|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
94-294 |
4.93e-85 |
|
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: 254.87 E-value: 4.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 94 DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSF 173
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 174 DIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLG------GLALMMQLARELKILARDLGVAVVVTNHLT 247
Cdd:cd19489 81 DPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGgskhseGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 485464609 248 RDWDGRRF---KPALGRSWSFVPSTRILLDVTEGAGTlGSSQRTVCLTKS 294
Cdd:cd19489 161 RGGDGGQQgstKPALGEYWESVPSTRLLLSRDENDPE-ESGVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
100-274 |
1.25e-44 |
|
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: 150.58 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 100 GEVTEIVGGPGSGKTQVCLCVAANVAHsLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDifrml 179
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL-LGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 180 DMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGG-----------LALMMQLARELKILARDLGVAVVVTNHLTR 248
Cdd:cd01393 75 TLAHLLALDSLPESLFPPPNTSLVVVDSVSALFRKAFPRggdgdsssslrARLLSQLARALQKLAAQFNLAVVVTNQVTT 154
|
170 180 190
....*....|....*....|....*....|
gi 485464609 249 DWDGR----RFKPALGRSWSFVPSTRILLD 274
Cdd:cd01393 155 KIRGGsgasLVPPALGNTWEHSVSTRLLLY 184
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-295 |
4.68e-27 |
|
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: 105.86 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 90 DKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQART--------QD 156
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkGGLDGGVLYIDTESKFSAERLAEIAEARFpeafsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEKQASALQRIQVVRSFDIFRMLDMLQDLRgtiaqqEATSSGAVKVVIVDSVTAVV-----APLLGGLALMMQLARE--- 228
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLE------EHILSSGVRLVVIDSIAALVrrefgGSDGEVTERHNALAREass 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485464609 229 LKILARDLGVAVVVTNHL-TRDWDGRRF----KPALGRSWSFVPSTRILLDVtegagTLGSSQRTVCLTKSP 295
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQAtTHFGDAGDGssgvTAALGDAWAHAVNTRLRLER-----CLLQLRRVLEIVKSP 221
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-295 |
1.40e-24 |
|
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: 97.68 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 100 GEVTEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGgmtasrllqllqartqdeekqasalqriqvvrSFD 174
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVqipkcFGGLAGEAIYIDTEG--------------------------------SFN 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 175 I--FRMLDMLQdLRGTIAQQEA--TSSGAVKVVIVDSVTAVVAPLLGGLALM----MQLARELKILARDLGVAVVVTNHL 246
Cdd:cd19492 49 IhyFRVHDYVE-LLALINSLPKflEDHPKVKLIVVDSIAFPFRHDFDDLAQRtrllNGLAQLLHSLARQHNLAVVLTNQV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 485464609 247 T---RDWDGRRFKPALGRSWSFVPSTRILLdvtegagTLGSSQRTVCLTKSP 295
Cdd:cd19492 128 TtkiSEDGQSQLVPALGESWSHACTTRLFL-------TWDEKQRFAHLYKSP 172
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
10-300 |
1.60e-24 |
|
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: 100.97 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 10 PGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS----YKALVALRRvlLAQFSAFPlNGADLYEELKTSTAIlSTG 85
Cdd:TIGR02236 5 PGVGPATAEKLREAGYDTFEAIAVASPKELSEIAGISegtaAKIIQAARK--AADLGGFE-TADDVLERRKTIGKI-TTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 86 IGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAH-----SLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKq 160
Cdd:TIGR02236 81 SKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARGLDPDE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 161 asALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssGAVKVVIVDSVTAVVA---PLLGGLALMMQ-LARELKILAR-- 234
Cdd:TIGR02236 160 --VLKNIYVARAYNSNHQMLLVEKAEDLIKELN----NPVKLLIVDSLTSHFRaeyVGRGALAERQQkLNKHLHDLLRla 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 235 DL-GVAVVVTNHLTRDWD---GRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 300
