|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
94-298 |
2.21e-92 |
|
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: 273.74 E-value: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 94 DAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHVVFLDSTGGFTASRLYQMLQARVEDREEQMEALQRVQVVRVF 173
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 174 DIYEMLRALHEVRDCLSQQVESSAGLLKAVLIDSVSAVLSPLLGG-RQSEGLAIMMQLARELKTLAKEFSVAVLVTNQVT 252
Cdd:cd19489 81 DPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGGsKHSEGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1121940426 253 RDNSTS---ALKSALGRSWSFVPSTRVLLQGRAAPWEEGTAHTACLAKS 298
Cdd:cd19489 161 RGGDGGqqgSTKPALGEYWESVPSTRLLLSRDENDPEESGVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
100-279 |
1.77e-38 |
|
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: 134.79 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 100 GEVTELAGAPGSGKTQVCLSIAANVsLGLRQHVVFLDSTGGFTASRLYQMLQARVEDREEQMEALQRVQVVRVFDIYEML 179
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANA-LLLGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPDTLAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 180 RALhevrDCLsQQVESSAGLLKAVLIDSVSAVLSPLLGGR------QSEGLAIMMQLARELKTLAKEFSVAVLVTNQVTR 253
Cdd:cd01393 80 LAL----DSL-PESLFPPPNTSLVVVDSVSALFRKAFPRGgdgdssSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1121940426 254 D----NSTSALKSALGRSWSFVPSTRVLLQ 279
Cdd:cd01393 155 KirggSGASLVPPALGNTWEHSVSTRLLLY 184
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-299 |
2.38e-32 |
|
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: 119.73 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 90 DQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARV--------ED 156
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMparkgGLDGGVLYIDTESKFSAERLAEIAEARFpeafsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 157 REEQMEALQRVQVVRVFDIYEMLRALHEVRDCLSQqveSSAGLlkaVLIDSVSAVLSPLLGGRQSEGLAIMMQLARE--- 233
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILS---SGVRL---VVIDSIAALVRREFGGSDGEVTERHNALAREass 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121940426 234 LKTLAKEFSVAVLVTNQVTRDNST-----SALKSALGRSWSFVPSTRVLLQGRaapwEEGTAHTACLAKSP 299
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQATTHFGDagdgsSGVTAALGDAWAHAVNTRLRLERC----LLQLRRVLEIVKSP 221
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
10-251 |
5.27e-27 |
|
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: 107.91 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 10 PGLTEEMIQLLRANNIRTVVDFV---SSDLEDVAQNC-SVSYKVLVAVRRvlLAQFSAFPTnGADLYEElKSSTAILPTG 85
Cdd:TIGR02236 5 PGVGPATAEKLREAGYDTFEAIAvasPKELSEIAGISeGTAAKIIQAARK--AADLGGFET-ADDVLER-RKTIGKITTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 86 SPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARVEDREeq 160
Cdd:TIGR02236 81 SKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARGLDPD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 161 mEALQRVQVVRVFDI-YEMLRAlhevrDCLSQQVESSAGLLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELKTL- 237
Cdd:TIGR02236 159 -EVLKNIYVARAYNSnHQMLLV-----EKAEDLIKELNNPVKLLIVDSLTSHFRAEYVGR--GALAERQQkLNKHLHDLl 230
|
250
....*....|....*.
