|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
91-327 |
6.23e-96 |
|
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: 286.91 E-value: 6.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 91 DEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYF----NT 166
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 167 EEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqGNLKERNKFLAREASSLKYLA 246
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 247 EEFSIPVILTNQITTHLSGAlasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILQYLDS-ERRQILIAKS 325
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDA-------------------GDGSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKS 220
|
..
gi 1012377115 326 PL 327
Cdd:cd19493 221 PL 222
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
101-312 |
1.36e-58 |
|
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: 189.87 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 101 GSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESAFSAERLVEIAESrfprYFNTEEKLLLTSSKVHLY 180
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL------LGGGVVWIDTEGAFPPSRLVQILEA----SPSSELELAEALSRLLYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 181 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDAQLQG--NLKERNKFLAREASSLKYLAEEFSIPVILTN 257
Cdd:cd01393 71 RPPDTLAHLLALDSLPESLFPpPNTSLVVVDSVSALFRKAFPRGGDGdsSSSLRARLLSQLARALQKLAAQFNLAVVVTN 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1012377115 258 QITTHLSGAlasqadlvspaddlslsegtSGSSCVIAALGNTWSHSVNTRLILQY 312
Cdd:cd01393 151 QVTTKIRGG--------------------SGASLVPPALGNTWEHSVSTRLLLYR 185
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
65-341 |
2.26e-48 |
|
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: 165.55 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 65 QTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTE 144
Cdd:pfam08423 4 TTATELHQRRSELIQ---ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 145 SAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAq 223
Cdd:pfam08423 81 GTFRPERLVAIAE----RYgLDPEDVL----DNVAYARAYNSEHQMQLLQQAAAMMSESRFALLIVDSATALYRTDFSG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 224 lQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSG-ALASQADLVSPaddlslsegtsgsscviaALGNTWSH 302
Cdd:pfam08423 152 -RGELAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVDGaAGMFSGDPKKP------------------IGGHIMAH 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 1012377115 303 SVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEG 341
Cdd:pfam08423 213 ASTTRLSLRKGRGEQRICKIYDSPCLPESEAVFAIGSGG 251
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
90-326 |
7.27e-48 |
|
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: 164.00 E-value: 7.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEK 169
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSLPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 170 LLLTSSKVHLYREL-TCDEVLQriESLEEEIISKGIKLVILDSVASVVRKEFDAQlQGNLKERNKFLAREASSLKYLAEE 248
Cdd:cd19491 81 NFLDNIFVEHVADLeTLEHCLN--YQLPALLERGPIRLVVIDSIAALFRSEFDTS-RSDLVERAKYLRRLADHLKRLADK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012377115 249 FSIPVILTNQITTHL-SGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQILIAKSP 326
Cdd:cd19491 158 YNLAVVVVNQVTDRFdSSSDASGLGVLDYLSQFSSFSGGVSGNRKVPALGLTWANLVNTRLMLSRTPKRITDSSAASIS 236
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
101-326 |
3.20e-38 |
|
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: 136.20 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 101 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFsaerlveiaesrfpryfnteekllltssKVHLY 180
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF----------------------------NIHYF 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 181 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDaqlqgNLKERNKFLAREASSLKYLAEEFSIPVILTNQI 259
Cdd:cd19492 53 RVHDYVELLALINSLPKFLEDhPKVKLIVVDSIAFPFRHDFD-----DLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1012377115 260 TTHLSgalasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILqYLDSERRQILIAKSP 326
Cdd:cd19492 128 TTKIS---------------------EDGQSQLVPALGESWSHACTTRLFL-TWDEKQRFAHLYKSP 172
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
4-342 |
3.31e-38 |
|
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: 140.30 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 4 KKLKRVGlsqelcdrlsrhqILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafL 83
Cdd:TIGR02238 15 KKLKSAG-------------ICTVNGVIMTTRRALCKIKGLSEAKVDKIKEAASKIINPGFITAFEISQKRKKVLK---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 84 STTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY 163
Cdd:TIGR02238 79 TTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAE----RF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 164 FNTEEKLLltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:TIGR02238 155 GVDPDAVL---DNILYARAYTSEHQMELLDYLAAKFSEEPFRLLIVDSIMALFRVDFSG--RGELSERQQKLAQMLSRLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:TIGR02238 230 KISEEFNVAVFVTNQVQADPGATMTFIADPKKPIG------------------GHVLAHASTTRILLRKGRGEERVAKLY 291
|
330
....*....|....*....