Cdd:TIGR02236 234 DLyNAAVVVTNQVMARPDaffGDPTRPIGGHILGHAATFRVYLRKGKG------DKRIARLVDSPHLPEG 297
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
82-307 |
9.40e-23 |
|
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: 93.92 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLQARTQdeekqa 161
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAA-KQGKKVVYIDTE-GLSPERFQQIAGERFE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SALQRIQVVRSFDIFRMLDMLQDLRGTIaqqeatSSGAVKVVIVDSVTAVV-APLLGGLALMMQLARELKIL---ARDLG 237
Cdd:cd01394 73 SIASNIIVFEPYSFDEQGVAIQEAEKLL------KSDKVDLVVVDSATALYrLELGDDSEANRELSRQMSKLlsiARKYD 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 238 VAVVVTNHLTRDWDGRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTGLQEMIDI 307
Cdd:cd01394 147 IPVVITNQVYSDIDDDRLKPVGGTLLEHWSKAIIRLEKSPP------GLRRATLEKHRSRPEGQSAGFRI 210
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-244 |
2.96e-22 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 94.94 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 10 PGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSYKA----LVALRRVL-LAQFSAfplnGADLYEELKtSTAILST 84
Cdd:PRK04301 12 PGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTaakiIEAAREAAdIGGFET----ALEVLERRK-NVGKITT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 85 GIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEK 159
Cdd:PRK04301 87 GSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVqlpeeKGGLEGKAVYIDTEGTFRPERIEQMAEALGLDPDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 160 qasALQRIQVVRSFDI---FRMLDMLQDLrgtIAQQEatssgAVKVVIVDSVTAVVA---PLLGGLA-----LMMQLARE 228
Cdd:PRK04301 167 ---VLDNIHVARAYNSdhqMLLAEKAEEL---IKEGE-----NIKLVIVDSLTAHFRaeyVGRGNLAerqqkLNKHLHDL 235
|
250
....*....|....*.
gi 485464609 229 LKiLARDLGVAVVVTN 244
Cdd:PRK04301 236 LR-LADLYNAAVVVTN 250
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
82-273 |
9.64e-22 |
|
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: 92.36 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:pfam08423 19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLCVTCQLPLEMgggEGKALYIDTEGTFRPERLVAIAERYGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGL----ALMMQLARELKIL 232
Cdd:pfam08423 99 PE---DVLDNVAYARAYNSEHQMQLLQQAAAMMSESR------FALLIVDSATALYRTDFSGRgelaERQQHLAKFLRTL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 485464609 233 AR---DLGVAVVVTNHLTRDWDGRRF-------KPALGRSWSFVPSTRILL 273
Cdd:pfam08423 170 QRladEFGVAVVITNQVVAQVDGAAGmfsgdpkKPIGGHIMAHASTTRLSL 220
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
82-264 |
2.31e-21 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 90.31 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLqartqdEEKQA 161
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAA-KNGKKVIYIDTE-GLSPERFKQIA------GEDFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SALQRIQVVRSFDiFRMLDM-LQDLRGTIAQQeatssgaVKVVIVDSVTAVV-APLLG---GLALMMQLARELKIL---A 233
Cdd:PRK09361 77 ELLSNIIIFEPSS-FEEQSEaIRKAEKLAKEN-------VGLIVLDSATSLYrLELEDeedNSKLNRELGRQLTHLlklA 148
|
170 180 190
....*....|....*....|....*....|....
gi 485464609 234 RDLGVAVVVTNHLTRDWDGRRFKPALGRS---WS 264
Cdd:PRK09361 149 RKHDLAVVITNQVYSDIDSDGLRPLGGHTlehWS 182
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
89-295 |
1.83e-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: 88.50 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 89 LDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQ--ARTQDEEKQA 161
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLClqLALTVQLPRElggLGGGAVYICTESSFPSKRLQQLASslPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SALQRIQVVRSFDifrmldmLQDLRGTIAQQ--EATSSGAVKVVIVDSVTAVV----APLLGGLA----LMMQLARELKI 231
Cdd:cd19491 81 NFLDNIFVEHVAD-------LETLEHCLNYQlpALLERGPIRLVVIDSIAALFrsefDTSRSDLVerakYLRRLADHLKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 232 LARDLGVAVVVTNHLTRDWD-------------------------GRRFKPALGRSWSFVPSTRILLDVTEGAGTLGSSQ 286
Cdd:cd19491 154 LADKYNLAVVVVNQVTDRFDsssdasglgvldylsqfssfsggvsGNRKVPALGLTWANLVNTRLMLSRTPKRITDSSAA 233
|
250
....*....|...
