|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
53-289 |
9.53e-98 |
|
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: 288.06 E-value: 9.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 53 DEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYF----NT 128
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 129 EEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqGNLKERNKFLAREASSLKYLA 208
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 209 EEFSIPVILTNQITTHLSGAlasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILQYLDS-ERRQILIAKS 287
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDA-------------------GDGSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKS 220
|
..
gi 1012377119 288 PL 289
Cdd:cd19493 221 PL 222
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
63-274 |
3.17e-61 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 193.72 E-value: 3.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 63 GSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESAFSAERLVEIAESrfprYFNTEEKLLLTSSKVHLY 142
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL------LGGGVVWIDTEGAFPPSRLVQILEA----SPSSELELAEALSRLLYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 143 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDAQLQG--NLKERNKFLAREASSLKYLAEEFSIPVILTN 219
Cdd:cd01393 71 RPPDTLAHLLALDSLPESLFPpPNTSLVVVDSVSALFRKAFPRGGDGdsSSSLRARLLSQLARALQKLAAQFNLAVVVTN 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1012377119 220 QITTHLSGAlasqadlvspaddlslsegtSGSSCVIAALGNTWSHSVNTRLILQY 274
Cdd:cd01393 151 QVTTKIRGG--------------------SGASLVPPALGNTWEHSVSTRLLLYR 185
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
52-288 |
9.91e-50 |
|
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: 166.31 E-value: 9.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 52 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEK 131
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSLPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 132 LLLTSSKVHLYREL-TCDEVLQriESLEEEIISKGIKLVILDSVASVVRKEFDAQlQGNLKERNKFLAREASSLKYLAEE 210
Cdd:cd19491 81 NFLDNIFVEHVADLeTLEHCLN--YQLPALLERGPIRLVVIDSIAALFRSEFDTS-RSDLVERAKYLRRLADHLKRLADK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012377119 211 FSIPVILTNQITTHL-SGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQILIAKSP 288
Cdd:cd19491 158 YNLAVVVVNQVTDRFdSSSDASGLGVLDYLSQFSSFSGGVSGNRKVPALGLTWANLVNTRLMLSRTPKRITDSSAASIS 236
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
27-303 |
3.76e-49 |
|
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: 164.78 E-value: 3.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 27 QTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTE 106
Cdd:pfam08423 4 TTATELHQRRSELIQ---ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 107 SAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAq 185
Cdd:pfam08423 81 GTFRPERLVAIAE----RYgLDPEDVL----DNVAYARAYNSEHQMQLLQQAAAMMSESRFALLIVDSATALYRTDFSG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 186 lQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSG-ALASQADLVSPaddlslsegtsgsscviaALGNTWSH 264
Cdd:pfam08423 152 -RGELAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVDGaAGMFSGDPKKP------------------IGGHIMAH 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 1012377119 265 SVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEG 303
Cdd:pfam08423 213 ASTTRLSLRKGRGEQRICKIYDSPCLPESEAVFAIGSGG 251
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
63-288 |
1.94e-39 |
|
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: 136.97 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 63 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFsaerlveiaesrfpryfnteekllltssKVHLY 142
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF----------------------------NIHYF 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 143 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDaqlqgNLKERNKFLAREASSLKYLAEEFSIPVILTNQI 221
Cdd:cd19492 53 RVHDYVELLALINSLPKFLEDhPKVKLIVVDSIAFPFRHDFD-----DLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1012377119 222 TTHLSgalasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILqYLDSERRQILIAKSP 288
Cdd:cd19492 128 TTKIS---------------------EDGQSQLVPALGESWSHACTTRLFL-TWDEKQRFAHLYKSP 172
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
45-304 |
1.43e-38 |
|
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: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 124
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERLRAIAQR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yFNTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSL 204
Cdd:cd01123 77 -FGLDPDDVL--DNVAYARAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSG--RGELSARQMHLAKFLRML 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 205 KYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILI 284
Cdd:cd01123 152 QRLADEFGVAVVVTNQVVAQVDGAMMFAADPKKPIG------------------GNILAHASTTRLYLRKGRGETRICKI 213
|
250 260
....*....|....*....|
gi 1012377119 285 AKSPLAPFTSFVYTIKEEGL 304
Cdd:cd01123 214 YDSPCLPEAEAVFAITADGV 233
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
2-304 |
2.01e-36 |
|
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: 133.36 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 2 KVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCI 81