gi 1121940426 238 --AKEFSVAVLVTNQV 251
Cdd:TIGR02236 231 rlADLYNAAVVVTNQV 246
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
82-288 |
1.97e-26 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 104.17 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-GLRqhVVFLDsTGGFTASRLYQMLQARVEdreeq 160
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKnGKK--VIYID-TEGLSPERFKQIAGEDFE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 161 mEALQRVQVVRVFDIYEMLRALHEvrdcLSQQVESSAGLlkaVLIDSVSAvLSPLLGGRQSEGLAIMMQLARELKTL--- 237
Cdd:PRK09361 77 -ELLSNIIIFEPSSFEEQSEAIRK----AEKLAKENVGL---IVLDSATS-LYRLELEDEEDNSKLNRELGRQLTHLlkl 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1121940426 238 AKEFSVAVLVTNQVTRDNSTSALKSALGRS---WS--------FVPSTR--VLLQGRAAPweEG 288
Cdd:PRK09361 148 ARKHDLAVVITNQVYSDIDSDGLRPLGGHTlehWSktilrlekFRNGKRraTLEKHRSRP--EG 209
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-299 |
4.84e-26 |
|
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: 101.53 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 100 GEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFtasrlyqmlqarvedreeqmealqRVQVVRVFD 174
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQIpkcfgGLAGEAIYIDTEGSF------------------------NIHYFRVHD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 175 IYEMLRALHEVRDCLSQQVEssaglLKAVLIDSVSAVLspllggRQS-EGLAIM----MQLARELKTLAKEFSVAVLVTN 249
Cdd:cd19492 57 YVELLALINSLPKFLEDHPK-----VKLIVVDSIAFPF------RHDfDDLAQRtrllNGLAQLLHSLARQHNLAVVLTN 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1121940426 250 QVT---RDNSTSALKSALGRSWSFVPSTRVLLQgraapWEEGTaHTACLAKSP 299
Cdd:cd19492 126 QVTtkiSEDGQSQLVPALGESWSHACTTRLFLT-----WDEKQ-RFAHLYKSP 172
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-251 |
5.38e-26 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 105.34 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 10 PGLTEEMIQLLRANNIRTVVDFVSSDLEDVAQNCSVS----YKVLVAVRRvlLAQFSAFPTnGADLYEELKSsTAILPTG 85
Cdd:PRK04301 12 PGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGestaAKIIEAARE--AADIGGFET-ALEVLERRKN-VGKITTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 86 SPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARVEDREeq 160
Cdd:PRK04301 88 SKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekgGLEGKAVYIDTEGTFRPERIEQMAEALGLDPD-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 161 mEALQRVQVVRVFDIYEMLRALHEVRDcLSQQVESsaglLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELKTL-- 237
Cdd:PRK04301 166 -EVLDNIHVARAYNSDHQMLLAEKAEE-LIKEGEN----IKLVIVDSLTAHFRAEYVGR--GNLAERQQkLNKHLHDLlr 237
|
250
....*....|....*
gi 1121940426 238 -AKEFSVAVLVTNQV 251
Cdd:PRK04301 238 lADLYNAAVVVTNQV 252
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
82-251 |
6.53e-24 |
|
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: 97.82 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARVED 156
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeegGLNGKAVYIDTENTFRPERIMQMAKALGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 157 REeqmEALQRVQVVRVFDIYEMLRALHEVRDcLSQQVESsaglLKAVLIDSVSAVLSPLLGGRqsEGLAIMMQ-LARELK 235
Cdd:cd19515 81 PD---EVLDNIYVARAYNSNHQMLLVEKAED-LIKEGNN----IKLLIVDSLTSHFRAEYVGR--GTLAERQQkLNKHLH 150
|
170
....*....|....*....
gi 1121940426 236 TL---AKEFSVAVLVTNQV 251
Cdd:cd19515 151 DLhrlADLYNIAVLVTNQV 169
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
89-279 |
1.50e-23 |
|
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: 96.98 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 89 LDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARvEDREEQMEA 163
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelgGLGGGAVYICTESSFPSKRLQQLASSL-PKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 164 LQ---RVQVVRVFDIYEMLRALHEVRDCLSQQvessaGLLKAVLIDSVSAVLSPLLG---GRQSEGLAIMMQLARELKTL 237
Cdd:cd19491 80 KNfldNIFVEHVADLETLEHCLNYQLPALLER-----GPIRLVVIDSIAALFRSEFDtsrSDLVERAKYLRRLADHLKRL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1121940426 238 AKEFSVAVLVTNQVTRDNSTSALKS-------------------------ALGRSWSFVPSTRVLLQ 279