gi 1012377115 324 KSPLAPFTSFVYTIKEEGL 342
Cdd:TIGR02238 292 DSPDMPEAEASFQITEGGI 310
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
83-342 |
1.05e-37 |
|
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: 136.89 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 162
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERLRAIAQR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 yFNTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSL 242
Cdd:cd01123 77 -FGLDPDDVL--DNVAYARAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSG--RGELSARQMHLAKFLRML 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 243 KYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILI 322
Cdd:cd01123 152 QRLADEFGVAVVVTNQVVAQVDGAMMFAADPKKPIG------------------GNILAHASTTRLYLRKGRGETRICKI 213
|
250 260
....*....|....*....|
gi 1012377115 323 AKSPLAPFTSFVYTIKEEGL 342
Cdd:cd01123 214 YDSPCLPEAEAVFAITADGV 233
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
5-343 |
2.18e-37 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 138.59 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 5 KLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLS 84
Cdd:PTZ00035 25 KLQSAGINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEAKVEKIKEAASKLVPMGFISATEYLEARKNIIR---IT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 85 TTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY- 163
Cdd:PTZ00035 102 TGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAE----RFg 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 164 FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:PTZ00035 178 LDPEDVL----DNIAYARAYNHEHQMQLLSQAAAKMAEERFALLIVDSATALFRVDYSG--RGELAERQQHLGKFLRALQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:PTZ00035 252 KLADEFNVAVVITNQVMADVDGASMFVADPKKPIG------------------GHIIAHASTTRLSLRKGRGEQRICKIY 313
|
330 340
....*....|....*....|
gi 1012377115 324 KSPLAPFTSFVYTIKEEGLV 343
Cdd:PTZ00035 314 DSPNLPESEAVFAISEGGII 333
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
37-342 |
6.74e-37 |
|
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: 136.78 E-value: 6.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 37 ELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQ 116
Cdd:TIGR02239 35 QLLEIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRQEVIQ---LTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 117 FCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESL 195
Cdd:TIGR02239 112 LCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----RYgLNPEDVL----DNVAYARAYNTDHQLQLLQQA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 196 EEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALAS-QADLV 274
Cdd:TIGR02239 184 AAMMSESRFALLIVDSATALYRTDFSG--RGELSARQMHLARFLRSLQRLADEFGVAVVITNQVVAQVDGAGSMfAGDPK 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012377115 275 SPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 342
Cdd:TIGR02239 262 KPIG------------------GNIMAHASTTRLSLRKGRGEQRICKIYDSPCLPESEAMFAIYEDGI 311
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
37-342 |
1.12e-36 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 137.17 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 37 ELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQ 116
Cdd:PLN03186 62 DLLQIKGISEAKVEKILEAASKLVPLGFTTASQLHAQRQEIIQ---ITTGSRELDKILEGGIETGSITEIYGEFRTGKTQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 117 FCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsRF-------------PRYFNTEEKLlltsskvhlyrel 183
Cdd:PLN03186 139 LCHTLCVTCQLPLDQGGGEGKAMYIDTEGTFRPQRLIQIAE-RFglngadvlenvayARAYNTDHQS------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 184 tcdEVLQRIESLeeeIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHL 263