Cdd:TIGR02238 38 KIKGLSEAKVDKIKEAASKIINPGFITAFEISQKRKKVLK---ITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 82 MMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRYFNTEEKLLltsSKVHLYRELTCDEVLQRIESLEEEI 161
Cdd:TIGR02238 115 TLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAE----RFGVDPDAVL---DNILYARAYTSEHQMELLDYLAAKF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 162 ISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADd 241
Cdd:TIGR02238 188 SEEPFRLLIVDSIMALFRVDFSG--RGELSERQQKLAQMLSRLNKISEEFNVAVFVTNQVQADPGATMTFIADPKKPIG- 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012377119 242 lslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 304
Cdd:TIGR02238 265 -----------------GHVLAHASTTRILLRKGRGEERVAKLYDSPDMPEAEASFQITEGGI 310
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
3-305 |
2.63e-36 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 133.58 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 3 VTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIM 82
Cdd:PTZ00035 61 IKGISEAKVEKIKEAASKLVPMGFISATEYLEARKNIIR---ITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 83 MSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEI 161
Cdd:PTZ00035 138 LCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAE----RFgLDPEDVL----DNIAYARAYNHEHQMQLLSQAAAKM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 162 ISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADd 241
Cdd:PTZ00035 210 AEERFALLIVDSATALFRVDYSG--RGELAERQQHLGKFLRALQKLADEFNVAVVITNQVMADVDGASMFVADPKKPIG- 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012377119 242 lslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLV 305
Cdd:PTZ00035 287 -----------------GHIIAHASTTRLSLRKGRGEQRICKIYDSPNLPESEAVFAISEGGII 333
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
1-304 |
2.80e-36 |
|
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: 132.93 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 1 MKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFC 80
Cdd:TIGR02239 37 LEIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRQEVIQ---LTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLC 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 81 IMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEE 159
Cdd:TIGR02239 114 HTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----RYgLNPEDVL----DNVAYARAYNTDHQLQLLQQAAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 160 EIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALAS-QADLVSP 238
Cdd:TIGR02239 186 MMSESRFALLIVDSATALYRTDFSG--RGELSARQMHLARFLRSLQRLADEFGVAVVITNQVVAQVDGAGSMfAGDPKKP 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1012377119 239 ADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 304
Cdd:TIGR02239 264 IG------------------GNIMAHASTTRLSLRKGRGEQRICKIYDSPCLPESEAMFAIYEDGI 311
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
45-303 |
3.07e-36 |
|
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: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpR 124
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 Y-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASS 203
Cdd:cd19513 77 YgLNGEDVL----DNVAYARAYNTDHQMQLLIQASAMMAESRYALLIVDSATALYRTDYSG--RGELSARQMHLAKFLRM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 204 LKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQIL 283
Cdd:cd19513 151 LQRLADEFGVAVVITNQVVAQVDGAAMFAGDPKKPIG------------------GNIMAHASTTRLYLRKGRGETRICK 212
|
250 260
....*....|....*....|
gi 1012377119 284 IAKSPLAPFTSFVYTIKEEG 303
Cdd:cd19513 213 IYDSPCLPEAEAVFAITEDG 232
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
3-304 |
7.60e-36 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 132.55 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 3 VTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIM 82
Cdd:PLN03186 66 IKGISEAKVEKILEAASKLVPLGFTTASQLHAQRQEIIQ---ITTGSRELDKILEGGIETGSITEIYGEFRTGKTQLCHT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 83 MSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsRF-------------PRYFNTEEKLlltsskvhlyreltcdE 149
Cdd:PLN03186 143 LCVTCQLPLDQGGGEGKAMYIDTEGTFRPQRLIQIAE-RFglngadvlenvayARAYNTDHQS----------------E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 150 VLQRIESLeeeIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGAL 229
Cdd:PLN03186 206 LLLEAASM---MAETRFALMIVDSATALYRTEFSG--RGELSARQMHLGKFLRSLQRLADEFGVAVVITNQVVAQVDGSA 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012377119 230 ASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 304
Cdd:PLN03186 281 FFAGPQLKPIG------------------GNIMAHASTTRLALRKGRGENRICKVISSPCLPEAEARFSISSEGV 337
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
45-304 |
1.61e-35 |
|
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: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 124
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRIRPIAER---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yFNTEEKLLLTSSkvhLY-RELTCDEVLQRIESLEEEIISKGI-KLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 202
Cdd:cd19514 77 -FGVDHDAVLDNI---LYaRAYTSEHQMELLDYVAAKFHEEAVfRLLIIDSIMALFRVDFSG--RGELAERQQKLAQMLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 203 SLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQI 282
Cdd:cd19514 151 RLQKISEEYNVAVFITNQVTADPGAAMTFQADPKKPIG------------------GHILAHASTTRISLRKGRGEERIA 212
|
250 260
....*....|....*....|..
