|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
94-267 |
1.58e-69 |
|
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: 214.42 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 94 DAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQHVFFLDSTGGFTASRLYQMLQARVEDKEE-------------- 159
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEidkalqrirvvrvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 160 ------------------QVESSAGPLKAVLIDSVSAVLSPLLGG-RQSEGLAIMMQLARELKTLAKEFSVAVVVTNQVT 220
Cdd:cd19489 81 dpyelldlleelrntlsqQQENLYSRLKLVIIDSLSALISPLLGGsKHSEGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 971425752 221 RDSSTG---ALKSALGRSWSFVPSTRVLLQGRAVPWEEGaAPHTACLAKS 267
Cdd:cd19489 161 RGGDGGqqgSTKPALGEYWESVPSTRLLLSRDENDPEES-GVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
100-247 |
3.21e-30 |
|
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: 112.45 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 100 GEVTELAGAPGSGKTQVCLSIAASVsLGLRQHVFFLDSTGGFTASRLYQMLQARVEDKEEQVE----------------- 162
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANA-LLLGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEalsrllyfrppdtlahl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 163 ----------SSAGPLKAVLIDSVSAVLSPLLGGR------QSEGLAIMMQLARELKTLAKEFSVAVVVTNQVTRDSSTG 226
Cdd:cd01393 80 laldslpeslFPPPNTSLVVVDSVSALFRKAFPRGgdgdssSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGG 159
|
170 180
....*....|....*....|....*
gi 971425752 227 A----LKSALGRSWSFVPSTRVLLQ 247
Cdd:cd01393 160 SgaslVPPALGNTWEHSVSTRLLLY 184
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-268 |
1.54e-25 |
|
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: 99.61 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 100 GEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFtasRLYQMlqaRVEDKEEQVE---------SSA 165
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIpkcfgGLAGEAIYIDTEGSF---NIHYF---RVHDYVELLAlinslpkflEDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 166 GPLKAVLIDSVSAVLspllggRQS-EGLAIM----MQLARELKTLAKEFSVAVVVTNQVT---RDSSTGALKSALGRSWS 237
Cdd:cd19492 75 PKVKLIVVDSIAFPF------RHDfDDLAQRtrllNGLAQLLHSLARQHNLAVVLTNQVTtkiSEDGQSQLVPALGESWS 148
|
170 180 190
....*....|....*....|....*....|.
gi 971425752 238 FVPSTRVLLQgravpWEEGAapHTACLAKSP 268
Cdd:cd19492 149 HACTTRLFLT-----WDEKQ--RFAHLYKSP 172
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-268 |
1.03e-23 |
|
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: 96.23 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 90 DQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQARVEDKEEQVESS 164
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMparkgGLDGGVLYIDTESKFSAERLAEIAEARFPEAFSGFMEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 165 AGPLKAVL----------------------------------IDSVSAVLSPLLGGRQSEGLA---IMMQLARELKTLAK 207
Cdd:cd19493 81 NERAEEMLkrvavvrvttlaqllerlpnleehilssgvrlvvIDSIAALVRREFGGSDGEVTErhnALAREASSLKRLAE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971425752 208 EFSVAVVVTNQVTRDSSTGA-----LKSALGRSWSFVPSTRVLLQgravpWEEGAAPHTACLAKSP 268
Cdd:cd19493 161 EFRIAVLVTNQATTHFGDAGdgssgVTAALGDAWAHAVNTRLRLE-----RCLLQLRRVLEIVKSP 221
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
10-219 |
5.48e-22 |
|
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: 93.27 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 10 PGLTEEMIQLLRANNIRTVVDFV---SSDLEDVAQ-SCSLSYKALVAVRRvlLAQFSAFPTnGADLYEElKSSTAILPTG 85
Cdd:TIGR02236 5 PGVGPATAEKLREAGYDTFEAIAvasPKELSEIAGiSEGTAAKIIQAARK--AADLGGFET-ADDVLER-RKTIGKITTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 86 NPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQAR------- 153
Cdd:TIGR02236 81 SKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARgldpdev 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 154 ------------------VEDKEEQVESSAGPLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELKTL---AKEFSV 211
Cdd:TIGR02236 161 lkniyvaraynsnhqmllVEKAEDLIKELNNPVKLLIVDSLTSHFRAEYVGR--GALAERQQkLNKHLHDLlrlADLYNA 238
|
....*...