Cdd:PLN03186 205 ---ELLLEAASM---MAETRFALMIVDSATALYRTEFSG--RGELSARQMHLGKFLRSLQRLADEFGVAVVITNQVVAQV 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012377115 264 SGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 342
Cdd:PLN03186 277 DGSAFFAGPQLKPIG------------------GNIMAHASTTRLALRKGRGENRICKVISSPCLPEAEARFSISSEGV 337
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
83-341 |
2.05e-35 |
|
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: 130.52 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpR 162
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 Y-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASS 241
Cdd:cd19513 77 YgLNGEDVL----DNVAYARAYNTDHQMQLLIQASAMMAESRYALLIVDSATALYRTDYSG--RGELSARQMHLAKFLRM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 242 LKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQIL 321
Cdd:cd19513 151 LQRLADEFGVAVVITNQVVAQVDGAAMFAGDPKKPIG------------------GNIMAHASTTRLYLRKGRGETRICK 212
|
250 260
....*....|....*....|
gi 1012377115 322 IAKSPLAPFTSFVYTIKEEG 341
Cdd:cd19513 213 IYDSPCLPEAEAVFAITEDG 232
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
83-342 |
1.04e-34 |
|
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: 128.63 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 162
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRIRPIAER---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 yFNTEEKLLLTSSkvhLY-RELTCDEVLQRIESLEEEIISKGI-KLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 240
Cdd:cd19514 77 -FGVDHDAVLDNI---LYaRAYTSEHQMELLDYVAAKFHEEAVfRLLIIDSIMALFRVDFSG--RGELAERQQKLAQMLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 241 SLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQI 320
Cdd:cd19514 151 RLQKISEEYNVAVFITNQVTADPGAAMTFQADPKKPIG------------------GHILAHASTTRISLRKGRGEERIA 212
|
250 260
....*....|....*....|..
gi 1012377115 321 LIAKSPLAPFTSFVYTIKEEGL 342
Cdd:cd19514 213 KIYDSPDLPENEATFAITAGGI 234
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-259 |
5.51e-34 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 128.84 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 10 GLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACA-PKMQTAYGIKAQRSadfSPAFLSTTLS 88
Cdd:PRK04301 13 GVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTAAKIIEAAREAADiGGFETALEVLERRK---NVGKITTGSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 89 ALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpRYFNTEE 168
Cdd:PRK04301 90 ELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAVYIDTEGTFRPERIEQMAEA---LGLDPDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 169 KLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLA 246
Cdd:PRK04301 167 VL----DNIHVARAYNSDHQMLLAEKA-EELIKEGenIKLVIVDSLTAHFRAEYVG--RGNLAERQQKLNKHLHDLLRLA 239
|
250
....*....|...
gi 1012377115 247 EEFSIPVILTNQI 259
Cdd:PRK04301 240 DLYNAAVVVTNQV 252
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
83-343 |
8.75e-34 |
|
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: 126.32 E-value: 8.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpR 162
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERIMQMAKA---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 YFNTEEKLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 240
Cdd:cd19515 78 GLDPDEVL----DNIYVARAYNSNHQMLLVEKA-EDLIKEGnnIKLLIVDSLTSHFRAEYVG--RGTLAERQQKLNKHLH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 241 SLKYLAEEFSIPVILTNQitthlsgalasqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQI 320
Cdd:cd19515 151 DLHRLADLYNIAVLVTNQ---------------VMAKPDAFFGDPTQ------AIGGHILGHAATFRVYLRKGKGGKRIA 209
|
250 260
....*....|....*....|...