Cdd:cd19491 155 ADKYNLAVVVVNQVTDRFDSSSDASglgvldylsqfssfsggvsgnrkvpALGLTWANLVNTRLMLS 221
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
66-281 |
5.30e-23 |
|
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: 95.83 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 66 TNGADLYEElKSSTAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQH-----VVFLDSTGG 140
Cdd:pfam08423 4 TTATELHQR-RSELIQITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGggegkALYIDTEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 141 FTASRLYQMLQARVEDREeqmEALQRVQVVRVFDIYEMLRALHEVRDCLSqqvESSAGLLkavLIDSVSAVLSPLLGGRQ 220
Cdd:pfam08423 83 FRPERLVAIAERYGLDPE---DVLDNVAYARAYNSEHQMQLLQQAAAMMS---ESRFALL---IVDSATALYRTDFSGRG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121940426 221 --SEGLAIMMQLARELKTLAKEFSVAVLVTNQVTRDNSTSAL-------KSALGRSWSFVPSTRVLL-QGR 281
Cdd:pfam08423 154 elAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVDGAAGmfsgdpkKPIGGHIMAHASTTRLSLrKGR 224
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
82-269 |
1.89e-22 |
|
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: 93.15 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVslgLRQH--VVFLDsTGGFTASRLYQMLQARVEdree 159
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEA---AKQGkkVVYID-TEGLSPERFQQIAGERFE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 160 qmEALQRVQVVRVFDIYEMLRALHEVRDCLSqqvESSAGLlkaVLIDSVSAvlspLLGGRQSEGLAIMMQLARELKTL-- 237
Cdd:cd01394 73 --SIASNIIVFEPYSFDEQGVAIQEAEKLLK---SDKVDL---VVVDSATA----LYRLELGDDSEANRELSRQMSKLls 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1121940426 238 -AKEFSVAVLVTNQV---TRDNSTSALKSALGRSWS 269
Cdd:cd01394 141 iARKYDIPVVITNQVysdIDDDRLKPVGGTLLEHWS 176
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
82-254 |
4.86e-21 |
|
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: 89.90 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARVED 156
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLpidrgGGEGKAIYIDTEGTFRPERLRAIAQRFGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 157 REeqmEALQRVQVVRVFDIYEMLRALHEVRDCLSQQVessaglLKAVLIDSVSAVLSPLLGGRqSEGLAIMMQLA---RE 233
Cdd:cd01123 81 PD---DVLDNVAYARAFNSDHQTQLLDQAAAMMVESR------FKLLIVDSATALYRTDYSGR-GELSARQMHLAkflRM 150
|
170 180
....*....|....*....|.
gi 1121940426 234 LKTLAKEFSVAVLVTNQVTRD 254
Cdd:cd01123 151 LQRLADEFGVAVVVTNQVVAQ 171
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
100-297 |
5.76e-21 |
|
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: 89.33 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 100 GEVTELAGAPGSGKTQVCLSIAAN---------VSLGLRQ-HVVFLDSTGGFTASRLYQMLQARV---------EDREEQ 160
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggVPLGGLEaAVVFIDTDGRFDILRLRSILEARIraaiqaansSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 161 ME-----ALQRVQVVRVFDIYEMLRALHEVRDCLSQQveSSAGLLKAVLIDSVSA--------VLSPLLGGRQSEglAIM 227
Cdd:cd19490 81 VEeiareCLQRLHIFRCHSSLQLLATLLSLENYLLSL--SANPELGLLLIDSISAfywqdrfsAELARAAPLLQE--AAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 228 MQLARELKTLAKEFSVAVLVTNQVTRDNSTSALKSALGRSWSFVPSTRVLLQGRAAPWEEGTAHTACLAK 297
Cdd:cd19490 157 RAILRELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHREYLPRPWQRLVTHRLVLSR 226
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
17-251 |
9.94e-19 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 85.55 E-value: 9.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 17 IQLLRANNIRTVVDFVSSDLEDVAQNCSVSY----KVLVAVRRVLLAQFsafpTNGADLYEElKSSTAILPTGSPSLDQL 92
Cdd:PLN03186 41 IKKLKDAGIHTVESLAYAPKKDLLQIKGISEakveKILEAASKLVPLGF----TTASQLHAQ-RQEIIQITTGSRELDKI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 93 LDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQ-----HVVFLDSTGGFTASRLYQMLQARVEDREeqmEALQRV 167
Cdd:PLN03186 116 LEGGIETGSITEIYGEFRTGKTQLCHTLCVTCQLPLDQgggegKAMYIDTEGTFRPQRLIQIAERFGLNGA---DVLENV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 168 QVVRVFDIYEMLRALHEVRdclSQQVESSAGLLkavLIDSVSAVLSPLLGGRqSEGLAIMMQLA---RELKTLAKEFSVA 244
Cdd:PLN03186 193 AYARAYNTDHQSELLLEAA---SMMAETRFALM---IVDSATALYRTEFSGR-GELSARQMHLGkflRSLQRLADEFGVA 265
|
....*..