gi 485464609 287 ----RTVCLTKSP 295
Cdd:cd19491 234 sisvRRLEVVFSP 246
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
82-300 |
7.65e-19 |
|
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: 83.95 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQlppeeGGLNGKAVYIDTENTFRPERIMQMAKALGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEKqasALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgAVKVVIVDSVTAVVA---PLLGGLALMMQ-LARELKIL 232
Cdd:cd19515 81 PDE---VLDNIYVARAYNSNHQMLLVEKAEDLIKEGN-----NIKLLIVDSLTSHFRaeyVGRGTLAERQQkLNKHLHDL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485464609 233 AR--DL-GVAVVVTNHLTRDWD---GRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 300
Cdd:cd19515 153 HRlaDLyNIAVLVTNQVMAKPDaffGDPTQAIGGHILGHAATFRVYLRKGKG------GKRIARLVDSPHLPEG 220
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
11-273 |
1.12e-18 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 85.17 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS-YKALvalrRVLLAQFSAFPL---NGADLYEElKTSTAILSTGI 86
Cdd:PLN03186 35 GIAALDIKKLKDAGIHTVESLAYAPKKDLLQIKGISeAKVE----KILEAASKLVPLgftTASQLHAQ-RQEIIQITTGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVahSLQQ-----NVLYVDSNGGMTASRLLQLLQARTQDeek 159
Cdd:PLN03186 110 RELDKILEGGIETGSITEIYGEFRTGKTQLChtLCVTCQL--PLDQgggegKAMYIDTEGTFRPQRLIQIAERFGLN--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 160 QASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGG----LALMMQLARELKILAR- 234
Cdd:PLN03186 185 GADVLENVAYARAYNTDHQSELLLEAASMMAETR------FALMIVDSATALYRTEFSGrgelSARQMHLGKFLRSLQRl 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 485464609 235 --DLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILL 273
Cdd:PLN03186 259 adEFGVAVVITNQVVAQVDGSAFfagpqlKPIGGNIMAHASTTRLAL 305
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
82-300 |
7.97e-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: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLChtLAVTCQLPIDrggGEGKAIYIDTEGTFRPERLRAIAQRFGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGG----LALMMQLARELKIL 232
Cdd:cd01123 81 PD---DVLDNVAYARAFNSDHQTQLLDQAAAMMVESR------FKLLIVDSATALYRTDYSGrgelSARQMHLAKFLRML 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485464609 233 AR---DLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 300
Cdd:cd01123 152 QRladEFGVAVVVTNQVVAQVDGAMMfaadpkKPIGGNILAHASTTRLYLRKGRG------ETRICKIYDSPCLPEA 222
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
82-252 |
1.79e-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: 77.36 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGG----LALMMQLARELKIL 232
Cdd:cd19513 81 GE---DVLDNVAYARAYNTDHQMQLLIQASAMMAESR------YALLIVDSATALYRTDYSGrgelSARQMHLAKFLRML 151
|
170 180
....*....|....*....|...
gi 485464609 233 AR---DLGVAVVVTNHLTRDWDG 252
Cdd:cd19513 152 QRladEFGVAVVITNQVVAQVDG 174
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
11-252 |
7.66e-16 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 76.96 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSY----KALVALRRVLLAQFsafpLNGADLYEeLKTSTAILSTGI 86
Cdd:PTZ00035 30 GINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEakveKIKEAASKLVPMGF----ISATEYLE-ARKNIIRITTGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQQN---VLYVDSNGGMTASRLLQLLQARTQDEEkqa 161
Cdd:PTZ00035 105 TQLDKLLGGGIETGSITELFGEFRTGKTQLChtLCVTCQLPIEQGGGegkVLYIDTEGTFRPERIVQIAERFGLDPE--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAvvapLL-------GGLA-LMMQLARELKILA 233
Cdd:PTZ00035 182 DVLDNIAYARAYNHEHQMQLLSQAAAKMAEER------FALLIVDSATA----LFrvdysgrGELAeRQQHLGKFLRALQ 251
|
250 260
....*....|....*....|..