gi 1012377119 283 LIAKSPLAPFTSFVYTIKEEGL 304
Cdd:cd19514 213 KIYDSPDLPENEATFAITAGGI 234
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
45-305 |
1.41e-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: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpR 124
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERIMQMAKA---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 YFNTEEKLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 202
Cdd:cd19515 78 GLDPDEVL----DNIYVARAYNSNHQMLLVEKA-EDLIKEGnnIKLLIVDSLTSHFRAEYVG--RGTLAERQQKLNKHLH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 203 SLKYLAEEFSIPVILTNQitthlsgalasqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQI 282
Cdd:cd19515 151 DLHRLADLYNIAVLVTNQ---------------VMAKPDAFFGDPTQ------AIGGHILGHAATFRVYLRKGKGGKRIA 209
|
250 260
....*....|....*....|...
gi 1012377119 283 LIAKSPLAPFTSFVYTIKEEGLV 305
Cdd:cd19515 210 RLVDSPHLPEGEAVFRITEKGIE 232
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
28-221 |
2.85e-34 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 127.69 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 28 TAYGIKAQRSadfSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTES 107
Cdd:PRK04301 70 TALEVLERRK---NVGKITTGSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAVYIDTEG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 108 AFSAERLVEIAESrfpRYFNTEEKLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAq 185
Cdd:PRK04301 147 TFRPERIEQMAEA---LGLDPDEVL----DNIHVARAYNSDHQMLLAEKA-EELIKEGenIKLVIVDSLTAHFRAEYVG- 217
|
170 180 190
....*....|....*....|....*....|....*.
gi 1012377119 186 lQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQI 221
Cdd:PRK04301 218 -RGNLAERQQKLNKHLHDLLRLADLYNAAVVVTNQV 252
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
58-287 |
2.26e-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: 119.66 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 58 GGVACGSLTEITGPPGCGKTQFCimMSILATLPTNMGgleGAVVYIDTESAFSAERLVEIAESRfpryFNTEEKLLLTSS 137
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLC--LTAAANVASRSG---QNVLYIDTKSSFSARRLAQILKSR----AQDAEEIDKALQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 138 KVHLYRELTCDEVLQRIESL------EEEIISKGIKLVILDSVASVVRKEFDA--QLQGNLkernkFLAREASSLKYLAE 209
Cdd:cd19489 73 RIRVVRVFDPYELLDLLEELrntlsqQQENLYSRLKLVIIDSLSALISPLLGGskHSEGHA-----LLASLARLLKKLAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 210 EFSIPVILTNQITThlsgalasqadlvspaddlSLSEGTSGSSCviAALGNTWSHSVNTRLILQYLD-----SERRQILI 284
Cdd:cd19489 148 EYQIAVLVTNLTVR-------------------GGDGGQQGSTK--PALGEYWESVPSTRLLLSRDEndpeeSGVCTATL 206
|
...
gi 1012377119 285 AKS 287
Cdd:cd19489 207 LKS 209
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
45-305 |
7.76e-32 |
|
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: 121.00 E-value: 7.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpR 124
Cdd:TIGR02236 77 ITTGSKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENTFRPERIMQMAEA---R 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 YFNTEEKLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG---IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREA 201
Cdd:TIGR02236 154 GLDPDEVL----KNIYVARAYNSNHQMLLVEKA-EDLIKELnnpVKLLIVDSLTSHFRAEYVG--RGALAERQQKLNKHL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 202 SSLKYLAEEFSIPVILTNQitthlsgalasqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQ 281
Cdd:TIGR02236 227 HDLLRLADLYNAAVVVTNQ---------------VMARPDAFFGDPTR------PIGGHILGHAATFRVYLRKGKGDKRI 285
|
250 260
....*....|....*....|....