gi 1121940426 245 VLVTNQV 251
Cdd:PLN03186 266 VVITNQV 272
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
82-252 |
2.31e-18 |
|
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: 82.37 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQ-----HVVFLDSTGGFTASRLYQMLQARVED 156
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQgggegKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 157 REeqmEALQRVQVVRVFDIYEMLRALHEvrdCLSQQVESSAGLLkavLIDSVSAVLSPLLGGRqSEGLAIMMQLARELKT 236
Cdd:cd19513 81 GE---DVLDNVAYARAYNTDHQMQLLIQ---ASAMMAESRYALL---IVDSATALYRTDYSGR-GELSARQMHLAKFLRM 150
|
170
....*....|....*....
gi 1121940426 237 L---AKEFSVAVLVTNQVT 252
Cdd:cd19513 151 LqrlADEFGVAVVITNQVV 169
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
69-252 |
7.67e-18 |
|
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: 82.47 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 69 ADLYEELKSSTAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQ-----HVVFLDSTGGFTA 143
Cdd:TIGR02239 65 ATEFHQRRQEVIQLTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLAVTCQLPIDQgggegKALYIDTEGTFRP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 144 SRLYQMLQARVEDREeqmEALQRVQVVRVFDIYEMLRALHEVRDCLSqqvESSAGLLkavLIDSVSAVLSPLLGGRqSEG 223
Cdd:TIGR02239 145 ERLLAIAERYGLNPE---DVLDNVAYARAYNTDHQLQLLQQAAAMMS---ESRFALL---IVDSATALYRTDFSGR-GEL 214
|
170 180 190
....*....|....*....|....*....|..
gi 1121940426 224 LAIMMQLARELKTL---AKEFSVAVLVTNQVT 252
Cdd:TIGR02239 215 SARQMHLARFLRSLqrlADEFGVAVVITNQVV 246
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
11-254 |
5.12e-17 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 80.43 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 11 GLTEEMIQLLRANNIRTVvdfvssdlEDVAQNCSVSY------------KVLVAVRRVLLAQFsafpTNGADLYEeLKSS 78
Cdd:PTZ00035 30 GINAADIKKLKEAGICTV--------ESVAYATKKDLcnikgiseakveKIKEAASKLVPMGF----ISATEYLE-ARKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 79 TAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQ-----HVVFLDSTGGFTASRLYQMLQAR 153
Cdd:PTZ00035 97 IIRITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQgggegKVLYIDTEGTFRPERIVQIAERF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 154 VEDREeqmEALQRVQVVRVFDIYEMLRALHEVRdclSQQVESSAGLLkavLIDSVSAVLSPLLGGRQ--SEGLAIMMQLA 231
Cdd:PTZ00035 177 GLDPE---DVLDNIAYARAYNHEHQMQLLSQAA---AKMAEERFALL---IVDSATALFRVDYSGRGelAERQQHLGKFL 247
|
250 260
....*....|....*....|...