gi 485464609 234 R---DLGVAVVVTNHLTRDWDG 252
Cdd:PTZ00035 252 KladEFNVAVVITNQVMADVDG 273
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
11-252 |
1.89e-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: 75.53 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS-YKAlvalRRVLLAQFSAFPLN--GADLYEELKTSTAILSTGIG 87
Cdd:TIGR02239 8 GITAADIKKLQEAGLHTVESVAYAPKKQLLEIKGISeAKA----DKILAEAAKLVPMGftTATEFHQRRQEVIQLTTGSK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 88 SLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQDEEKqas 162
Cdd:TIGR02239 84 ELDKLLGGGIETGSITEIFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLNPED--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 163 ALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATssgavkVVIVDSVTAVVAPLLGG----LALMMQLA---RELKILARD 235
Cdd:TIGR02239 161 VLDNVAYARAYNTDHQLQLLQQAAAMMSESRFA------LLIVDSATALYRTDFSGrgelSARQMHLArflRSLQRLADE 234
|
250
....*....|....*..
gi 485464609 236 LGVAVVVTNHLTRDWDG 252
Cdd:TIGR02239 235 FGVAVVITNQVVAQVDG 251
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
100-273 |
5.76e-15 |
|
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: 72.77 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 100 GEVTEIVGGPGSGKTQVCLCVAAN----------VAHSLQQNVLYVDSNGGMTASRLLQLLQAR--------------TQ 155
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggvPLGGLEAAVVFIDTDGRFDILRLRSILEARiraaiqaanssddeED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 156 DEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEAtsSGAVKVVIVDSVTA-----------VVAPLLGGLALMMQ 224
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSLSA--NPELGLLLIDSISAfywqdrfsaelARAAPLLQEAALRA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485464609 225 LARELKILARDLGVAVVVTNHL---TRDWDGRR--------------FKPALGRSWSFVPSTRILL 273
Cdd:cd19490 159 ILRELRRLRRRFQLVVIATKQAlfpGKSASTDNpaannavskasapsHREYLPRPWQRLVTHRLVL 224
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
82-298 |
3.66e-12 |
|
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: 65.07 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLShtLCVTAQLPGSMgggGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 eekQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQqeatsSGAVKVVIVDSVTA---VVAPLLGGLALMMQ-LARELKIL 232
Cdd:cd19514 81 ---HDAVLDNILYARAYTSEHQMELLDYVAAKFHE-----EAVFRLLIIDSIMAlfrVDFSGRGELAERQQkLAQMLSRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485464609 233 ---ARDLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILLdvTEGAGtlgsSQRTVCLTKSPRQP 298
Cdd:cd19514 153 qkiSEEYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISL--RKGRG----EERIAKIYDSPDLP 221
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
82-247 |
5.37e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 61.47 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSlQQNVLYVDSNggMTASRLLQLLQARTQDEEKQA 161
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRR-GEKGLYVSFE--ESPEQLLRRAESLGLDLEEYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SAlQRIQVVRSFDIFRMLD---MLQDLRGTIAQQEAtssgavKVVIVDSVTAVVAPLLGGLALMMQLaRELKILARDLGV 238
Cdd:COG0467 79 ES-GLLRIIDLSPEELGLDleeLLARLREAVEEFGA------KRVVIDSLSGLLLALPDPERLREFL-HRLLRYLKKRGV 150
|
....*....