gi 971425752 212 AVVVTNQV 219
Cdd:TIGR02236 239 AVVVTNQV 246
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
82-237 |
4.11e-21 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 89.15 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-GLRqhVFFLDsTGGFTASRLYQMLQARVE----- 155
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKnGKK--VIYID-TEGLSPERFKQIAGEDFEellsn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 156 -------DKEEQVE--SSAGPLKA-----VLIDSVSAvLSPLLGGRQSEGLAIMMQLARELKTL---AKEFSVAVVVTNQ 218
Cdd:PRK09361 82 iiifepsSFEEQSEaiRKAEKLAKenvglIVLDSATS-LYRLELEDEEDNSKLNRELGRQLTHLlklARKHDLAVVITNQ 160
|
170 180
....*....|....*....|..
gi 971425752 219 VTRDSSTGALKSALGRS---WS 237
Cdd:PRK09361 161 VYSDIDSDGLRPLGGHTlehWS 182
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
66-249 |
7.66e-21 |
|
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: 89.28 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 66 TNGADLYEElKSSTAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQH-----VFFLDSTGG 140
Cdd:pfam08423 4 TTATELHQR-RSELIQITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGggegkALYIDTEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 141 FTASRLYQMLQ---------------ARVEDKEEQVE--------SSAGPLKAVLIDSVSAVLSPLLGGRQ--SEGLAIM 195
Cdd:pfam08423 83 FRPERLVAIAErygldpedvldnvayARAYNSEHQMQllqqaaamMSESRFALLIVDSATALYRTDFSGRGelAERQQHL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971425752 196 MQLARELKTLAKEFSVAVVVTNQVTRDSSTGAL-------KSALGRSWSFVPSTRVLL-QGR 249
Cdd:pfam08423 163 AKFLRTLQRLADEFGVAVVITNQVVAQVDGAAGmfsgdpkKPIGGHIMAHASTTRLSLrKGR 224
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
89-247 |
1.56e-20 |
|
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: 88.12 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 89 LDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQA----------- 152
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelgGLGGGAVYICTESSFPSKRLQQLASSlpkryhlekak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 153 ---------RVEDKEEQVES---------SAGPLKAVLIDSVSAVLSPLLG---GRQSEGLAIMMQLARELKTLAKEFSV 211
Cdd:cd19491 81 nfldnifveHVADLETLEHClnyqlpallERGPIRLVVIDSIAALFRSEFDtsrSDLVERAKYLRRLADHLKRLADKYNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971425752 212 AVVVTNQVT-------------------------RDSSTGALKSALGRSWSFVPSTRVLLQ 247
Cdd:cd19491 161 AVVVVNQVTdrfdsssdasglgvldylsqfssfsGGVSGNRKVPALGLTWANLVNTRLMLS 221
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-219 |
2.39e-19 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 86.08 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 10 PGLTEEMIQLLRANNIRTVVDFVSSDLEDVAQSCSLSYKA----LVAVRRvlLAQFSAFPTnGADLYEELKSsTAILPTG 85
Cdd:PRK04301 12 PGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTaakiIEAARE--AADIGGFET-ALEVLERRKN-VGKITTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 86 NPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQARVEDKE-- 158
Cdd:PRK04301 88 SKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekgGLEGKAVYIDTEGTFRPERIEQMAEALGLDPDev 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 159 -------------------EQVESSAG---PLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELKTL---AKEFSVA 212
Cdd:PRK04301 168 ldnihvaraynsdhqmllaEKAEELIKegeNIKLVIVDSLTAHFRAEYVGR--GNLAERQQkLNKHLHDLlrlADLYNAA 245
|
....*..
gi 971425752 213 VVVTNQV 219
Cdd:PRK04301 246 VVVTNQV 252
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
82-229 |
3.28e-19 |
|
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: 83.90 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVslgLRQH--VFFLDsTGGFTASRLYQMLQARVE---- 155
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEA---AKQGkkVVYID-TEGLSPERFQQIAGERFEsias 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 156 --------DKEEQVE--------SSAGPLKAVLIDSVSAvlspLLGGRQSEGLAIMMQLARELKTL---AKEFSVAVVVT 216
Cdd:cd01394 77 niivfepySFDEQGVaiqeaeklLKSDKVDLVVVDSATA----LYRLELGDDSEANRELSRQMSKLlsiARKYDIPVVIT 152
|
170
....*....|...