gi 1012377115 321 LIAKSPLAPFTSFVYTIKEEGLV 343
Cdd:cd19515 210 RLVDSPHLPEGEAVFRITEKGIE 232
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
34-343 |
1.20e-31 |
|
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: 122.54 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 34 SPLELMKVTGLSyRGVHELLCMVSRACAP--KMQTAYGIKAQRSadfSPAFLSTTLSALDEALHGGVACGSLTEITGPPG 111
Cdd:TIGR02236 30 SPKELSEIAGIS-EGTAAKIIQAARKAADlgGFETADDVLERRK---TIGKITTGSKELDELLGGGIETQAITEVFGEFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 112 CGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpRYFNTEEKLlltsSKVHLYRELTCDEVLQR 191
Cdd:TIGR02236 106 SGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENTFRPERIMQMAEA---RGLDPDEVL----KNIYVARAYNSNHQMLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 192 IESLeEEIISKG---IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQitthlsgala 268
Cdd:TIGR02236 179 VEKA-EDLIKELnnpVKLLIVDSLTSHFRAEYVG--RGALAERQQKLNKHLHDLLRLADLYNAAVVVTNQ---------- 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012377115 269 sqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLV 343
Cdd:TIGR02236 246 -----VMARPDAFFGDPTR------PIGGHILGHAATFRVYLRKGKGDKRIARLVDSPHLPEGEAVFRITEKGIE 309
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
96-325 |
1.64e-31 |
|
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: 119.28 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 96 GGVACGSLTEITGPPGCGKTQFCimMSILATLPTNMGgleGAVVYIDTESAFSAERLVEIAESRfpryFNTEEKLLLTSS 175
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLC--LTAAANVASRSG---QNVLYIDTKSSFSARRLAQILKSR----AQDAEEIDKALQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 176 KVHLYRELTCDEVLQRIESL------EEEIISKGIKLVILDSVASVVRKEFDA--QLQGNLkernkFLAREASSLKYLAE 247
Cdd:cd19489 73 RIRVVRVFDPYELLDLLEELrntlsqQQENLYSRLKLVIIDSLSALISPLLGGskHSEGHA-----LLASLARLLKKLAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 248 EFSIPVILTNQITThlsgalasqadlvspaddlSLSEGTSGSSCviAALGNTWSHSVNTRLILQYLD-----SERRQILI 322
Cdd:cd19489 148 EYQIAVLVTNLTVR-------------------GGDGGQQGSTK--PALGEYWESVPSTRLLLSRDEndpeeSGVCTATL 206
|
...
gi 1012377115 323 AKS 325
Cdd:cd19489 207 LKS 209
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
83-261 |
2.94e-31 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 119.20 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESaFSAERLVEIAESRFpr 162
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAK------NGKKVIYIDTEG-LSPERFKQIAGEDF-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 yfnteEKLLltsSKVHLYRELTCDEVLQRIESLeEEIISKGIKLVILDSVASVVRKEFDAQLQGnlKERNKFLAREASSL 242
Cdd:PRK09361 76 -----EELL---SNIIIFEPSSFEEQSEAIRKA-EKLAKENVGLIVLDSATSLYRLELEDEEDN--SKLNRELGRQLTHL 144
|
170
....*....|....*....
gi 1012377115 243 KYLAEEFSIPVILTNQITT 261
Cdd:PRK09361 145 LKLARKHDLAVVITNQVYS 163
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
83-261 |
2.98e-30 |
|
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: 116.26 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlpTNMGGLegaVVYIDTEsAFSAERLVEIAESRFPR 162
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEA---AKQGKK---VVYIDTE-GLSPERFQQIAGERFES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 yfnteeklllTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqlQGNLKERNKFLAREASSL 242
Cdd:cd01394 74 ----------IASNIIVFEPYSFDEQGVAIQEAEKLLKSDKVDLVVVDSATALYRLE-----LGDDSEANRELSRQMSKL 138
|
170
....*....|....*....
gi 1012377115 243 KYLAEEFSIPVILTNQITT 261
Cdd:cd01394 139 LSIARKYDIPVVITNQVYS 157
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
5-343 |
5.36e-30 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 118.73 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 5 KLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSadfSPAFLS 84
Cdd:PLN03187 33 KLISQGINAGDVKKLQDAGIYTCNGLMMHTKKNLTGIKGLSEAKVDKICEAAEKLLNQGFITGSDALLKRK---SVVRIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 85 TTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpryF 164
Cdd:PLN03187 110 TGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGGGNGKVAYIDTEGTFRPDRIVPIAER-----F 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 165 NTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKY 244
Cdd:PLN03187 185 GMDADAVL--DNIIYARAYTYEHQYNLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTG--RGELAERQQKLAQMLSRLTK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 245 LAEEFSIPVILTNQItthlsgalasQADlvsPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQILIAK 324
Cdd:PLN03187 261 IAEEFNVAVYMTNQV----------IAD---PGGGMFISDPKK------PAGGHVLAHAATIRLMLRKGKGEQRVCKVFD 321
|
330
....*....|....*....