gi 485464609 239 AVVVTNHLT 247
Cdd:COG0467 151 TTLLTSETG 159
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
68-273 |
1.90e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 60.95 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 68 GADLYEELKTSTAIlSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQ---QNVLYVDSNGGMT 142
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAhtLCVTTQLPTEMGggnGKVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 143 ASRLLQLLQARTQDEEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQeatssgAVKVVIVDSVTA---VVAPLLGGL 219
Cdd:PLN03187 174 PDRIVPIAERFGMDAD---AVLDNIIYARAYTYEHQYNLLLGLAAKMAEE------PFRLLIVDSVIAlfrVDFTGRGEL 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485464609 220 ALMMQ-----LARELKIlARDLGVAVVVTNHLTRDWDGRRF-----KPALGRSWSFVPSTRILL 273
Cdd:PLN03187 245 AERQQklaqmLSRLTKI-AEEFNVAVYMTNQVIADPGGGMFisdpkKPAGGHVLAHAATIRLML 307
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
82-298 |
1.79e-09 |
|
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: 57.87 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:TIGR02238 78 ITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLShtLCVTAQLPREMgggNGKVAYIDTEGTFRPDRIRAIAERFGVD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLrgtiaqQEATSSGAVKVVIVDSVTA---VVAPLLGGLALMMQ-LARELKIL 232
Cdd:TIGR02238 158 PD---AVLDNILYARAYTSEHQMELLDYL------AAKFSEEPFRLLIVDSIMAlfrVDFSGRGELSERQQkLAQMLSRL 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485464609 233 ---ARDLGVAVVVTNHLTRD--------WDGRrfKPALGRSWSFVPSTRILLdvTEGAGtlgsSQRTVCLTKSPRQP 298
Cdd:TIGR02238 229 nkiSEEFNVAVFVTNQVQADpgatmtfiADPK--KPIGGHVLAHASTTRILL--RKGRG----EERVAKLYDSPDMP 297
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
82-232 |
1.84e-07 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 51.09 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------DSNGGMTA----------S 144
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALKYGEPGVFVtleeppeDLRENARSfgwdlekleeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 145 RLLQLLQARTQDEEkqasalqRIQVVRSFDIFRMLDMLqdlrgtiaqQEATSSGAVKVVIVDSVTAVVAPLLGGLA--LM 222
Cdd:pfam06745 81 GKLAIIDASTSGIG-------IAEVEDRFDLEELIERL---------REAIREIGAKRVVIDSITTLFYLLKPAVAreIL 144
|
170
....*....|
gi 485464609 223 MQLARELKIL 232
Cdd:pfam06745 145 RRLKRVLKGL 154
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
82-253 |
1.94e-07 |
|
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: 51.36 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYVDSNggMTASRLLQ-LLQARTQDEek 159
Cdd:cd00984 2 LPTGFTDLDKLT-GGLQPGDLI-IIAArPSMGKTAFALNIAENIALDEGLPVLFFSLE--MSAEQLAErLLSSESGVS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 160 qasaLQRIQVVRSFD-----IFRMLDMLQDL--------RGTIAQQEATS------SGAVKVVIVDSVTAVVAPllgGLA 220
Cdd:cd00984 76 ----LSKLRTGRLDDedwerLTAAMGELSELplyiddtpGLTVDEIRAKArrlkreHGGLGLIVIDYLQLIRGS---KRA 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 485464609 221 LMMQLA-----RELKILARDLGVAVVVTNHLTRDWDGR 253
Cdd:cd00984 149 ENRQQEvaeisRSLKALAKELNVPVIALSQLNRGVESR 186
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
97-299 |
2.07e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 51.83 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 97 LYTGEVTEIVGGPGSGKTQVCLCVAANVAHSL--------QQNVLYVDSNGGMTA--SRLLQLLQARTQDEEKQASalqR 166
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGpwlgrrvpPGKVLYLAAEDDRGElrRRLKALGADLGLPFADLDG---R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 167 IQVVRSFDIFRMLDMLQDLRGTIAQqeatssGAVKVVIVDSVTAVVApllGGL---ALMMQLARELKILARDLGVAVVVT 243
Cdd:COG3598 87 LRLLSLAGDLDDTDDLEALERAIEE------EGPDLVVIDPLARVFG---GDEndaEEMRAFLNPLDRLAERTGAAVLLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 485464609 244 NHLT-RDWDGRRFKPALG-RSWSFVPSTRILLDVTEGAGTlgssqRTVCLTKSPRQPT 299
Cdd:COG3598 158 HHTGkGGAGKDSGDRARGsSALRGAARSVLVLSREKGEDL-----RVLTRAKSNYGPE 210
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
100-249 |
2.67e-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: 50.07 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 100 GEVTEIVGGPGSGKTQVCLCVAANVA----------HSLQQNVLYVDSNGG--MTASRLLQLLQARTQDEEkqasaLQRI 167
Cdd:pfam13481 33 GGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprVPEQGKVLYVSAEGPadELRRRLRAAGADLDLPAR-----LLFL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 168 QVVRSFDIFRMLDMLQDLRGTIAQ--QEATSSGAVKVVIVDSVTAVVAPLLGGLALMMQLARELKILARDLGVAVVVTNH 245
Cdd:pfam13481 108 SLVESLPLFFLDRGGPLLDADVDAleAALEEVEDPDLVVIDPLARALGGDENSNSDVGRLVKALDRLARRTGATVLLVHH 187
|
....