gi 971425752 217 NQVTRDSSTGALK 229
Cdd:cd01394 153 NQVYSDIDDDRLK 165
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
17-219 |
1.27e-18 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 84.40 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 17 IQLLRANNIRTVvdfvssdlEDVAQScslSYKALVAVR--------RVLLAQFSAFP---TNGADLYEElKSSTAILPTG 85
Cdd:PLN03186 41 IKKLKDAGIHTV--------ESLAYA---PKKDLLQIKgiseakveKILEAASKLVPlgfTTASQLHAQ-RQEIIQITTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 86 NPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQ-----HVFFLDSTGGFTASRLYQMLQ--------- 151
Cdd:PLN03186 109 SRELDKILEGGIETGSITEIYGEFRTGKTQLCHTLCVTCQLPLDQgggegKAMYIDTEGTFRPQRLIQIAErfglngadv 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 152 ------ARVEDKEEQVE--SSAGPLKA------VLIDSVSAVLSPLLGGRqSEGLAIMMQLA---RELKTLAKEFSVAVV 214
Cdd:PLN03186 189 lenvayARAYNTDHQSEllLEAASMMAetrfalMIVDSATALYRTEFSGR-GELSARQMHLGkflRSLQRLADEFGVAVV 267
|
....*
gi 971425752 215 VTNQV 219
Cdd:PLN03186 268 ITNQV 272
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
82-219 |
1.86e-18 |
|
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: 82.03 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQARVED 156
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeegGLNGKAVYIDTENTFRPERIMQMAKALGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 157 ------------------------KEEQVESSAGPLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELKTL---AKE 208
Cdd:cd19515 81 pdevldniyvaraynsnhqmllveKAEDLIKEGNNIKLLIVDSLTSHFRAEYVGR--GTLAERQQkLNKHLHDLhrlADL 158
|
170
....*....|.
gi 971425752 209 FSVAVVVTNQV 219
Cdd:cd19515 159 YNIAVLVTNQV 169
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
82-227 |
5.84e-18 |
|
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: 81.04 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQMLQ----- 151
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLpidrgGGEGKAIYIDTEGTFRPERLRAIAQrfgld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 152 ----------ARVEDKEEQVE--------SSAGPLKAVLIDSVSAVLSPLLGGRqSEGLAIMMQLA---RELKTLAKEFS 210
Cdd:cd01123 81 pddvldnvayARAFNSDHQTQlldqaaamMVESRFKLLIVDSATALYRTDYSGR-GELSARQMHLAkflRMLQRLADEFG 159
|
170
....*....|....*..
gi 971425752 211 VAVVVTNQVTRDSSTGA 227
Cdd:cd01123 160 VAVVVTNQVVAQVDGAM 176
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
82-220 |
3.68e-16 |
|
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: 75.82 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQ-----HVFFLDSTGGFTASRLYQMLQ----- 151
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQgggegKALYIDTEGTFRPERLLAIAErygln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 152 ----------ARVEDKEEQVE--SSAGPLKA------VLIDSVSAVLSPLLGGRqSEGLAIMMQLARELKTL---AKEFS 210
Cdd:cd19513 81 gedvldnvayARAYNTDHQMQllIQASAMMAesryalLIVDSATALYRTDYSGR-GELSARQMHLAKFLRMLqrlADEFG 159
|
170
....*....|
gi 971425752 211 VAVVVTNQVT 220
Cdd:cd19513 160 VAVVITNQVV 169
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
11-227 |
3.27e-15 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 74.65 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 11 GLTEEMIQLLRANNIRTVvdfvssdlEDVAQSCS--------LSY----KALVAVRRVLLAQFsafpTNGADLYEeLKSS 78
Cdd:PTZ00035 30 GINAADIKKLKEAGICTV--------ESVAYATKkdlcnikgISEakveKIKEAASKLVPMGF----ISATEYLE-ARKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 79 TAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQ-----HVFFLDSTGGFTASRLYQM---- 149
Cdd:PTZ00035 97 IIRITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQgggegKVLYIDTEGTFRPERIVQIaerf 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 150 -----------LQARVEDKEEQVE--SSAGPLKA------VLIDSVSAVLSPLLGGRQ--SEGLAIMMQLARELKTLAKE 208
Cdd:PTZ00035 177 gldpedvldniAYARAYNHEHQMQllSQAAAKMAeerfalLIVDSATALFRVDYSGRGelAERQQHLGKFLRALQKLADE 256
|
250
....*....|....*....