gi 1012377115 325 SPLAPFTSFVYTIKEEGLV 343
Cdd:PLN03187 322 APNLPEAEAEFQITSGGIM 340
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
90-261 |
1.98e-28 |
|
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: 110.97 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATlptnmgGLEGAVVYIDTEsAFSAERLVEIAESRFPRYFnteek 169
Cdd:TIGR02237 1 IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNAA------RQGKKVVYIDTE-GLSPERFKQIAEDRPERAL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 170 llltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqLQGNLKERNKFLAREASSLKYLAEEF 249
Cdd:TIGR02237 69 -----SNFIVFEVFDFDEQGVAIQKTSKFIDRDSASLVVVDSFTALYRLE----LSDDRISRNRELARQLTLLLSLARKK 139
|
170
....*....|..
gi 1012377115 250 SIPVILTNQITT 261
Cdd:TIGR02237 140 NLAVVITNQVYT 151
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
101-311 |
2.94e-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: 94.34 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 101 GSLTEITGPPGCGKTQFCIMMSILATLPTN-----MGGLEGAVVYIDTESAFSAERLVEIAESRF----------PRYFN 165
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCILPSSwggvpLGGLEAAVVFIDTDGRFDILRLRSILEARIraaiqaanssDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 166 TEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIIS----KGIKLVILDSVAS---VVRKEFDAQLQGNLKERNkFLARE 238
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSlsanPELGLLLIDSISAfywQDRFSAELARAAPLLQEA-ALRAI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012377115 239 ASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSgsscviaALGNTWSHSVNTRLILQ 311
Cdd:cd19490 160 LRELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHRE-------YLPRPWQRLVTHRLVLS 225
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
83-344 |
1.60e-12 |
|
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: 66.52 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILATlptnmGGLEGA-VVYIDTESafSAERLVEIAESRFP 161
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFG--LQFLYA-----GAKNGEpGLFFTFEE--SPERLLRNAKSFGW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 162 --RYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 239
Cdd:cd01124 72 dfDEMEDEGKLIIVDAPPTEAGRFSLDELLSRILS---IIKSFKAKRVVIDSLSG---------LRRAKEDQMRARRIVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 240 SSLKYLAEEFsIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgssCVIaalgntwshsvntRLILQYLDSE-RR 318
Cdd:cd01124 140 ALLNELRAAG-VTTIFTSEMRSFLSSESAGGGDVSFIVD------------GVI-------------LLRYVEIEGElRR 193
|
250 260
....*....|....*....|....*...
gi 1012377115 319 QILIAKSPLAPF--TSFVYTIKEEGLVL 344
Cdd:cd01124 194 TIRVLKMRGTGHdtGTHPFEITDKGIVV 221
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
83-344 |
5.87e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 64.94 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILAtlptnmgglEGA-----VVYIDTESafSAERLVEIAE 157
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLA--LQFLA---------EGLrrgekGLYVSFEE--SPEQLLRRAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 158 SrfpryFNTEEKLLLTSSKVHL------YRELTCDEVLQRIeslEEEIISKGIKLVILDSVASVVRkefdaqLQGNLKER 231
Cdd:COG0467 69 S-----LGLDLEEYIESGLLRIidlspeELGLDLEELLARL---REAVEEFGAKRVVIDSLSGLLL------ALPDPERL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 232 NKFLAReassLKYLAEEFSIPVILTNQITTHLSgalasqadlvspaddlslsegtsgsscviAALGNTWSHSVNTRLILQ 311
Cdd:COG0467 135 REFLHR----LLRYLKKRGVTTLLTSETGGLED-----------------------------EATEGGLSYLADGVILLR 181
|
250 260 270
....*....|....*....|....*....|....*...