gi 1012377119 282 ILIAKSPLAPFTSFVYTIKEEGLV 305
Cdd:TIGR02236 286 ARLVDSPHLPEGEAVFRITEKGIE 309
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
45-223 |
1.69e-31 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 117.66 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESaFSAERLVEIAESRFpr 124
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAK------NGKKVIYIDTEG-LSPERFKQIAGEDF-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yfnteEKLLltsSKVHLYRELTCDEVLQRIESLeEEIISKGIKLVILDSVASVVRKEFDAQLQGnlKERNKFLAREASSL 204
Cdd:PRK09361 76 -----EELL---SNIIIFEPSSFEEQSEAIRKA-EKLAKENVGLIVLDSATSLYRLELEDEEDN--SKLNRELGRQLTHL 144
|
170
....*....|....*....
gi 1012377119 205 KYLAEEFSIPVILTNQITT 223
Cdd:PRK09361 145 LKLARKHDLAVVITNQVYS 163
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
45-223 |
1.34e-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: 115.10 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlpTNMGGLegaVVYIDTEsAFSAERLVEIAESRFPR 124
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEA---AKQGKK---VVYIDTE-GLSPERFQQIAGERFES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yfnteeklllTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqlQGNLKERNKFLAREASSL 204
Cdd:cd01394 74 ----------IASNIIVFEPYSFDEQGVAIQEAEKLLKSDKVDLVVVDSATALYRLE-----LGDDSEANRELSRQMSKL 138
|
170
....*....|....*....
gi 1012377119 205 KYLAEEFSIPVILTNQITT 223
Cdd:cd01394 139 LSIARKYDIPVVITNQVYS 157
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
45-309 |
3.95e-29 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 114.49 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 124
Cdd:PLN03187 108 ITTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGGGNGKVAYIDTEGTFRPDRIVPIAER---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yFNTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSL 204
Cdd:PLN03187 184 -FGMDADAVL--DNIIYARAYTYEHQYNLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTG--RGELAERQQKLAQMLSRL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 205 KYLAEEFSIPVILTNQItthlsgalasQADlvsPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQILI 284
Cdd:PLN03187 259 TKIAEEFNVAVYMTNQV----------IAD---PGGGMFISDPKK------PAGGHVLAHAATIRLMLRKGKGEQRVCKV 319
|
250 260
....*....|....*....|....*
gi 1012377119 285 AKSPLAPFTSFVYTIKEEGLVLQDA 309
Cdd:PLN03187 320 FDAPNLPEAEAEFQITSGGIMDAKD 344
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
52-223 |
6.85e-29 |
|
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: 110.58 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 52 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATlptnmgGLEGAVVYIDTEsAFSAERLVEIAESRFPRYFnteek 131
Cdd:TIGR02237 1 IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNAA------RQGKKVVYIDTE-GLSPERFKQIAEDRPERAL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 132 llltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqLQGNLKERNKFLAREASSLKYLAEEF 211
Cdd:TIGR02237 69 -----SNFIVFEVFDFDEQGVAIQKTSKFIDRDSASLVVVDSFTALYRLE----LSDDRISRNRELARQLTLLLSLARKK 139
|
170
....*....|..
gi 1012377119 212 SIPVILTNQITT 223
Cdd:TIGR02237 140 NLAVVITNQVYT 151
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
63-273 |
1.86e-23 |
|
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: 96.26 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 63 GSLTEITGPPGCGKTQFCIMMSILATLPTN-----MGGLEGAVVYIDTESAFSAERLVEIAESRF----------PRYFN 127
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCILPSSwggvpLGGLEAAVVFIDTDGRFDILRLRSILEARIraaiqaanssDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 128 TEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIIS----KGIKLVILDSVAS---VVRKEFDAQLQGNLKERNkFLARE 200
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSlsanPELGLLLIDSISAfywQDRFSAELARAAPLLQEA-ALRAI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012377119 201 ASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSgsscviaALGNTWSHSVNTRLILQ 273
Cdd:cd19490 160 LRELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHRE-------YLPRPWQRLVTHRLVLS 225
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
45-306 |
3.64e-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: 64.98 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILATlptnmGGLEGA-VVYIDTESafSAERLVEIAESRFP 123
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFG--LQFLYA-----GAKNGEpGLFFTFEE--SPERLLRNAKSFGW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 124 --RYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 201
Cdd:cd01124 72 dfDEMEDEGKLIIVDAPPTEAGRFSLDELLSRILS---IIKSFKAKRVVIDSLSG---------LRRAKEDQMRARRIVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 202 SSLKYLAEEFsIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgssCVIaalgntwshsvntRLILQYLDSE-RR 280
Cdd:cd01124 140 ALLNELRAAG-VTTIFTSEMRSFLSSESAGGGDVSFIVD------------GVI-------------LLRYVEIEGElRR 193
|
250 260
....*....|....*....|....*...