gi 971425752 209 FSVAVVVTNQVTRDSSTGA 227
Cdd:PTZ00035 257 FNVAVVITNQVMADVDGAS 275
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
69-220 |
4.83e-15 |
|
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: 73.99 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 69 ADLYEELKSSTAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQ-----HVFFLDSTGGFTA 143
Cdd:TIGR02239 65 ATEFHQRRQEVIQLTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQLPIDQgggegKALYIDTEGTFRP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 144 SRLYQMLQ---------------ARVEDKEEQVE--SSAGPLKA------VLIDSVSAVLSPLLGGRqSEGLAIMMQLAR 200
Cdd:TIGR02239 145 ERLLAIAEryglnpedvldnvayARAYNTDHQLQllQQAAAMMSesrfalLIVDSATALYRTDFSGR-GELSARQMHLAR 223
|
170 180
....*....|....*....|...
gi 971425752 201 ELKTL---AKEFSVAVVVTNQVT 220
Cdd:TIGR02239 224 FLRSLqrlADEFGVAVVITNQVV 246
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
68-230 |
8.95e-15 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 73.66 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 68 GADLYEELKSSTAIlPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQH-----VFFLDSTGGFT 142
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGggngkVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 143 ASRLYQM---------------LQARVEDKEEQVES--------SAGPLKAVLIDSVSAVLSPLLGGRQ--SEGLAIMMQ 197
Cdd:PLN03187 174 PDRIVPIaerfgmdadavldniIYARAYTYEHQYNLllglaakmAEEPFRLLIVDSVIALFRVDFTGRGelAERQQKLAQ 253
|
170 180 190
....*....|....*....|....*....|...
gi 971425752 198 LARELKTLAKEFSVAVVVTNQVTRDSSTGALKS 230
Cdd:PLN03187 254 MLSRLTKIAEEFNVAVYMTNQVIADPGGGMFIS 286
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
82-250 |
6.37e-14 |
|
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: 69.69 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRLYQM------- 149
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLpgsmgGGGGKVAYIDTEGTFRPDRIRPIaerfgvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 150 --------LQARVEDKEEQVE---------SSAGPLKAVLIDSVSAVLSPLLGGR-----QSEGLAIMMQlarELKTLAK 207
Cdd:cd19514 81 hdavldniLYARAYTSEHQMElldyvaakfHEEAVFRLLIIDSIMALFRVDFSGRgelaeRQQKLAQMLS---RLQKISE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 971425752 208 EFSVAVVVTNQVTRDSSTGAL------KSALGRSWSFVPSTRVLL-QGRA 250
Cdd:cd19514 158 EYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISLrKGRG 207
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
72-250 |
1.30e-13 |
|
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: 69.81 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 72 YEELKSSTAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSL-----GLRQHVFFLDSTGGFTASRL 146
Cdd:TIGR02238 68 ISQKRKKVLKITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLpremgGGNGKVAYIDTEGTFRPDRI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 147 YQM---------------LQARVEDKEEQVE--------SSAGPLKAVLIDSVSAVLSPLLGGR-----QSEGLAIMMQl 198
Cdd:TIGR02238 148 RAIaerfgvdpdavldniLYARAYTSEHQMElldylaakFSEEPFRLLIVDSIMALFRVDFSGRgelseRQQKLAQMLS- 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 971425752 199 arELKTLAKEFSVAVVVTNQVTRDSS------TGALKSALGRSWSFVPSTRVLL-QGRA 250
Cdd:TIGR02238 227 --RLNKISEEFNVAVFVTNQVQADPGatmtfiADPKKPIGGHVLAHASTTRILLrKGRG 283
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
100-248 |
3.06e-11 |
|
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: 61.98 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 100 GEVTELAGAPGSGKTQVCLSIAAS---------VSLGLRQ-HVFFLDSTGGFTASRLYQMLQARV---------EDKEEQ 160
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggVPLGGLEaAVVFIDTDGRFDILRLRSILEARIraaiqaansSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 161 VE----------------SSA-------------------GPLKAVLIDSVSA--------VLSPLLGGRQSEglAIMMQ 197
Cdd:cd19490 81 VEeiareclqrlhifrchSSLqllatllslenyllslsanPELGLLLIDSISAfywqdrfsAELARAAPLLQE--AALRA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971425752 198 LARELKTLAKEFSVAVVVTNQ-----------------VTRDSSTGALKSALGRSWSFVPSTRVLLQG 248
Cdd:cd19490 159 ILRELRRLRRRFQLVVIATKQalfpgksastdnpaannAVSKASAPSHREYLPRPWQRLVTHRLVLSR 226
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