gi 1121940426 232 RELKTLAKEFSVAVLVTNQVTRD 254
Cdd:PTZ00035 248 RALQKLADEFNVAVVITNQVMAD 270
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
82-282 |
3.33e-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: 70.85 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRLYQMLQARVED 156
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLpgsmgGGGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 157 REeqmEALQRVQVVRVFDIYEMLralhEVRDCLSQQVESSAgLLKAVLIDSVSAVLSPLLGGR-----QSEGLAIMMQla 231
Cdd:cd19514 81 HD---AVLDNILYARAYTSEHQM----ELLDYVAAKFHEEA-VFRLLIIDSIMALFRVDFSGRgelaeRQQKLAQMLS-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1121940426 232 rELKTLAKEFSVAVLVTNQVTRDNSTSAL------KSALGRSWSFVPSTRVLL-QGRA 282
Cdd:cd19514 151 -RLQKISEEYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISLrKGRG 207
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
72-302 |
2.17e-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: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 72 YEELKSSTAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSL-----GLRQHVVFLDSTGGFTASRL 146
Cdd:TIGR02238 68 ISQKRKKVLKITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLpremgGGNGKVAYIDTEGTFRPDRI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 147 YQMLQARVEDREeqmEALQRVQVVRVFD---IYEMLRALHEvrdclsqqvESSAGLLKAVLIDSVSAVLSPLLGGR---- 219
Cdd:TIGR02238 148 RAIAERFGVDPD---AVLDNILYARAYTsehQMELLDYLAA---------KFSEEPFRLLIVDSIMALFRVDFSGRgels 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 220 -QSEGLAIMMQlarELKTLAKEFSVAVLVTNQVTRDNSTSAL------KSALGRSWSFVPSTRVLL-QGRaapweeGTAH 291
Cdd:TIGR02238 216 eRQQKLAQMLS---RLNKISEEFNVAVFVTNQVQADPGATMTfiadpkKPIGGHVLAHASTTRILLrKGR------GEER 286
|
250
....*....|.
gi 1121940426 292 TACLAKSPRQP 302
Cdd:TIGR02238 287 VAKLYDSPDMP 297
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
68-254 |
6.22e-13 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 68.65 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 68 GADLYEELKSSTAIlPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQH-----VVFLDSTGGFT 142
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGggngkVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 143 ASRLYQMLQARVEDREeqmEALQRVQVVRVFDIYEMLRALhevrdcLSQQVESSAGLLKAVLIDSVSAVLSPLLGGRQ-- 220
Cdd:PLN03187 174 PDRIVPIAERFGMDAD---AVLDNIIYARAYTYEHQYNLL------LGLAAKMAEEPFRLLIVDSVIALFRVDFTGRGel 244
|
170 180 190
....*....|....*....|....*....|....
gi 1121940426 221 SEGLAIMMQLARELKTLAKEFSVAVLVTNQVTRD 254
Cdd:PLN03187 245 AERQQKLAQMLSRLTKIAEEFNVAVYMTNQVIAD 278
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
82-252 |
1.93e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 62.63 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANvslGLRQ--HVVFLdstgGFTASR--LYQMLQARVEDR 157
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAE---GLRRgeKGLYV----SFEESPeqLLRRAESLGLDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 158 EEQMEAlQRVQVVRVFDIyEMLRALHEVRDCLSQQVESSAGllKAVLIDSVSAVLspLLGGRQSEGLAIMMQLARELKTL 237
Cdd:COG0467 75 EEYIES-GLLRIIDLSPE-ELGLDLEELLARLREAVEEFGA--KRVVIDSLSGLL--LALPDPERLREFLHRLLRYLKKR 148
|
170
....*....|....*
gi 1121940426 238 akefSVAVLVTNQVT 252
Cdd:COG0467 149 ----GVTTLLTSETG 159
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
82-253 |
1.29e-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: 54.83 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHVVF--------------LDSTGGFTASRL- 146
Cdd:cd00984 2 LPTGFTDLDKLT-GGLQPGDLIIIAARPSMGKTAFALNIAENIALDEGLPVLFfslemsaeqlaerlLSSESGVSLSKLr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 147 --YQMLqarvEDREEQMEALQRVQVVRVF-DIYEMLRaLHEVRDcLSQQVESSAGLLKAVLIDSVSAVLSPLLGG-RQSE 222
Cdd:cd00984 81 tgRLDD----EDWERLTAAMGELSELPLYiDDTPGLT-VDEIRA-KARRLKREHGGLGLIVIDYLQLIRGSKRAEnRQQE 154
|
170 180 190
....*....|....*....|....*....|.