gi 1012377115 312 YLDSE---RRQILIAKSPLAPF--TSFVYTIKEEGLVL 344
Cdd:COG0467 182 YVELGgelRRALSVLKMRGSAHdrTIREFEITDGGIEV 219
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
101-335 |
1.14e-09 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 59.14 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 101 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLE---GAVVYIDTESAFSA--ERLVEIAESRFPRYFNTEEKLLLTSs 175
Cdd:COG3598 13 GGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRvppGKVLYLAAEDDRGElrRRLKALGADLGLPFADLDGRLRLLS- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 176 kvhLYRELTCDEVLQRiesLEEEIISKGIKLVILDSVASVvrkefdaqLQGNLKERN---KFLAReassLKYLAEEFSIP 252
Cdd:COG3598 92 ---LAGDLDDTDDLEA---LERAIEEEGPDLVVIDPLARV--------FGGDENDAEemrAFLNP----LDRLAERTGAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 253 VILtnqI--TTHLSGALASQadlvspaddlslsEGTSGSScviaALGNtwshSVNTRLILQYL-DSERRQILIAKSPLAP 329
Cdd:COG3598 154 VLL---VhhTGKGGAGKDSG-------------DRARGSS----ALRG----AARSVLVLSREkGEDLRVLTRAKSNYGP 209
|
....*.
gi 1012377115 330 FTSFVY 335
Cdd:COG3598 210 EIALRW 215
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
84-219 |
2.18e-09 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 58.64 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 84 STTLSALDEAL-HGGVACGSLTEITGPPGCGKTQFCimMSILATLpTNMGGLegaVVYIDTESAFS---AERL-VEIaes 158
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLA--LHAIAEA-QKAGGI---AAFIDAEHALDpeyAKKLgVDI--- 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1012377115 159 rfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKE 219
Cdd:COG0468 116 ---------DNLLVSQPD-------TGEQALEIAETL---VRSGAVDLIVVDSVAALVPKA 157
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
83-268 |
8.32e-09 |
|
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: 56.00 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTqfcimmSILATLPTNMGGLEGAVVYIdtesafSAERLVEIAESRFPR 162
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKS------TLLLQVAARLAQRGGKVLYV------SGEESLSQIKLRAER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 163 yfnteekLLLTSSKVHLYREltcdevlQRIESLEEEIISKGIKLVILDSVASVVRKEFD------AQLqgnlkernkfla 236
Cdd:cd01121 132 -------LGLGSDNLYLLAE-------TNLEAILAEIEELKPSLVVIDSIQTVYSPELTsspgsvSQV------------ 185
|
170 180 190
....*....|....*....|....*....|...
gi 1012377115 237 RE-ASSLKYLAEEFSIPVILTNQITThlSGALA 268
Cdd:cd01121 186 REcAAELLRLAKETGIPVFLVGHVTK--DGAIA 216
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-231 |
1.21e-07 |
|
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: 52.17 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 82 FLSTTLSALDEAL-HGGVACGSLTEITGPPGCGKTQfcIMMSILAtlptNMGGLEGAVVYIDTESAFS---AERL-VEIa 156
Cdd:cd00983 4 VIPTGSLSLDIALgIGGLPRGRIIEIYGPESSGKTT--LALHAIA----EAQKLGGTAAFIDAEHALDpeyAKKLgVDI- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012377115 157 esrfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKefdAQLQGNLKER 231
Cdd:cd00983 77 -----------DNLLVSQPD-------TGEQALEIADTL---IRSGAVDLIVVDSVAALVPK---AEIEGEMGDS 127
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
90-266 |
1.36e-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: 52.25 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSIlatlptnmgglEGAV------VYIDTESafSAERLVEIAES---RF 160
Cdd:pfam06745 8 LDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLY-----------NGALkygepgVFVTLEE--PPEDLRENARSfgwDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 161 PRYFNtEEKLL---LTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqgnlkeRNKFLAr 237
Cdd:pfam06745 75 EKLEE-EGKLAiidASTSGIGIAEVEDRFDLEELIERLREAIREIGAKRVVIDSITTLFYLLKPAVA------REILRR- 146
|
170 180
....*....|....*....|....*....