82-221 |
3.58e-08 |
|
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: 53.28 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQHV-FF-------------LDSTGGFTASRL- 146
Cdd:cd00984 2 LPTGFTDLDKLT-GGLQPGDLIIIAARPSMGKTAFALNIAENIALDEGLPVlFFslemsaeqlaerlLSSESGVSLSKLr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 147 --------YQMLQA----------RVEDKE----EQVESSA-------GPLKAVLIDSVSAVLSPLLGG-RQSEGLAIMm 196
Cdd:cd00984 81 tgrlddedWERLTAamgelselplYIDDTPgltvDEIRAKArrlkrehGGLGLIVIDYLQLIRGSKRAEnRQQEVAEIS- 159
|
170 180
....*....|....*....|....*
gi 971425752 197 qlaRELKTLAKEFSVAVVVTNQVTR 221
Cdd:cd00984 160 ---RSLKALAKELNVPVIALSQLNR 181
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
82-203 |
5.55e-08 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 52.23 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAA--------------------------SVSLGLRQHV--- 132
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAeglrrgekglyvsfeespeqllrraeSLGLDLEEYIesg 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971425752 133 --FFLD---STGGFTASRLYQMLQARVEDKEEQVessagplkaVLIDSVSAVLspLLGGRQSEGLAIMMQLARELK 203
Cdd:COG0467 82 llRIIDlspEELGLDLEELLARLREAVEEFGAKR---------VVIDSLSGLL--LALPDPERLREFLHRLLRYLK 146
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
83-219 |
4.09e-07 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 50.55 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 83 PTGNPSLDQLL-DAGLYTGEVTELAGAPGSGKTQVCLSIAASVslglrQH----VFFLDSTGGFT---ASRL----YQML 150
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA-----QKaggiAAFIDAEHALDpeyAKKLgvdiDNLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 151 QARVEDKEEQVE-------SsaGPLKAVLIDSVSAvLSP---LLG--GRQSEGL-AIMM-QLARELKTLAKEFSVAVVVT 216
Cdd:COG0468 120 VSQPDTGEQALEiaetlvrS--GAVDLIVVDSVAA-LVPkaeIEGemGDSHVGLqARLMsQALRKLTGAISKSNTTVIFI 196
|
...
gi 971425752 217 NQV 219
Cdd:COG0468 197 NQL 199
|
|
| PRK08760 |
PRK08760 |
replicative DNA helicase; Provisional |
61-229 |
2.06e-06 |
|
replicative DNA helicase; Provisional
Pssm-ID: 181547 [Multi-domain] Cd Length: 476 Bit Score: 48.76 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 61 FSAFPTNGADLYEELK------SSTAILPTGNPSLDQLlDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQHV-- 132
Cdd:PRK08760 185 FVAMPGALKDAFEELRnrfengGNITGLPTGYNDFDAM-TAGLQPTDLIILAARPAMGKTTFALNIAEYAAIKSKKGVav 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 133 FFLDSTGGFTASRLY--------QMLQ-ARVEDKE-EQVESSAGPLKA--VLIDSVSAVLSPLLGGR-------QSEGLA 193
Cdd:PRK08760 264 FSMEMSASQLAMRLIssngrinaQRLRtGALEDEDwARVTGAIKMLKEtkIFIDDTPGVSPEVLRSKcrrlkreHDLGLI 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 971425752 194 IM--MQL-----------------ARELKTLAKEFSVAVVVTNQVTRDSSTGALK 229
Cdd:PRK08760 344 VIdyLQLmsvpgnsenrateiseiSRSLKGLAKELNVPVIALSQLNRSLETRTDK 398
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-234 |
2.17e-06 |
|
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: 46.60 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 99 TGEVTELAGAPGSGKTQVCLSIAAsvSLGLRQHVFFLDSTGGFTASRLYQMLQARVEDKEEQVESSAGPLKA-------- 170
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR--ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAlalarklk 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971425752 171 ---VLIDSVSAVLSPllggrQSEGLAIMMQLARELKTLAKEFSVAVVVTNQVTRDSSTGALKSALGR 234
Cdd:smart00382 79 pdvLILDEITSLLDA-----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
82-221 |
3.20e-06 |
|
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli 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: 427509 [Multi-domain] Cd Length: 254 Bit Score: 47.41 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQHV-FF-------------LDSTGGFTASRLY 147
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLIIIAARPSMGKTAFALNIARNAAVKHKKPVaIFslemsaeqlvmrlLASEAGVDSQKLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 148 qmlQARVEDKE-EQVESSAGPLKA--VLID-----SVSAVLSPLLGGRQSEGLAIMM----QL----------------- 198
Cdd:pfam03796 81 ---TGQLTDEDwEKLAKAAGRLSEapLYIDdtpglSIAEIRAKARRLKREHGLGLIVidylQLmsggsrgenrqqeisei 157
|
170 180
....*....|....*....|...