gi 485464609 246 LTRD 249
Cdd:pfam13481 188 VGKD 191
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
83-246 |
3.18e-07 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 51.32 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 83 STGIGSLDKLL-DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVahslQQN---VLYVDSNG----------GMTASRLLq 148
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA----QKAggiAAFIDAEHaldpeyakklGVDIDNLL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 149 LLQARTQDeekQAsalqriqvvrsFDIfrmLDMLqdlrgtiaqqeaTSSGAVKVVIVDSVTAVV--APLLG-------GL 219
Cdd:COG0468 120 VSQPDTGE---QA-----------LEI---AETL------------VRSGAVDLIVVDSVAALVpkAEIEGemgdshvGL 170
|
170 180
....*....|....*....|....*....
gi 485464609 220 A--LMMQLARELKILARDLGVAVVVTNHL 246
Cdd:COG0468 171 QarLMSQALRKLTGAISKSNTTVIFINQL 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-261 |
6.24e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 99 TGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDsnggMTASRLLQLLQARTQDEEKQASALQRIQVVRsfdifRM 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYID----GEDILEEVLDQLLLIIVGGKKASGSGELRLR-----LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 179 LDMLQDLRgtiaqqeatssgaVKVVIVDSVTAVVAPLLGGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGRRFKPA 258
Cdd:smart00382 71 LALARKLK-------------PDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
...
gi 485464609 259 LGR 261
Cdd:smart00382 138 FDR 140
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
82-249 |
7.93e-07 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 49.45 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYV---DSNG--GMTASRllqlLQARTQD 156
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLA-QRGGKVLYVsgeESLSqiKLRAER----LGLGSDN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 157 eekqasalqrIQVVRSFDIFRMLDMLQDLRgtiaqqeatssgaVKVVIVDSVTAVVAPLLGGL-----------ALMMQL 225
Cdd:cd01121 139 ----------LYLLAETNLEAILAEIEELK-------------PSLVVIDSIQTVYSPELTSSpgsvsqvrecaAELLRL 195
|
170 180
....*....|....*....|....
gi 485464609 226 ARElkilardLGVAVVVTNHLTRD 249
Cdd:cd01121 196 AKE-------TGIPVFLVGHVTKD 212
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
82-289 |
2.76e-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: 47.64 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVdsngGM--TASRLLQllQART--QDE 157
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGA-KNGEPGLFF----TFeeSPERLLR--NAKSfgWDF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 158 EKQASALqRIQVVRSFDIFRMLDMLQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLGGLAL---MMQLARELkilaR 234
Cdd:cd01124 74 DEMEDEG-KLIIVDAPPTEAGRFSLDELLSRILS--IIKSFKAKRVVIDSLSGLRRAKEDQMRArriVIALLNEL----R 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 485464609 235 DLGVAVVVTNHLTrdwDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLgssQRTV 289
Cdd:cd01124 147 AAGVTTIFTSEMR---SFLSSESAGGGDVSFIVDGVILLRYVEIEGEL---RRTI 195
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
82-249 |
3.92e-06 |
|
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: 46.98 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 144
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFVtfeespediiknmASFGwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 145 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLdmlqdLRGTIAQQeatSSGAVKVVIvDSVTAVvaplLGGLALMMQ 224
Cdd:cd19485 81 GKLLILDASPEPSE--------EEVTGEYDLEALL-----IRIEYAIR---KIGAKRVSL-DSLEAV----FSGLSDSAV 139
|
170 180
....*....|....*....|....*...