gi 1012377119 281 QILIAKSPLAPF--TSFVYTIKEEGLVL 306
Cdd:cd01124 194 TIRVLKMRGTGHdtGTHPFEITDKGIVV 221
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
45-306 |
7.60e-12 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 63.78 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILAtlptnmgglEGA-----VVYIDTESafSAERLVEIAE 119
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLA--LQFLA---------EGLrrgekGLYVSFEE--SPEQLLRRAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 120 SrfpryFNTEEKLLLTSSKVHL------YRELTCDEVLQRIeslEEEIISKGIKLVILDSVASVVRkefdaqLQGNLKER 193
Cdd:COG0467 69 S-----LGLDLEEYIESGLLRIidlspeELGLDLEELLARL---REAVEEFGAKRVVIDSLSGLLL------ALPDPERL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 194 NKFLAReassLKYLAEEFSIPVILTNQITTHLSgalasqadlvspaddlslsegtsgsscviAALGNTWSHSVNTRLILQ 273
Cdd:COG0467 135 REFLHR----LLRYLKKRGVTTLLTSETGGLED-----------------------------EATEGGLSYLADGVILLR 181
|
250 260 270
....*....|....*....|....*....|....*...
gi 1012377119 274 YLDSE---RRQILIAKSPLAPF--TSFVYTIKEEGLVL 306
Cdd:COG0467 182 YVELGgelRRALSVLKMRGSAHdrTIREFEITDGGIEV 219
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
63-297 |
6.82e-10 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 59.14 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 63 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLE---GAVVYIDTESAFSA--ERLVEIAESRFPRYFNTEEKLLLTSs 137
Cdd:COG3598 13 GGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRvppGKVLYLAAEDDRGElrRRLKALGADLGLPFADLDGRLRLLS- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 138 kvhLYRELTCDEVLQRiesLEEEIISKGIKLVILDSVASVvrkefdaqLQGNLKERN---KFLAReassLKYLAEEFSIP 214
Cdd:COG3598 92 ---LAGDLDDTDDLEA---LERAIEEEGPDLVVIDPLARV--------FGGDENDAEemrAFLNP----LDRLAERTGAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 215 VILtnqI--TTHLSGALASQadlvspaddlslsEGTSGSScviaALGNtwshSVNTRLILQYL-DSERRQILIAKSPLAP 291
Cdd:COG3598 154 VLL---VhhTGKGGAGKDSG-------------DRARGSS----ALRG----AARSVLVLSREkGEDLRVLTRAKSNYGP 209
|
....*.
gi 1012377119 292 FTSFVY 297
Cdd:COG3598 210 EIALRW 215
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
46-181 |
1.30e-09 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 58.64 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 46 STTLSALDEAL-HGGVACGSLTEITGPPGCGKTQFCimMSILATLpTNMGGLegaVVYIDTESAFS---AERL-VEIaes 120
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLA--LHAIAEA-QKAGGI---AAFIDAEHALDpeyAKKLgVDI--- 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1012377119 121 rfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKE 181
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 ... |
45-230 |
4.39e-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: 56.39 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTqfcimmSILATLPTNMGGLEGAVVYIdtesafSAERLVEIAESRFPR 124
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKS------TLLLQVAARLAQRGGKVLYV------SGEESLSQIKLRAER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yfnteekLLLTSSKVHLYREltcdevlQRIESLEEEIISKGIKLVILDSVASVVRKEFD------AQLqgnlkernkfla 198
Cdd:cd01121 132 -------LGLGSDNLYLLAE-------TNLEAILAEIEELKPSLVVIDSIQTVYSPELTsspgsvSQV------------ 185
|
170 180 190
....*....|....*....|....*....|...