gi 971425752 199 ARELKTLAKEFSVAVVVTNQVTR 221
Cdd:pfam03796 158 SRSLKALAKELNVPVIALSQLSR 180
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
82-222 |
3.56e-06 |
|
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: 47.53 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKT----QVCLSIAAS------VS-------LGLRQHVFfldstgGFTAS 144
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKStlllQVAARLAQRggkvlyVSgeeslsqIKLRAERL------GLGSD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 145 RLYQMLQARVEDKEEQVESSAgPlKAVLIDSVSAVLSPLLGG--------RQSeglaimmqlARELKTLAKEFSVAVVVT 216
Cdd:cd01121 138 NLYLLAETNLEAILAEIEELK-P-SLVVIDSIQTVYSPELTSspgsvsqvREC---------AAELLRLAKETGIPVFLV 206
|
....*.
gi 971425752 217 NQVTRD 222
Cdd:cd01121 207 GHVTKD 212
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
97-215 |
3.58e-06 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 47.59 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 97 LYTGEVTELAGAPGSGKTQVCLSIAASVSLG------------------------------------------LRQHVFF 134
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAGgpwlgrrvppgkvlylaaeddrgelrrrlkalgadlglpfadLDGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 135 LDSTGGFTASRLYQMLQARVEdkeeqvessAGPLKAVLIDSVSAVlsplLGGRQSEGlAIMMQLARELKTLAKEFSVAVV 214
Cdd:COG3598 90 LSLAGDLDDTDDLEALERAIE---------EEGPDLVVIDPLARV----FGGDENDA-EEMRAFLNPLDRLAERTGAAVL 155
|
.
gi 971425752 215 V 215
Cdd:COG3598 156 L 156
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
82-203 |
9.72e-06 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 45.72 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLS-IAASVSLG--------------LRQHV--FFLDSTGGFTAS 144
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQfLYAGAKNGepglfftfeesperLLRNAksFGWDFDEMEDEG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971425752 145 RLYQMLQARVEDKEEQVES---------SAGPLKAVLIDSVSAVLSPLLggRQSEGLAIMMQLARELK 203
Cdd:cd01124 81 KLIIVDAPPTEAGRFSLDEllsrilsiiKSFKAKRVVIDSLSGLRRAKE--DQMRARRIVIALLNELR 146
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
82-218 |
2.16e-05 |
|
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: 44.60 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIA-ASVSLGLRQHVFFLDSTGGFTASRLYQM---LQARVEDK 157
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAkAAAARGERSVLFSFDESIGTLFERSEALgidLRAMVEKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 158 EEQVES------SAGPL-------------KAVLIDSVSAVLSPLLGGRqseglAIMMQLARELKTLAKEfSVAVVVTNQ 218
Cdd:cd19487 81 LLSIEQidpaelSPGEFaqrvrtsveqedaRVVVIDSLNGYLNAMPDER-----FLILQMHELLSYLNNQ-GVTTLLIVA 154
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
82-227 |
5.01e-05 |
|
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: 43.77 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAAS-----------VSL-----GLRQHV------------- 132
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNgalkygepgvfVTLeeppeDLRENArsfgwdlekleee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 133 ---FFLDSTGGFTasrlyqmLQARVEDKEEqVESSAGPL---------KAVLIDSVSAvlsplLGGRQSEGLA--IMMQL 198
Cdd:pfam06745 81 gklAIIDASTSGI-------GIAEVEDRFD-LEELIERLreaireigaKRVVIDSITT-----LFYLLKPAVAreILRRL 147
|
170 180
....*....|....*....|....*....