gi 485464609 225 LARELKILA---RDLGVAVVVTNHLTRD 249
Cdd:cd19485 140 VRAELLRLFawlKQKGVTAIMTGERGED 167
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
82-244 |
8.46e-06 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 46.14 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGgmtasrlLQLLQARTqdeEKQA 161
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDES-------IGTLFERS---EALG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 162 SALQRIQVVRSFDIfRMLDMLQDLRGTIAQQEATS--SGAVKVVIVDSVTAVVAPLLGGLALMMQLARELKILARdLGVA 239
Cdd:cd19487 71 IDLRAMVEKGLLSI-EQIDPAELSPGEFAQRVRTSveQEDARVVVIDSLNGYLNAMPDERFLILQMHELLSYLNN-QGVT 148
|
....*
gi 485464609 240 VVVTN 244
Cdd:cd19487 149 TLLIV 153
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
105-254 |
9.53e-06 |
|
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: 46.02 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 105 IVGGPGSGKTQVCLCVAANVAHSLQQNVLYV---DSNGgMTASRLL-----------QLLQARTQDEEKQA-SALQRIQV 169
Cdd:cd19483 3 IGAGSGIGKSTIVRELAYHLITEHGEKVGIIsleESVE-ETAKGLAgkhlgkpepleLPRDDITEEEEDDAfDNELGSGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 170 VRSFDIFRMLDMlQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLGGLALMMQ--LARELKILARDLGVAVVVTNHLT 247
Cdd:cd19483 82 FFLYDHFGSLDW-DNLKEKIRY--MVKVLGCKVIVLDHLTILVSGLDSSDERKELdeIMTELAALVKELGVTIILVSHLR 158
|
....*..
gi 485464609 248 RDWDGRR 254
Cdd:cd19483 159 RPGGGKG 165
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
82-243 |
7.38e-05 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 44.10 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 144
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQFLVNGIKRFDEPGVFVtfeespediirnvASFGwdlqKLIDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 145 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLDMLQDlrgtiAQQeatSSGAVKVVIvDSVTAvvapLLGGLALMMQ 224
Cdd:PRK09302 93 GKLFILDASPDPSE--------QEEAGEYDLEALFIRIEY-----AID---KIGAKRVVL-DSIEA----LFSGFSNEAV 151
|
170 180
....*....|....*....|..
gi 485464609 225 LARELKILA---RDLGVAVVVT 243
Cdd:PRK09302 152 VRRELRRLFawlKQKGVTAVIT 173
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-246 |
1.82e-04 |
|
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: 42.16 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 82 LSTGIGSLDKLLDAGLY-TGEVTEIVGGPGSGKTQVCLCVAANvAHSLQQNVLYVDSNGGMT---ASRL------LQLLQ 151
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAE-AQKLGGTAAFIDAEHALDpeyAKKLgvdidnLLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 152 ARTQDEekqasalqriqvvrsfdifrMLDMLQDLrgtiaqqeaTSSGAVKVVIVDSVTAVV--APLLGGL---------A 220
Cdd:cd00983 84 PDTGEQ--------------------ALEIADTL---------IRSGAVDLIVVDSVAALVpkAEIEGEMgdshvglqaR 134
|
170 180
....*....|....*....|....*.
gi 485464609 221 LMMQLARELKILARDLGVAVVVTNHL 246
Cdd:cd00983 135 LMSQALRKLTGSLSKSKTTVIFINQL 160
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
100-281 |
1.27e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 39.67 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 100 GEVTEIVGGPGSGKTQVCLCVAANVA--------HSLQQ-NVLYVDSNGGmtASRLLQLLQARTQDEEKQASALQRIQVV 170
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVAtgrdwlgeRRVKQgRVVYLAAEDP--RDGLRRRLKAIGAHLGDEDAALAENLVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464609 171 RSFDIFRMLDmlqDLRGTIAQQEATSSGAVKVVIVDSVTAVvaplLGGL-----ALMMQLARELKILARDLGVAVVVTNH 245
Cdd:cd01125 79 ENLRGKPVSI---DAEAPELERIIEELEGVRLIIIDTLARV----LHGGdendaADMGAFVAGLDRIARETGAAVLLVHH 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 485464609 246 LTRDWDGRRFKPALGRSwSFVPSTRILLDVTEGAGT 281
Cdd:cd01125 152 TGKDAAGDSQQAARGSS-ALRGAADAEINLSKMDAT 186
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
82-135 |
1.46e-03 |
|
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: 39.71 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 485464609 82 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYV 135
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLI-IIAArPSMGKTAFALNIARNAAVKHKKPVAIF 54
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-114 |
1.57e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 39.86 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 485464609 61 FSAFPLNGADLyeELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKT 114
Cdd:PRK09302 236 ISVLPLTAMRL--TQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKT 287
|
|
| |