gi 1012377115 238 eassLKYLAEEFSIPVILTNQITTHLSGA 266
Cdd:pfam06745 147 ----LKRVLKGLGVTAIFTSEKPSGEGGI 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
101-268 |
1.80e-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: 50.45 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 101 GSLTEITGPPGCGKTQfcIMMSILATLPTNMGGlegaVVYIDTESAFSAERLVEIAESRFPRYFNTeekllltsskvhly 180
Cdd:smart00382 2 GEVILIVGPPGSGKTT--LARALARELGPPGGG----VIYIDGEDILEEVLDQLLLIIVGGKKASG-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 181 reltcdEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLareasslkyLAEEFSIPVILTNQIT 260
Cdd:smart00382 62 ------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL---------LKSEKNLTVILTTNDE 126
|
....*...
gi 1012377115 261 THLSGALA 268
Cdd:smart00382 127 KDLGPALL 134
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
106-264 |
5.85e-07 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 50.26 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 106 ITGPPGCGKTQFC--IMMSILATLPTNMGglegavvYIDTESAF--SAERLV-------EIAESRFPRYFNTEEKLLLT- 173
Cdd:cd19483 3 IGAGSGIGKSTIVreLAYHLITEHGEKVG-------IISLEESVeeTAKGLAgkhlgkpEPLELPRDDITEEEEDDAFDn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 174 ---SSKVHLYRE---LTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKEfdaqlqgNLKERNKFLAREASSLKYLAE 247
Cdd:cd19483 76 elgSGRFFLYDHfgsLDWDNLKEKIRYM---VKVLGCKVIVLDHLTILVSGL-------DSSDERKELDEIMTELAALVK 145
|
170
....*....|....*..
gi 1012377115 248 EFSIPVILTNqittHLS 264
Cdd:cd19483 146 ELGVTIILVS----HLR 158
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
83-278 |
5.05e-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: 47.29 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlptnMGGLEGAVVYI---DTESAFSAERLVEIAESR 159
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAA-----AARGERSVLFSfdeSIGTLFERSEALGIDLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 160 FpryfntEEKLLLTSSKVHLyRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 239
Cdd:cd19487 76 M------VEKGLLSIEQIDP-AELSPGEFAQRVRT---SVEQEDARVVVIDSLNG---------YLNAMPDERFLILQMH 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1012377115 240 SSLKYLAEEfSIPVILTNQITTHLSGALASQADLVSPAD 278
Cdd:cd19487 137 ELLSYLNNQ-GVTTLLIVAQHGLLGGDMGTPVDISYLAD 174
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
77-256 |
7.95e-06 |
|
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: 46.22 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 77 DFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSI-LAT----LPTNMGGLEGAVVYIDTE-SAFSAE 150
Cdd:pfam13481 9 DVLADGLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAaVATgkpwLGGPRVPEQGKVLYVSAEgPADELR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 151 RLVEIAESRFPRyfntEEKLLLTSSK--VHLYRELTCDEVLQR-IESLEEEII-SKGIKLVILDSVASVVRKEFDAQlqg 226
Cdd:pfam13481 89 RRLRAAGADLDL----PARLLFLSLVesLPLFFLDRGGPLLDAdVDALEAALEeVEDPDLVVIDPLARALGGDENSN--- 161
|
170 180 190
....*....|....*....|....*....|
gi 1012377115 227 nlKERNKFLAReassLKYLAEEFSIPVILT 256
Cdd:pfam13481 162 --SDVGRLVKA----LDRLARRTGATVLLV 185
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
83-259 |
1.83e-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: 42.77 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALH-GGVACGSLTEITGPPGCGKTQfcIMMSILATLPTNmgglEGAVVYIDTESAFSaerlveiaesrfP 161
Cdd:pfam00154 33 ISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTT--LALHAIAEAQKA----GGTAAFIDAEHALD------------P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 162 RY-----FNTEEklLLTSSKvhlyreltcDEVLQRIESLEEEIISKGIKLVILDSVASVVRKefdAQLQGNLKERNKFL- 235
Cdd:pfam00154 95 VYakklgVDIDN--LLVSQP---------DTGEQALEIADMLVRSGAIDLIVVDSVAALVPK---AEIEGEMGDSHVGLq 160
|
170 180
....*....|....*....|....*...