gi 971425752 199 ARELktlaKEFSVAVVVTNQVtRDSSTGA 227
Cdd:pfam06745 148 KRVL----KGLGVTAIFTSEK-PSGEGGI 171
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
69-182 |
2.51e-04 |
|
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: 41.21 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 69 ADLYEELKSSTAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQH----------VFFLDST 138
Cdd:pfam13481 2 AEPLELLDVLADGLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPWLggprvpeqgkVLYVSAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 971425752 139 GGF--TASRLYQMLQARVEDKEEQVESSAGPLKAVLIDSVSAVLSP 182
Cdd:pfam13481 82 GPAdeLRRRLRAAGADLDLPARLLFLSLVESLPLFFLDRGGPLLDA 127
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-123 |
6.47e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.02 E-value: 6.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971425752 61 FSAFPTNGADLyeELKSSTAILPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKTqvclSIAAS 123
Cdd:PRK09302 236 ISVLPLTAMRL--TQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKT----LLASK 292
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
82-222 |
1.04e-03 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 40.45 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAASVSLGLRQHV-FF-------------LDSTGGFTASRLy 147
Cdd:COG0305 174 VPTGFTDLDKLT-GGLQPGDLIILAARPSMGKTAFALNIARNAAIKEGKPVaIFslemsaeqlvmrlLSSEARIDSSKL- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 148 qmLQARVEDKE-EQVESSAGPLKA--VLIDsVSAVLSPL--------LggRQSEGLAIMM----QL-------------- 198
Cdd:COG0305 252 --RTGKLSDEDwERLSSAAGELSEapIYID-DTPGLTIAeirakarrL--KREHGLGLIVidylQLmsgsgrsenrqqei 326
|
170 180
....*....|....*....|....*..
gi 971425752 199 ---ARELKTLAKEFSVAVVVTNQVTRD 222
Cdd:COG0305 327 seiSRSLKALAKELNVPVIALSQLSRA 353
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-124 |
1.26e-03 |
|
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: 39.46 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 971425752 82 LPTGNPSLDQLLDAGLY-TGEVTELAGAPGSGKTQVCLSIAASV 124
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAEA 48
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
84-127 |
2.00e-03 |
|
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410896 [Multi-domain] Cd Length: 225 Bit Score: 38.87 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 971425752 84 TGNPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLS-IAASVSLG 127
Cdd:cd19488 3 TGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQfLLEGAANG 47
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
103-222 |
2.23e-03 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 37.10 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 103 TELAGAPGSGKTQVCLSIAASVSLGlRQHVFFLDstggftasrLYQMLQARVEDKEEQvessaGPLKAVLIDSVSAVLSP 182
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLS-DEPVIFIS---------FLDTILEAIEDLIEE-----KKLDIIIIDSLSSLARA 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 971425752 183 LLGGRQSEGLAIMMqlarELKTLAKEFSVAVVVTNQVTRD 222
Cdd:cd01120 66 SQGDRSSELLEDLA----KLLRAARNTGITVIATIHSDKF 101
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
82-222 |
3.23e-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: 38.12 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKT--QVCLSIAASVSLG--------------LRQHV--FFLDSTgGFTA 143
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTlfAAQFLVNGIKEFGepgvfvtfeespedIIKNMasFGWDLP-KLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971425752 144 SRLYQMLQARVEDKEEQV-------------ESSAGPLKA--VLIDSVSAVLSpllggrqseGLAIMMQLARELKTLA-- 206
Cdd:cd19485 80 EGKLLILDASPEPSEEEVtgeydlealliriEYAIRKIGAkrVSLDSLEAVFS---------GLSDSAVVRAELLRLFaw 150
|
170
....*....|....*..
gi 971425752 207 -KEFSVAVVVTNQVTRD 222
Cdd:cd19485 151 lKQKGVTAIMTGERGED 167
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
82-114 |
7.79e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 37.55 E-value: 7.79e-03
10 20 30
....*....|....*....|....*....|...
gi 971425752 82 LPTGNPSLDQLLDAGLYTGEVTELAGAPGSGKT 114
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKT 45
|
|
| |
