGEVRVD 64
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| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
87-149 |
7.24e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.92 E-value: 7.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 87 LPRGALTEVTGPSGCGKTQLCmmlsvLATLPKSLGGLdsgvvYIDTESAFSAERLVEMAQSRF 149
Cdd:cd03238 18 IPLNVLVVVTGVSGSGKSTLV-----NEGLYASGKAR-----LISFLPKFSRNKLIFIDQLQF 70
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|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
87-144 |
7.29e-03 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 37.65 E-value: 7.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 87 LPRGALTEVTGPSGCGKTqlcmmlsvlaTLPKSLGGL---DSGVVYIDTE--SAFSAERLVEM 144
Cdd:COG1127 28 VPRGEILAIIGGSGSGKS----------VLLKLIIGLlrpDSGEILVDGQdiTGLSEKELYEL 80
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
54-131 |
8.37e-03 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 37.38 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 54 APAVITALDLWKRkeelcFST---SLPALDRL-LHggLPRGALTEVTGPSGCGKTQLcmmLSVLAtlpkslgGLD---SG 126
Cdd:COG1116 4 AAPALELRGVSKR-----FPTgggGVTALDDVsLT--VAAGEFVALVGPSGCGKSTL---LRLIA-------GLEkptSG 66
|
....*
gi 1207153678 127 VVYID 131
Cdd:COG1116 67 EVLVD 71
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
75-203 |
8.46e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 37.32 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153678 75 SLPALDRL-LHggLPRGALTEVTGPSGCGKTQLcmmLSVLATLPKSlgglDSGVVYIDTESAFSAerlvemaqsrfpeff 153
Cdd:cd03296 14 DFVALDDVsLD--IPSGELVALLGPSGSGKTTL---LRLIAGLERP----DSGTILFGGEDATDV--------------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153678 154 SVKERLLEMAARVH-LFRELTCQD-------VLKRLERLEEDIIACRA----GLVILDSVAS 203
Cdd:cd03296 70 PVQERNVGFVFQHYaLFRHMTVFDnvafglrVKPRSERPPEAEIRAKVhellKLVQLDWLAD 131
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
75-133 |
8.81e-03 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 37.11 E-value: 8.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153678 75 SLPALDRL-LHggLPRGALTEVTGPSGCGKTqlcmmlsvlaTLPKSLGGL---DSGVVYIDTE 133
Cdd:cd03259 12 SVRALDDLsLT--VEPGEFLALLGPSGCGKT----------TLLRLIAGLerpDSGEILIDGR 62
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