gi 1012377115 236 AREAS-SLKYLAEEFS---IPVILTNQI 259
Cdd:pfam00154 161 ARLMSqALRKLTGSISksnTTVIFINQI 188
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
82-274 |
5.29e-04 |
|
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 410864 [Multi-domain] Cd Length: 256 Bit Score: 41.34 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 82 FLSTTLSALDEALHGGVAcGSLTEITGPPGCGKTQFCIMMSIlatlptNMGGLEGAVVYIdtesaFSAE--------RLV 153
Cdd:cd00984 1 GLPTGFTDLDKLTGGLQP-GDLIIIAARPSMGKTAFALNIAE------NIALDEGLPVLF-----FSLEmsaeqlaeRLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 154 eIAESRFPR------YFNTEEKLLLTSSKVHLYRE---------LTCDEVLQRIESLEEEiiSKGIKLVILDSVasvvrk 218
Cdd:cd00984 69 -SSESGVSLsklrtgRLDDEDWERLTAAMGELSELplyiddtpgLTVDEIRAKARRLKRE--HGGLGLIVIDYL------ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012377115 219 efdaQL-QGNLKERNKFLAREASS--LKYLAEEFSIPVILTNQ-------------ITTHL--SGALASQADLV 274
Cdd:cd00984 140 ----QLiRGSKRAENRQQEVAEISrsLKALAKELNVPVIALSQlnrgvesrtdkrpMLSDLreSGSIEQDADVV 209
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
83-232 |
2.56e-03 |
|
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: 39.27 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGlegavVYIDTESafSAERLVEIAES---R 159
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPG-----VFVTFEE--SPEDIIKNMASfgwD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 160 FPRYFNtEEKLLLtsskVHLYRELTCDEVLQR------IESLEEEIISKGIKLVILDSV---------ASVVRKEFdAQL 224
Cdd:cd19485 74 LPKLVA-EGKLLI----LDASPEPSEEEVTGEydlealLIRIEYAIRKIGAKRVSLDSLeavfsglsdSAVVRAEL-LRL 147
|
....*...
gi 1012377115 225 QGNLKERN 232
Cdd:cd19485 148 FAWLKQKG 155
|
|
| PRK13853 |
PRK13853 |
type IV secretion system protein VirB4; Provisional |
103-142 |
6.53e-03 |
|
type IV secretion system protein VirB4; Provisional
Pssm-ID: 139913 [Multi-domain] Cd Length: 789 Bit Score: 38.69 E-value: 6.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1012377115 103 LTEITGPPGCGKTQFciMMSILATLPTNMGGLEGAVVYID 142
Cdd:PRK13853 428 MTAIFGPIGRGKTTL--MTFILAMLEQSMVDRAGAVVFFD 465
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
106-255 |
8.37e-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: 37.18 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377115 106 ITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERL-VEIAESRFPRYFNTEEKLLLTSSKVHLYRELt 184
Cdd:pfam05621 40 LVGDSNNGKTMIVERFARLHPPTDDEDAEIVPVVVVQMPPKPDEKRLyVAILEALGAPFRPRDRLSKLEQQVLRLLRAV- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1012377115 185 cdevlqriesleeeiiskGIKLVILDsvasvvrkEFDAQLQGNLKERNKFLAreasSLKYLAEEFSIPVIL 255
Cdd:pfam05621 119 ------------------GVRMLIID--------EFHNLLAGSARKQREFLN----VLKSLGNELRIPIVG 159
|
|
| |