gi 1121940426 223 GLAIMmqlaRELKTLAKEFSVAVLVTNQVTR 253
Cdd:cd00984 155 VAEIS----RSLKALAKELNVPVIALSQLNR 181
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
83-251 |
1.62e-08 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 55.18 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 83 PTGSPSLDQLL-DAGLYTGEVTELAGAPGSGKTQVCLSIAANVslglrQH----VVFLDSTGGFT---ASRL----YQML 150
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA-----QKaggiAAFIDAEHALDpeyAKKLgvdiDNLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 151 QARVEDREEQMEalqrvqvvrvfdIYEMLralhevrdclsqqVESSAglLKAVLIDSVSAvLSP---LLG--GRQSEGL- 224
Cdd:COG0468 120 VSQPDTGEQALE------------IAETL-------------VRSGA--VDLIVVDSVAA-LVPkaeIEGemGDSHVGLq 171
|
170 180
....*....|....*....|....*...
gi 1121940426 225 AIMM-QLARELKTLAKEFSVAVLVTNQV 251
Cdd:COG0468 172 ARLMsQALRKLTGAISKSNTTVIFINQL 199
|
|
| PRK08760 |
PRK08760 |
replicative DNA helicase; Provisional |
61-261 |
2.43e-08 |
|
replicative DNA helicase; Provisional
Pssm-ID: 181547 [Multi-domain] Cd Length: 476 Bit Score: 54.92 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 61 FSAFPTNGADLYEELK------SSTAILPTGSPSLDQLlDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHV-V 133
Cdd:PRK08760 185 FVAMPGALKDAFEELRnrfengGNITGLPTGYNDFDAM-TAGLQPTDLIILAARPAMGKTTFALNIAEYAAIKSKKGVaV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 134 F-------------LDSTGGFTASRLyQMLQARVEDREEQMEALQRVQVVRVF--DI----YEMLRAlhevrDCLSQQVE 194
Cdd:PRK08760 264 FsmemsasqlamrlISSNGRINAQRL-RTGALEDEDWARVTGAIKMLKETKIFidDTpgvsPEVLRS-----KCRRLKRE 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1121940426 195 SSAGLlkaVLIDSVSAVLSPllgGRQSEGLAIMMQLARELKTLAKEFSVAVLVTNQVTRDNSTSALK 261
Cdd:PRK08760 338 HDLGL---IVIDYLQLMSVP---GNSENRATEISEISRSLKGLAKELNVPVIALSQLNRSLETRTDK 398
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
82-253 |
1.44e-07 |
|
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: 51.65 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHVVF--------------LDSTGGFTASRLY 147
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLIIIAARPSMGKTAFALNIARNAAVKHKKPVAIfslemsaeqlvmrlLASEAGVDSQKLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 148 qmlQARVEDRE-----EQMEALQRVQV-------VRVFDIYEMLRALHEVRDclsqqvessaglLKAVLIDS---VSAvl 212
Cdd:pfam03796 81 ---TGQLTDEDweklaKAAGRLSEAPLyiddtpgLSIAEIRAKARRLKREHG------------LGLIVIDYlqlMSG-- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1121940426 213 SPLLGGRQSEGLAImmqlARELKTLAKEFSVAVLVTNQVTR 253
Cdd:pfam03796 144 GSRGENRQQEISEI----SRSLKALAKELNVPVIALSQLSR 180
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
69-256 |
6.19e-07 |
|
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: 48.92 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 69 ADLYEELKSSTAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQH----------VVFLDST 138
Cdd:pfam13481 2 AEPLELLDVLADGLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPWLggprvpeqgkVLYVSAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 139 GGF--TASRLYQMLQARVEDREEQmeALQRVQVVRVFDIYEMLRALHEVRDCLSQQVESSAGlLKAVLIDSVSAVLspll 216
Cdd:pfam13481 82 GPAdeLRRRLRAAGADLDLPARLL--FLSLVESLPLFFLDRGGPLLDADVDALEAALEEVED-PDLVVIDPLARAL---- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1121940426 217 gGRQSEGLAIMMQLARELKTLAKEFSVAVLVTNQVTRDNS 256
Cdd:pfam13481 155 -GGDENSNSDVGRLVKALDRLARRTGATVLLVHHVGKDGA 193
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
82-235 |
1.61e-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: 48.41 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLS-IAANVSLGlrQHVVFLdstgGFTASRlyQMLQAR---VEDR 157