gi 1012377119 199 RE-ASSLKYLAEEFSIPVILTNQITThlSGALA 230
Cdd:cd01121 186 REcAAELLRLAKETGIPVFLVGHVTK--DGAIA 216
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
52-228 |
9.13e-08 |
|
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: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 52 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSIlatlptnmgglEGAV------VYIDTESafSAERLVEIAES---RF 122
Cdd:pfam06745 8 LDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLY-----------NGALkygepgVFVTLEE--PPEDLRENARSfgwDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 123 PRYFNtEEKLL---LTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqgnlkeRNKFLAr 199
Cdd:pfam06745 75 EKLEE-EGKLAiidASTSGIGIAEVEDRFDLEELIERLREAIREIGAKRVVIDSITTLFYLLKPAVA------REILRR- 146
|
170 180
....*....|....*....|....*....
gi 1012377119 200 eassLKYLAEEFSIPVILTNQITTHLSGA 228
Cdd:pfam06745 147 ----LKRVLKGLGVTAIFTSEKPSGEGGI 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
63-230 |
1.44e-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: 50.06 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 63 GSLTEITGPPGCGKTQfcIMMSILATLPTNMGGlegaVVYIDTESAFSAERLVEIAESRFPRYFNTeekllltsskvhly 142
Cdd:smart00382 2 GEVILIVGPPGSGKTT--LARALARELGPPGGG----VIYIDGEDILEEVLDQLLLIIVGGKKASG-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 143 reltcdEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLareasslkyLAEEFSIPVILTNQIT 222
Cdd:smart00382 62 ------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL---------LKSEKNLTVILTTNDE 126
|
....*...
gi 1012377119 223 THLSGALA 230
Cdd:smart00382 127 KDLGPALL 134
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
44-193 |
1.55e-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: 51.40 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 44 FLSTTLSALDEAL-HGGVACGSLTEITGPPGCGKTQfcIMMSILAtlptNMGGLEGAVVYIDTESAFS---AERL-VEIa 118
Cdd:cd00983 4 VIPTGSLSLDIALgIGGLPRGRIIEIYGPESSGKTT--LALHAIA----EAQKLGGTAAFIDAEHALDpeyAKKLgVDI- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012377119 119 esrfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKefdAQLQGNLKER 193
Cdd:cd00983 77 -----------DNLLVSQPD-------TGEQALEIADTL---IRSGAVDLIVVDSVAALVPK---AEIEGEMGDS 127
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
68-226 |
3.96e-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: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 68 ITGPPGCGKTQFC--IMMSILATLPTNMGglegavvYIDTESAF--SAERLV-------EIAESRFPRYFNTEEKLLLT- 135
Cdd:cd19483 3 IGAGSGIGKSTIVreLAYHLITEHGEKVG-------IISLEESVeeTAKGLAgkhlgkpEPLELPRDDITEEEEDDAFDn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 136 ---SSKVHLYRE---LTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKEfdaqlqgNLKERNKFLAREASSLKYLAE 209
Cdd:cd19483 76 elgSGRFFLYDHfgsLDWDNLKEKIRYM---VKVLGCKVIVLDHLTILVSGL-------DSSDERKELDEIMTELAALVK 145
|
170
....*....|....*..
gi 1012377119 210 EFSIPVILTNqittHLS 226
Cdd:cd19483 146 ELGVTIILVS----HLR 158
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
39-218 |
4.11e-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: 46.61 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 39 DFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSI-LAT----LPTNMGGLEGAVVYIDTE-SAFSAE 112
Cdd:pfam13481 9 DVLADGLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAaVATgkpwLGGPRVPEQGKVLYVSAEgPADELR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 113 RLVEIAESRFPRyfntEEKLLLTSSK--VHLYRELTCDEVLQR-IESLEEEII-SKGIKLVILDSVASVVR-KEFDAqlq 187
Cdd:pfam13481 89 RRLRAAGADLDL----PARLLFLSLVesLPLFFLDRGGPLLDAdVDALEAALEeVEDPDLVVIDPLARALGgDENSN--- 161
|
170 180 190
....*....|....*....|....*....|.
gi 1012377119 188 gnlKERNKFLAReassLKYLAEEFSIPVILT 218
Cdd:pfam13481 162 ---SDVGRLVKA----LDRLARRTGATVLLV 185
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
45-240 |
4.27e-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: 46.91 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlptnMGGLEGAVVYI---DTESAFSAERLVEIAESR 121
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAA-----AARGERSVLFSfdeSIGTLFERSEALGIDLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 122 FpryfntEEKLLLTSSKVHLyRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 201
Cdd:cd19487 76 M------VEKGLLSIEQIDP-AELSPGEFAQRVRT---SVEQEDARVVVIDSLNG---------YLNAMPDERFLILQMH 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1012377119 202 SSLKYLAEEfSIPVILTNQITTHLSGALASQADLVSPAD 240
Cdd:cd19487 137 ELLSYLNNQ-GVTTLLIVAQHGLLGGDMGTPVDISYLAD 174
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
45-221 |
1.25e-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: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALH-GGVACGSLTEITGPPGCGKTQfcIMMSILATLPTNmgglEGAVVYIDTESAFSaerlveiaesrfP 123
Cdd:pfam00154 33 ISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTT--LALHAIAEAQKA----GGTAAFIDAEHALD------------P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 124 RY-----FNTEEklLLTSSKvhlyreltcDEVLQRIESLEEEIISKGIKLVILDSVASVVRKefdAQLQGNLKERNKFL- 197
Cdd:pfam00154 95 VYakklgVDIDN--LLVSQP---------DTGEQALEIADMLVRSGAIDLIVVDSVAALVPK---AEIEGEMGDSHVGLq 160
|
170 180
....*....|....*....|....*...
gi 1012377119 198 AREAS-SLKYLAEEFS---IPVILTNQI 221
Cdd:pfam00154 161 ARLMSqALRKLTGSISksnTTVIFINQI 188
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
44-236 |
4.86e-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: 40.96 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 44 FLSTTLSALDEALHGGVAcGSLTEITGPPGCGKTQFCIMMSIlatlptNMGGLEGAVVYIdtesaFSAE--------RLV 115
Cdd:cd00984 1 GLPTGFTDLDKLTGGLQP-GDLIIIAARPSMGKTAFALNIAE------NIALDEGLPVLF-----FSLEmsaeqlaeRLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 116 eIAESRFPR------YFNTEEKLLLTSSKVHLYRE---------LTCDEVLQRIESLEEEiiSKGIKLVILDSVasvvrk 180
Cdd:cd00984 69 -SSESGVSLsklrtgRLDDEDWERLTAAMGELSELplyiddtpgLTVDEIRAKARRLKRE--HGGLGLIVIDYL------ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012377119 181 efdaQL-QGNLKERNKFLAREASS--LKYLAEEFSIPVILTNQ-------------ITTHL--SGALASQADLV 236
Cdd:cd00984 140 ----QLiRGSKRAENRQQEVAEISrsLKALAKELNVPVIALSQlnrgvesrtdkrpMLSDLreSGSIEQDADVV 209
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
45-194 |
2.48e-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: 38.89 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 45 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGlegavVYIDTESafSAERLVEIAESrfpr 124
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPG-----VFVTFEE--SPEDIIKNMAS---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 125 yFNTEEKLLLTSSK---VHLYRELTCDEVLQR------IESLEEEIISKGIKLVILDSV---------ASVVRKEFdAQL 186
Cdd:cd19485 70 -FGWDLPKLVAEGKlliLDASPEPSEEEVTGEydlealLIRIEYAIRKIGAKRVSLDSLeavfsglsdSAVVRAEL-LRL 147
|
....*...
gi 1012377119 187 QGNLKERN 194
Cdd:cd19485 148 FAWLKQKG 155
|
|
| PRK13853 |
PRK13853 |
type IV secretion system protein VirB4; Provisional |
65-104 |
3.76e-03 |
|
type IV secretion system protein VirB4; Provisional
Pssm-ID: 139913 [Multi-domain] Cd Length: 789 Bit Score: 39.07 E-value: 3.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1012377119 65 LTEITGPPGCGKTQFciMMSILATLPTNMGGLEGAVVYID 104
Cdd:PRK13853 428 MTAIFGPIGRGKTTL--MTFILAMLEQSMVDRAGAVVFFD 465
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
68-217 |
4.18e-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: 37.57 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012377119 68 ITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERL-VEIAESRFPRYFNTEEKLLLTSSKVHLYRELt 146
Cdd:pfam05621 40 LVGDSNNGKTMIVERFARLHPPTDDEDAEIVPVVVVQMPPKPDEKRLyVAILEALGAPFRPRDRLSKLEQQVLRLLRAV- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1012377119 147 cdevlqriesleeeiiskGIKLVILDsvasvvrkEFDAQLQGNLKERNKFLAreasSLKYLAEEFSIPVIL 217
Cdd:pfam05621 119 ------------------GVRMLIID--------EFHNLLAGSARKQREFLN----VLKSLGNELRIPIVG 159
|
|
| |