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQfLYAGAKNG--EPGLFF----TFEESP--ERLLRNaksFGWD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121940426 158 EEQMEALQRVQVVRvFDIYEMLRA-LHEVRDCLSQQVESsaGLLKAVLIDSVSAVLSPLLggRQSEGLAIMMQLARELK 235
Cdd:cd01124 73 FDEMEDEGKLIIVD-APPTEAGRFsLDELLSRILSIIKS--FKAKRVVIDSLSGLRRAKE--DQMRARRIVIALLNELR 146
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
82-235 |
3.98e-06 |
|
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: 47.24 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAAN-----------VSL-----GLRQHVVFLdstgGFTASR 145
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNgalkygepgvfVTLeeppeDLRENARSF----GWDLEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 146 LYQMLQARVEDREEQMEALQRvqVVRVFDIYEMLRAL-HEVRDclsqqvessaglLKA--VLIDSVSAvlsplLGGRQSE 222
Cdd:pfam06745 77 LEEEGKLAIIDASTSGIGIAE--VEDRFDLEELIERLrEAIRE------------IGAkrVVIDSITT-----LFYLLKP 137
|
170
....*....|....*
gi 1121940426 223 GLA--IMMQLARELK 235
Cdd:pfam06745 138 AVAreILRRLKRVLK 152
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
97-247 |
1.12e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 46.43 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 97 LYTGEVTELAGAPGSGKTQVCLSIAANVSLGL--------RQHVVFLDS--TGGFTASRLYQMLQARVEDREEQMEALQR 166
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGpwlgrrvpPGKVLYLAAedDRGELRRRLKALGADLGLPFADLDGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 167 VQVVRVFDIYEMLRALHevrdclsQQVESSAglLKAVLIDSVSAVlsplLGGRQSEGlAIMMQLARELKTLAKEFSVAVL 246
Cdd:COG3598 90 LSLAGDLDDTDDLEALE-------RAIEEEG--PDLVVIDPLARV----FGGDENDA-EEMRAFLNPLDRLAERTGAAVL 155
|
.
gi 1121940426 247 V 247
Cdd:COG3598 156 L 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-266 |
2.91e-05 |
|
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: 43.52 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 99 TGEVTELAGAPGSGKTQVCLSIAANvsLGLRQHVVFLDSTGGFtasRLYQMLQARVEDREEQMEALQRVQVVRvfDIYEM 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE--LGPPGGGVIYIDGEDI---LEEVLDQLLLIIVGGKKASGSGELRLR--LALAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 179 LRALHevrdclsqqvessaglLKAVLIDSVSAvlsplLGGRQSEGLAIMMQLARELKTLAKEFSVAVLVTNQVTRDNSTS 258
Cdd:smart00382 74 ARKLK----------------PDVLILDEITS-----LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
....*...
gi 1121940426 259 ALKSALGR 266
Cdd:smart00382 133 LLRRRFDR 140
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-124 |
8.30e-05 |
|
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: 43.31 E-value: 8.30e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1121940426 82 LPTGSPSLDQLLDAGLY-TGEVTELAGAPGSGKTQVCLSIAANV 124
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAEA 48
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
82-134 |
1.16e-04 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 43.53 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1121940426 82 LPTGSPSLDQLLdAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHVVF 134
Cdd:COG0305 174 VPTGFTDLDKLT-GGLQPGDLIILAARPSMGKTAFALNIARNAAIKEGKPVAI 225
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
82-250 |
5.55e-04 |
|
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: 40.75 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIA-ANVSLGLRQHVVFLDSTGGFTASRLYQM---LQARVEDR 157
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAkAAAARGERSVLFSFDESIGTLFERSEALgidLRAMVEKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 158 E---EQMEALQrvqvvrvfdiYEMLRALHEVRDclsqQVESSAglLKAVLIDSVSAVLSPLLGGRqseglAIMMQLAREL 234
Cdd:cd19487 81 LlsiEQIDPAE----------LSPGEFAQRVRT----SVEQED--ARVVVIDSLNGYLNAMPDER-----FLILQMHELL 139
|
170
....*....|....*.
gi 1121940426 235 KTLAKEfSVAVLVTNQ 250
Cdd:cd19487 140 SYLNNQ-GVTTLLIVA 154
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-114 |
6.06e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.40 E-value: 6.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1121940426 61 FSAFPTNGADLyeELKSSTAILPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKT 114
Cdd:PRK09302 236 ISVLPLTAMRL--TQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKT 287
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
82-256 |
7.91e-04 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 40.59 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQhVVFLdsTG--------------GFTASRLY 147
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGK-VLYV--SGeeslsqiklraerlGLGSDNLY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 148 QMLQARVEDREEQMEALQrVQVVRVFDIYEMlralhevrdcLSQQVESSAGllkavlidSVSAVlspllggRQSeglaim 227
Cdd:cd01121 141 LLAETNLEAILAEIEELK-PSLVVIDSIQTV----------YSPELTSSPG--------SVSQV-------REC------ 188
|
170 180
....*....|....*....|....*....
gi 1121940426 228 mqlARELKTLAKEFSVAVLVTNQVTRDNS 256
Cdd:cd01121 189 ---AAELLRLAKETGIPVFLVGHVTKDGA 214
|
|
| Las1 |
pfam04031 |
Las1-like; Las1 is an essential nuclear protein involved in cell morphogenesis and cell ... |
146-240 |
1.30e-03 |
|
Las1-like; Las1 is an essential nuclear protein involved in cell morphogenesis and cell surface growth.
Pssm-ID: 461138 Cd Length: 148 Bit Score: 38.72 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 146 LYQMLQARVEDREEQMEALQRVQVVRVfdiyemlralhevRDCLSQQVESSAGLLKAVLIDSVSAVLSPLLGGRQSEGLA 225
Cdd:pfam04031 12 VRQWLYDDSDDPDARRRALNRVSAWKS-------------RGNLPHAVESTALLLEAILLDEEGSLGGSEYELRLLYSMA 78
|
90 100
....*....|....*....|....*..
gi 1121940426 226 IM------------MQLARELKTLAKE 240
Cdd:pfam04031 79 IVrfvnglldpkqkGQYAISMASLAKE 105
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
82-254 |
1.80e-03 |
|
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410893 [Multi-domain] Cd Length: 226 Bit Score: 39.27 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKTQVCLSIAANVSLGLRQHVVF-------------LDSTG----GFTAS 144
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFvtfeespediiknMASFGwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 145 RLYQMLQARVEDREEqmealqrvQVVRVFDIYEML-RALHEVRdclsqqvesSAGlLKAVLIDSVSAVLSpllggrqseG 223
Cdd:cd19485 81 GKLLILDASPEPSEE--------EVTGEYDLEALLiRIEYAIR---------KIG-AKRVSLDSLEAVFS---------G 133
|
170 180 190
....*....|....*....|....*....|....
gi 1121940426 224 LAIMMQLARELKTLA---KEFSVAVLVTNQVTRD 254
Cdd:cd19485 134 LSDSAVVRAELLRLFawlKQKGVTAIMTGERGED 167
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
105-254 |
1.92e-03 |
|
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: 39.09 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 105 LAGAPGSGKTQVCLSIAAN--VSLGLRQHVVFLDSTGGFTASRLYQML--------QARVEDREEQM-EALQRVQV---V 170
Cdd:cd19483 3 IGAGSGIGKSTIVRELAYHliTEHGEKVGIISLEESVEETAKGLAGKHlgkpepleLPRDDITEEEEdDAFDNELGsgrF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121940426 171 RVFD---------IYEMLRALHEVRDClsqqvessagllKAVLIDSVSAVLSpllGGRQSEGLAIMMQLARELKTLAKEF 241
Cdd:cd19483 83 FLYDhfgsldwdnLKEKIRYMVKVLGC------------KVIVLDHLTILVS---GLDSSDERKELDEIMTELAALVKEL 147
|
170
....*....|...
gi 1121940426 242 SVAVLVTNQVTRD 254
Cdd:cd19483 148 GVTIILVSHLRRP 160
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
82-114 |
7.39e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 37.94 E-value: 7.39e-03
10 20 30
....*....|....*....|....*....|...
gi 1121940426 82 LPTGSPSLDQLLDAGLYTGEVTELAGAPGSGKT 114
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKT 45
|
|
| |
